PRGR_MOUSE
ID PRGR_MOUSE Reviewed; 926 AA.
AC Q00175; A6H6A5; E9QPW3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Progesterone receptor;
DE Short=PR;
DE AltName: Full=Nuclear receptor subfamily 3 group C member 3;
GN Name=Pgr; Synonyms=Nr3c3, Pr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RX PubMed=2069958; DOI=10.1021/bi00242a029;
RA Schott D.R., Shyamala G., Schneider W., Parry G.;
RT "Molecular cloning, sequence analyses, and expression of complementary DNA
RT encoding murine progesterone receptor.";
RL Biochemistry 30:7014-7020(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Brain;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC STRAIN=129/Sv;
RX PubMed=7802637; DOI=10.1006/bbrc.1994.2778;
RA Hagihara K., Wu-Peng X.S., Funabashi T., Kato J., Pfaff D.W.;
RT "Nucleic acid sequence and DNase hypersensitive sites of the 5' region of
RT the mouse progesterone receptor gene.";
RL Biochem. Biophys. Res. Commun. 205:1093-1101(1994).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=8603049; DOI=10.1016/0960-0760(95)00254-5;
RA Lydon J.P., DeMayo F.J., Conneely O.M., O'Malley B.W.;
RT "Reproductive phenotpes of the progesterone receptor null mutant mouse.";
RL J. Steroid Biochem. Mol. Biol. 56:67-77(1996).
RN [7]
RP FUNCTION (ISOFORM B), AND DISRUPTION PHENOTYPE (ISOFORMS A AND B).
RX PubMed=10976068; DOI=10.1126/science.289.5485.1751;
RA Mulac-Jericevic B., Mullinax R.A., DeMayo F.J., Lydon J.P., Conneely O.M.;
RT "Subgroup of reproductive functions of progesterone mediated by
RT progesterone receptor-B isoform.";
RL Science 289:1751-1754(2000).
RN [8]
RP INTERACTION WITH KLF9.
RX PubMed=12672823; DOI=10.1074/jbc.m212098200;
RA Zhang X.L., Zhang D., Michel F.J., Blum J.L., Simmen F.A., Simmen R.C.;
RT "Selective interactions of Kruppel-like factor 9/basic transcription
RT element-binding protein with progesterone receptor isoforms A and B
RT determine transcriptional activity of progesterone-responsive genes in
RT endometrial epithelial cells.";
RL J. Biol. Chem. 278:21474-21482(2003).
RN [9]
RP TISSUE SPECIFICITY (ISOFORMS A AND B).
RX PubMed=15044369; DOI=10.1210/en.2004-0212;
RA Gava N., Clarke C.L., Byth K., Arnett-Mansfield R.L., deFazio A.;
RT "Expression of progesterone receptors A and B in the mouse ovary during the
RT estrous cycle.";
RL Endocrinology 145:3487-3494(2004).
RN [10]
RP TISSUE SPECIFICITY (ISOFORMS A AND B).
RX PubMed=15878961; DOI=10.1210/en.2005-0346;
RA Aupperlee M.D., Smith K.T., Kariagina A., Haslam S.Z.;
RT "Progesterone receptor isoforms A and B: temporal and spatial differences
RT in expression during murine mammary gland development.";
RL Endocrinology 146:3577-3588(2005).
RN [11]
RP TISSUE SPECIFICITY (ISOFORMS A AND B).
RX PubMed=17003284; DOI=10.1677/joe.1.06923;
RA Turgeon J.L., Waring D.W.;
RT "Differential expression and regulation of progesterone receptor isoforms
RT in rat and mouse pituitary cells and LbetaT2 gonadotropes.";
RL J. Endocrinol. 190:837-846(2006).
CC -!- FUNCTION: The steroid hormones and their receptors are involved in the
CC regulation of eukaryotic gene expression and affect cellular
CC proliferation and differentiation in target tissues. Depending on the
CC isoform, progesterone receptor functions as transcriptional activator
CC or repressor. {ECO:0000250|UniProtKB:P06401}.
CC -!- FUNCTION: [Isoform A]: Ligand-dependent transdominant repressor of
CC steroid hormone receptor transcriptional activity including repression
CC of its isoform B, MR and ER. Transrepressional activity may involve
CC recruitment of corepressor NCOR2. {ECO:0000250|UniProtKB:P06401}.
CC -!- FUNCTION: [Isoform B]: Transcriptional activator of several
CC progesteron-dependent promoters in a variety of cell types. Involved in
CC activation of SRC-dependent MAPK signaling on hormone stimulation.
CC {ECO:0000250|UniProtKB:P06401}.
CC -!- SUBUNIT: Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the
CC interaction promotes ubiquitination, decreases sumoylation, and
CC represses transcriptional activity. Interacts with PIAS3; the
CC interaction promotes sumoylation of PR in a hormone-dependent manner,
CC inhibits DNA-binding, and alters nuclear export. Interacts with SP1;
CC the interaction requires ligand-induced phosphorylation on Ser-294 by
CC ERK1/2 MAPK. Interacts with PRMT2 (By similarity). Isoform A interacts
CC with NCOR2. Isoform B (but not isoform A) interacts with NCOA2 and
CC NCOA1. Isoform B (but not isoform A) interacts with KLF9.
CC {ECO:0000250|UniProtKB:P06401, ECO:0000269|PubMed:12672823}.
CC -!- INTERACTION:
CC Q00175; P19785: Esr1; NbExp=5; IntAct=EBI-346821, EBI-346765;
CC Q00175; P42227: Stat3; NbExp=4; IntAct=EBI-346821, EBI-602878;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling
CC is both hormone- and cell cycle-dependent. On hormone stimulation,
CC retained in the cytoplasm in the G(1) and G(2)/M phases (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=B; Synonyms=PRB, PR-B;
CC IsoId=Q00175-1; Sequence=Displayed;
CC Name=A; Synonyms=PRA, PR-A;
CC IsoId=Q00175-2; Sequence=VSP_058743;
CC -!- TISSUE SPECIFICITY: Expression of isoform A and isoform B in mammary
CC epithelial cells is temporally and spatially separated during normal
CC mammary gland development. Isoform A and isoform B are expressed in the
CC pituitary. Isoform A and isoform B are differentially expressed in the
CC ovary and oviduct, and the level of expression is dependent on both the
CC cell type and estrous cycle stage. {ECO:0000269|PubMed:15044369,
CC ECO:0000269|PubMed:15878961, ECO:0000269|PubMed:17003284}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- PTM: Phosphorylated on multiple serine sites. Several of these sites
CC are hormone-dependent. Phosphorylation on Ser-294 is highly hormone-
CC dependent and modulates ubiquitination and sumoylation on Lys-388.
CC Phosphorylation on Ser-345 also requires induction by hormone. Basal
CC phosphorylation on Ser-82, Ser-163, Ser-191 and Ser-400 is increased in
CC response to progesterone and can be phosphorylated in vitro by the
CC CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in
CC the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at
CC this site by CDK2 is ligand-independent, and increases nuclear
CC translocation and transcriptional activity. Phosphorylation at Ser-163
CC and Ser-294, but not at Ser-191, is impaired during the G(2)/M phase of
CC the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required
CC for interaction with SP1 (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylation is hormone-dependent and represses transcriptional
CC activity. Sumoylation on all three sites is enhanced by PIAS3.
CC Desumoylated by SENP1. Sumoylation on Lys-388, the main site of
CC sumoylation, is repressed by ubiquitination on the same site, and
CC modulated by phosphorylation at Ser-294 (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitination is hormone-dependent and represses sumoylation on
CC the same site. Promoted by MAPK-mediated phosphorylation on Ser-294 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required
CC for plasma membrane targeting and for rapid intracellular signaling via
CC ERK and AKT kinases and cAMP generation (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Infertile. Inability to ovulate, uterine
CC hyperplasia and inflammation, severely limited mammary gland
CC development and an impairment in the induction of a sexual behavioral
CC response (PubMed:8603049). In isoform A-defective mice less oocytes are
CC produced, only a subset of implantation-specific uterine epithelial
CC target genes is regulated, and an increased progesterone-dependent
CC proliferative activity of isoform B in the uterine epithelium is
CC observed. Isoform B-defective mice showed unaffected ovulation
CC (PubMed:10976068). {ECO:0000269|PubMed:10976068,
CC ECO:0000269|PubMed:8603049}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39971.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M68915; AAA39971.1; ALT_SEQ; mRNA.
DR EMBL; AC113506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466522; EDL24960.1; -; Genomic_DNA.
DR EMBL; BC145807; AAI45808.1; -; mRNA.
DR EMBL; U12644; AAA66067.1; -; Genomic_DNA.
DR CCDS; CCDS22816.1; -. [Q00175-1]
DR PIR; A39596; A39596.
DR RefSeq; NP_032855.2; NM_008829.2. [Q00175-1]
DR AlphaFoldDB; Q00175; -.
DR SMR; Q00175; -.
DR IntAct; Q00175; 5.
DR MINT; Q00175; -.
DR STRING; 10090.ENSMUSP00000063562; -.
DR ChEMBL; CHEMBL4969; -.
DR iPTMnet; Q00175; -.
DR PhosphoSitePlus; Q00175; -.
DR jPOST; Q00175; -.
DR PaxDb; Q00175; -.
DR PRIDE; Q00175; -.
DR ProteomicsDB; 291877; -. [Q00175-1]
DR ProteomicsDB; 291878; -. [Q00175-2]
DR Antibodypedia; 1685; 3059 antibodies from 56 providers.
DR DNASU; 18667; -.
DR Ensembl; ENSMUST00000070463; ENSMUSP00000063562; ENSMUSG00000031870. [Q00175-1]
DR Ensembl; ENSMUST00000098986; ENSMUSP00000096584; ENSMUSG00000031870. [Q00175-2]
DR Ensembl; ENSMUST00000189181; ENSMUSP00000140124; ENSMUSG00000031870. [Q00175-1]
DR GeneID; 18667; -.
DR KEGG; mmu:18667; -.
DR UCSC; uc009odo.1; mouse.
DR CTD; 5241; -.
DR MGI; MGI:97567; Pgr.
DR VEuPathDB; HostDB:ENSMUSG00000031870; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000159713; -.
DR InParanoid; Q00175; -.
DR OMA; YPKSSDE; -.
DR TreeFam; TF106510; -.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 18667; 2 hits in 76 CRISPR screens.
DR PRO; PR:Q00175; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q00175; protein.
DR Bgee; ENSMUSG00000031870; Expressed in gastrula and 125 other tissues.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042562; F:hormone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; IMP:MGI.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0005496; F:steroid binding; ISO:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
DR GO; GO:0060180; P:female mating behavior; ISO:MGI.
DR GO; GO:0002071; P:glandular epithelial cell maturation; IMP:MGI.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0030879; P:mammary gland development; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:1904709; P:negative regulation of granulosa cell apoptotic process; ISO:MGI.
DR GO; GO:0001542; P:ovulation from ovarian follicle; IMP:MGI.
DR GO; GO:0038001; P:paracrine signaling; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; IDA:MGI.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0042220; P:response to cocaine; ISO:MGI.
DR GO; GO:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; IMP:MGI.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR000128; Progest_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF02161; Prog_receptor; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00544; PROGESTRONER.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Cytoplasm; DNA-binding; Isopeptide bond;
KW Lipid-binding; Lipoprotein; Metal-binding; Nucleus; Palmitate;
KW Phosphoprotein; Receptor; Reference proteome; Steroid-binding;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..926
FT /note="Progesterone receptor"
FT /id="PRO_0000053695"
FT DOMAIN 672..906
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 557..632
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 560..580
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 596..615
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..559
FT /note="Modulating, Pro-Rich"
FT REGION 1..165
FT /note="AF3; mediates transcriptional activation (in isoform
FT B)"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..305
FT /note="Mediates transcriptional transrepression (in isoform
FT A)"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT REGION 168..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..539
FT /note="AF1; mediates transcriptional activation"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT REGION 673..926
FT /note="AF2; mediates transcriptional activation"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOTIF 56..60
FT /note="LXXL motif 1"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOTIF 116..120
FT /note="LXXL motif 1"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOTIF 184..188
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOD_RES 294
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOD_RES 345
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOD_RES 400
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 388
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 388
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06401"
FT CROSSLNK 524
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..165
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_058743"
FT CONFLICT 104
FT /note="A -> P (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="T -> P (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..181
FT /note="AGDSSGTGA -> VGDQSGTGR (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="A -> S (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="S -> Q (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="A -> P (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="D -> E (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..355
FT /note="PPVPC -> TPVPR (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="R -> A (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="Missing (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="G -> A (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="A -> G (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="G -> S (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="V -> I (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="S -> T (in Ref. 1; AAA39971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 926 AA; 98981 MW; E26DDDE9529996A7 CRC64;
MTELQAKDPQ VLHTSGASPS PPHIGSPLLA RLDSGPFQGS QHSDVSSVVS PIPISLDGLL
FPRSCRGPEL PDGKTGDQQS LSDVEGAFSG VEATHREGGR NSRAPEKDSR LLDSVLDSLL
TPSGTEQSHA SPPACEAITS WCLFGPELPE DPRSVPATKG LLSPLMSRPE IKAGDSSGTG
AGQKVLPKGL SPPRQLLLPT SGSAHWPGAG VKPSPQPAAG EVEEDSGLET EGSAAPLLKS
KPRALEGTGS GGGVAANAAS AAPGGVTLVP KEDSRFSAPR VSLEQDSPIA PGRSPLATTV
VDFIHVPILP LNHALLAART RQLLEGDSYD GGATAQGPFA PPRGSPSAPS PPVPCGDFPD
CTYPLEGDPK EDVFPLYGDF QTPGLKIKEE EEGADAAVRS PRPYLSAGAS SSTFPDFPLA
PAPQRAPSSR PGEAAVAGGP SSAAVSPASS SGSALECILY KAEGAPPTQG SFAPLPCKPP
AAGSCLLPRD SLPAAPATAA APAIYQPLGL NGLPQLGYQA AVLKDSLPQV YPPYLNYLRP
DSEASQSPQY GFDSLPQKIC LICGDEASGC HYGVLTCGSC KVFFKRAMEG QHNYLCAGRN
DCIVDKIRRK NCPACRLRKC CQAGMVLGGR KFKKFNKVRV MRTLDGVALP QSVGLPNESQ
ALGQRITFSP NQEIQLVPPL INLLMSIEPD VVYAGHDNTK PDTSSSLLTS LNQLGERQLL
SVVKWSKSLP GFRNLHIDDQ ITLIQYSWMS LMVFGLGWRS YKHVSGQMLY FAPDLILNEQ
RMKELSFYSL CLTMWQIPQE FVKLQVTHEE FLCMKVLLLL NTIPLEGLRS QSQFEEMRSS
YIRELIKAIG LRQKGVVPSS QRFYQLTKLL DSLHDLVKQL HLYCLNTFIQ SRTLAVEFPE
MMSEVIAAQL PKILAGMVKP LLFHKK
