ID   UBR5_RAT                Reviewed;        2788 AA.
AC   Q62671; F1LRS0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 3.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=E3 ubiquitin-protein ligase UBR5;
DE            EC=2.3.2.26;
DE   AltName: Full=100 kDa protein;
DE   AltName: Full=E3 ubiquitin-protein ligase, HECT domain-containing 1;
DE   AltName: Full=HECT-type E3 ubiquitin transferase UBR5;
DE   AltName: Full=Hyperplastic discs protein homolog;
GN   Name=Ubr5; Synonyms=Dd5, Edd, Edd1, Hyd;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1868-2788.
RC   STRAIN=Wistar; TISSUE=Testis;
RX   PubMed=1533713; DOI=10.1093/nar/20.7.1471;
RA   Mueller D., Rehbein M., Baumeister H., Richter D.;
RT   "Molecular characterization of a novel rat protein structurally related to
RT   poly(A) binding proteins and the 70K protein of the U1 small nuclear
RT   ribonucleoprotein particle (snRNP).";
RL   Nucleic Acids Res. 20:1471-1475(1992).
RN   [3]
RP   ERRATUM OF PUBMED:1533713.
RA   Mueller D., Rehbein M., Baumeister H., Richter D.;
RL   Nucleic Acids Res. 20:2624-2624(1992).
RN   [4]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFT.
RX   PubMed=10030672; DOI=10.1038/sj.onc.1202249;
RA   Callaghan M.J., Russell A.J., Woollatt E., Sutherland G.R.,
RA   Sutherland R.L., Watts C.K.W.;
RT   "Identification of a human HECT family protein with homology to the
RT   Drosophila tumor suppressor gene hyperplastic discs.";
RL   Oncogene 17:3479-3491(1998).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12239083; DOI=10.1210/en.2002-220262;
RA   Oughtred R., Bedard N., Adegoke O.A.J., Morales C.R., Trasler J.,
RA   Rajapurohitam V., Wing S.S.;
RT   "Characterization of rat100, a 300-kilodalton ubiquitin-protein ligase
RT   induced in germ cells of the rat testis and similar to the Drosophila
RT   hyperplastic discs gene.";
RL   Endocrinology 143:3740-3747(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2231 AND SER-2475, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end
CC       rule pathway. Recognizes and binds to proteins bearing specific N-
CC       terminal residues that are destabilizing according to the N-end rule,
CC       leading to their ubiquitination and subsequent degradation (By
CC       similarity). Involved in maturation and/or transcriptional regulation
CC       of mRNA by activating CDK9 by polyubiquitination. May play a role in
CC       control of cell cycle progression. May have tumor suppressor function.
CC       Regulates DNA topoisomerase II binding protein (TopBP1) for the DNA
CC       damage response. Plays an essential role in extraembryonic development.
CC       Ubiquitinates acetylated PCK1. Also acts as a regulator of DNA damage
CC       response by acting as a suppressor of RNF168, an E3 ubiquitin-protein
CC       ligase that promotes accumulation of 'Lys-63'-linked histone H2A and
CC       H2AX at DNA damage sites, thereby acting as a guard against excessive
CC       spreading of ubiquitinated chromatin at damaged chromosomes (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Binds TOPBP1. Associates with CDK9 and TFIIS/TCEA1 and forms a
CC       transcription regulatory complex made of CDK9, RNAP II, UBR5 and
CC       TFIIS/TCEA1 that can stimulate target gene transcription by recruiting
CC       their promoters. Interacts with PIH1D1. {ECO:0000250|UniProtKB:O95071}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highest levels found in testis. Also present in
CC       liver, kidney, lung and brain. {ECO:0000269|PubMed:12239083}.
CC   -!- DEVELOPMENTAL STAGE: In early postnatal life, expression in the testis
CC       increases to reach a maximum around day 28.
CC       {ECO:0000269|PubMed:12239083}.
CC   -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-thioester
CC       formation.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA45756.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X64411; CAA45756.1; ALT_FRAME; mRNA.
DR   PIR; S22659; S22659.
DR   PDB; 3NTW; X-ray; 2.60 A; A/C=2383-2442.
DR   PDBsum; 3NTW; -.
DR   SMR; Q62671; -.
DR   ELM; Q62671; -.
DR   IntAct; Q62671; 1.
DR   STRING; 10116.ENSRNOP00000009115; -.
DR   iPTMnet; Q62671; -.
DR   PhosphoSitePlus; Q62671; -.
DR   jPOST; Q62671; -.
DR   PaxDb; Q62671; -.
DR   UCSC; RGD:621236; rat.
DR   RGD; 621236; Ubr5.
DR   eggNOG; KOG0943; Eukaryota.
DR   InParanoid; Q62671; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q62671; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:RGD.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:2000780; P:negative regulation of double-strand break repair; ISS:UniProtKB.
DR   GO; GO:1901315; P:negative regulation of histone H2A K63-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0032700; P:negative regulation of interleukin-17 production; ISO:RGD.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:RGD.
DR   GO; GO:0050847; P:progesterone receptor signaling pathway; ISO:RGD.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:RGD.
DR   GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:RGD.
DR   GO; GO:2000779; P:regulation of double-strand break repair; IBA:GO_Central.
DR   GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR   CDD; cd14423; CUE_UBR5; 1.
DR   Gene3D; 2.130.10.30; -; 1.
DR   InterPro; IPR024725; E3_UbLigase_EDD_UBA.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR036053; PABP-dom.
DR   InterPro; IPR002004; PABP_HYD.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR003126; Znf_UBR.
DR   Pfam; PF11547; E3_UbLigase_EDD; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00658; PABP; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF50985; SSF50985; 1.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   SUPFAM; SSF63570; SSF63570; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS51309; PABC; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA damage; DNA repair; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..2788
FT                   /note="E3 ubiquitin-protein ligase UBR5"
FT                   /id="PRO_0000086933"
FT   DOMAIN          2367..2444
FT                   /note="PABC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT   DOMAIN          2451..2788
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   ZN_FING         1166..1234
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT   REGION          68..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          988..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1041..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1288..1308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1504..1729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1848..1881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1974..2011
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2106..2132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2313..2383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2463..2490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..591
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1020
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1061
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1510..1540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1552..1566
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1567..1597
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1611..1640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1649..1674
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1682..1729
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1865..1881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1986..2004
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2319..2360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2463..2480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2757
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         317
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         567
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         601
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         626
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         797
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         917
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1007
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1104
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1124
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1297
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1364
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1470
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1725
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1730
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1735
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1769
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1959
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         1980
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         2016
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         2018
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         2020
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         2066
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         2203
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         2231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         2279
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         2459
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         2473
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95071"
FT   MOD_RES         2475
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CONFLICT        1890
FT                   /note="Missing (in Ref. 2; CAA45756)"
FT                   /evidence="ECO:0000305"
FT   HELIX           2383..2396
FT                   /evidence="ECO:0007829|PDB:3NTW"
FT   HELIX           2400..2402
FT                   /evidence="ECO:0007829|PDB:3NTW"
FT   HELIX           2403..2410
FT                   /evidence="ECO:0007829|PDB:3NTW"
FT   HELIX           2415..2423
FT                   /evidence="ECO:0007829|PDB:3NTW"
FT   HELIX           2425..2439
FT                   /evidence="ECO:0007829|PDB:3NTW"
SQ   SEQUENCE   2788 AA;  308027 MW;  C2EA68B962627231 CRC64;
     MNKQAVKRLH MLREVSEKLN KYNLNSHPPL NVLEQATIKQ CVVGPNHAAF LLEDGRICRI
     GFSVQPDRLE LGKPDNNDGS KLNSSSGTGR TSRPGRTSDS PWFLSGSETL GRLAGNTLGS
     RWSSGVGGSG GGSSGRSSAG ARDSRRQTRV IRTGRDRGSG LLGSQPQPVI PASVIPEELI
     SQAQVVLQGK SRSVIIRELQ RTNLDVNLAV NNLLSRDDED GDDGDDTASE SYLPGEDLMS
     LLDADIHSAH PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRVLLLP LERDSELLRE
     RESVLRLRER RWLDGASFDN ERGSTSKEGE PNPDKKNTPV QSPVSLGEDL QWWPDKDGTK
     FTCIGALYSE LVAVSSKGEL YQWKWTESEP YRNAQNPSLH HPRATFLGLT NEKIVLLSAN
     SIRATVATEN NKVATWVDET LSSVASKLEH TAQTYSELQG ERIVSLHCCA LYTCAQLENN
     LYWWGVVPFS QRKKMLEKAR AKNKKPKSSA GVQSLNVRGG RQVCLRNNPL YHAGAVAFSI
     SAGIPKVGVL MESVWNMNDS CRFQLRSPES LKSMEKASKT IETKPESKQE PVKTEMGPPP
     SPASTCSDAS SIASSASMPY KRRRSTPAPK EEEKVNEEQW SLREVVFVED VKNVPVGKVL
     KVDGAYVAVK FPGTSSNTNC QNSSGPDADP SSLLQDCRLL RIDELQVVKT GGTPKVPDCF
     QRTPKKLCIP EKTEILAVNV DSKGVHAVLK TGNWVRYCIF DLATGKAEQE NNFPTSSVAF
     LGQNERSVAI FTAGQESPII LRDGNGTIYP MAKDCMGGIR DPDWLDLPPI SSLGMGVHSL
     INLPANSTIK KKAAIIIMAV EKQTLMQHIL RCDYEACRQY LVNLEQAVVL EQNLQMLQTF
     ISHRCDGNRN ILHACVSVCF PTSNKETKEE EEAERSERNT FAERLSAVEA IANAISVVSS
     NGPGNRAGSS SSRSLRLREM MRRSLRAAGL GRHEAGASSS DHQDPVSPPI APPSWVPDPP
     SMDPDGDIDF ILAPAVGSLT TAATGGGQGP STSTIPGPST EPSVVESKDR KANAHFILKL
     LCDSAVLQPY LRELLSAKDA RGMTPFMSAV SGRAYPAAIT ILETAQKIAK AEVSGSEKEE
     DVFMGMVCPS GTNPDDSPLY VLCCNDTCSF TWTGAEHINQ DIFECRTCGL LESLCCCTEC
     ARVCHKGHDC KLKRTSPTAY CDCWEKCKCK TLIAGQKSAR LDLLYRLLTA TNLVTLPNSR
     GEHLLLFLVQ TVARQTVEHC QYRPPRIRED RNRKTASPDD SDMPDHDLEP PRFAQLALER
     VLQDWNALRS MIMFGSQENK DPLSASSRIG HLLPEEQVYL NQQSGTIRLD CFTHCLIVKC
     TADILLLDTL LGTLVKELQN KYTPGRREEA IAVTMRFLRS VARVFVILSV EMASSKKKNN
     FIPQPIGKCK RVFQALLPYA VEELCNVAES LIVPVRMGIA RPTAPFTLAS TSIDAMQGSE
     ELFSVEPLPP RPSSDQSSSS SQSQSSYIIR NPQQRRISQS QPVRGREEEQ DDIVSADVEE
     VEVVEGVAGE EDHHDEQEEH GEENAEAEGH HDEHDEDGSD MELDLLAAAE TESDSESNHS
     NQDNASGRRS VVTAATAGSE AGASSVPAFF SEDDSQSNDS SDSDSSSSQS DDIEQETFML
     DEPLERTTNS SHANGAAQAP RSMQWAVRNT QHQRAASTAP SSTSTPAASS AGLIYIDPSN
     LRRSGTISTS AAAAAAALEA SNASSYLTSA SSLARAYSIV IRQISDLMGL IPKYNHLVYS
     QIPAAVKLTY QDAVNLQNYV EEKLIPTWNW MVSIMDSTEA QLRYGSALAS AGDPGHPNHP
     LHASQNSARR ERMTAREEAS LRTLEGRRRR ATLLSARQGM MSARGDFLNY ALSLMRSHND
     EHSDVLPVLD VCSLKHVAYV FQALIYWIKA MNQQTTLDTP QLERKRTREL LELGIDNEDS
     EHENDDDTSQ SATLNDKDDE SLPAETGQNH PFFRRSDSMT FLGCIPPNPF EVPLAEAIPL
     ADQPHLLQPN ARKEDLFGRP SQGLYSSSAG SGKCLVEVTM DRNCLEVLPT KMSYAANLKN
     VMNMQNRQKK AGEDQSMLAE EADSSKPGPS AHDVAAQLKS SLLAEIGLTE SEGPPLTSFR
     PQCSFMGMVI SHDMLLGRWR LSLELFGRVF MEDVGAEPGS ILTELGGFEV KESKFRREME
     KLRNQQSRDL SLEVDRDRDL LIQQTMRQLN NHFGRRCATT PMAVHRVKVT FKDEPGEGSG
     VARSFYTAIA QAFLSNEKLP NLDCIQNANK GTHTSLMQRL RNRGERDRER EREREMRRSS
     GLRAGSRRDR DRDFRRQLSI DTRPFRPASE GNPSDDPDPL PAHRQALGER LYPRVQAMQP
     AFASKITGML LELSPAQLLL LLASEDSLRA RVEEAMELIV AHGRENGADS ILDLGLLDSS
     EKVQENRKRH GSSRSVVDMD LDDTDDGDDN APLFYQPGKR GFYTPRPGKN TEARLNCFRN
     IGRILGLCLL QNELCPITLN RHVIKVLLGR KVNWHDFAFF DPVMYESLRQ LILASQSSDA
     DAVFSAMDLA FAVDLCKEEG GGQVELIPNG VNIPVTPQNV YEYVRKYAEH RMLVVAEQPL
     HAMRKGLLDV LPKNSLEDLT AEDFRLLVNG CGEVNVQMLI SFTSFNDESG ENAEKLLQFK
     RWFWSIVERM SMTERQDLVY FWTSSPSLPA SEEGFQPMPS ITIRPPDDQH LPTANTCISR
     LYVPLYSSKQ ILKQKLLLAI KTKNFGFV
//
