ID ESR2_RAT Reviewed; 530 AA. AC Q62986; O35784; O35785; O55015; O55016; O70195; Q9R185; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 27-MAR-2024, entry version 202. DE RecName: Full=Estrogen receptor beta; DE Short=ER-beta; DE AltName: Full=Nuclear receptor subfamily 3 group A member 2; GN Name=Esr2; Synonyms=Erbeta, Nr3a2; 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 [MRNA] OF 46-530 (ISOFORM 1). RC STRAIN=Sprague-Dawley; TISSUE=Prostate; RX PubMed=8650195; DOI=10.1073/pnas.93.12.5925; RA Kuiper G.G.J.M., Enmark E., Pelto-Huikko M., Nilsson S., Gustafsson J.-A.; RT "Cloning of a novel receptor expressed in rat prostate and ovary."; RL Proc. Natl. Acad. Sci. U.S.A. 93:5925-5930(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-530 (ISOFORM 2), FUNCTION (ISOFORMS 1 AND RP 2), AND TISSUE SPECIFICITY. RC STRAIN=Wistar; TISSUE=Ovary; RX PubMed=9600083; DOI=10.1006/bbrc.1998.8590; RA Maruyama K., Endoh H., Sasaki-Iwaoka H., Kanou H., Shimaya E., RA Hashimoto S., Kato S., Kawashima H.; RT "A novel isoform of rat estrogen receptor beta with 18 amino acid insertion RT in the ligand binding domain as a putative dominant negative regular of RT estrogen action."; RL Biochem. Biophys. Res. Commun. 246:142-147(1998). RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORM 2). RC STRAIN=Wistar; TISSUE=Prostate; RA Aldridge T.C.; RT "Tissue specific responses to estrogen: an explanation based on RT differential activation of multiple estrogen receptors with different RT estrogen response elements."; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE OF 46-530 (ISOFORMS 1; 3 AND 4), AND FUNCTION (ISOFORMS RP 1; 3 AND 4). RC STRAIN=Sprague-Dawley; RX PubMed=9492041; DOI=10.1210/endo.139.3.5840; RA Petersen D.N., Tkalcevic G.T., Koza-Taylor P.H., Turi T.G., Brown T.A.; RT "Identification of estrogen receptor beta2, a functional variant of RT estrogen receptor beta expressed in normal rat tissues."; RL Endocrinology 139:1082-1092(1998). RN [5] RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 5). RC STRAIN=Sprague-Dawley; TISSUE=Brain; RA Price R., Handa R.J.; RT "A novel splice variant of estrogen receptor beta found in rat brain."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP INTERACTION WITH UBE1C. RX PubMed=11818503; DOI=10.1210/mend.16.2.0778; RA Fan M., Long X., Bailey J.A., Reed C.A., Osborne E., Gize E.A., Kirk E.A., RA Bigsby R.M., Nephew K.P.; RT "The activating enzyme of NEDD8 inhibits steroid receptor function."; RL Mol. Endocrinol. 16:315-330(2002). RN [7] RP INTERACTION WITH DNAAF4. RX PubMed=19423554; DOI=10.1093/hmg/ddp215; RA Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E., RA Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E., RA Kere J.; RT "Functional interaction of DYX1C1 with estrogen receptors suggests RT involvement of hormonal pathways in dyslexia."; RL Hum. Mol. Genet. 18:2802-2812(2009). RN [8] RP INTERACTION WITH STUB1, AND TISSUE SPECIFICITY. RX PubMed=21808025; DOI=10.1073/pnas.1104391108; RA Zhang Q.G., Han D., Wang R.M., Dong Y., Yang F., Vadlamudi R.K., RA Brann D.W.; RT "C terminus of Hsc70-interacting protein (CHIP)-mediated degradation of RT hippocampal estrogen receptor-alpha and the critical period hypothesis of RT estrogen neuroprotection."; RL Proc. Natl. Acad. Sci. U.S.A. 108:E617-E624(2011). CC -!- FUNCTION: [Isoform 1]: Nuclear hormone receptor. Binds estrogens with CC an affinity similar to that of ESR1/ER-alpha, and activates expression CC of reporter genes containing estrogen response elements (ERE) in an CC estrogen-dependent manner. {ECO:0000250|UniProtKB:Q92731, CC ECO:0000269|PubMed:8650195, ECO:0000269|PubMed:9600083}. CC -!- FUNCTION: [Isoform 2]: Lacks ligand binding affinity and suppresses CC ESR1/ER-alpha and ESR2 isoform 1/ER-beta1 mediated transcriptional CC activation and may act as a dominant negative regulator of estrogen CC action. {ECO:0000269|PubMed:9600083}. CC -!- FUNCTION: [Isoform 3]: Unable to bind DNA and activate transcription CC due to the truncation of the DNA binding domain. CC {ECO:0000269|PubMed:9492041}. CC -!- FUNCTION: [Isoform 4]: Unable to bind DNA and activate transcription CC due to the truncation of the DNA binding domain. CC {ECO:0000269|PubMed:9492041}. CC -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ESR1. CC Interacts with NCOA1, NCOA3, NCOA5 and NCOA6 coactivators, leading to a CC strong increase of transcription of target genes. Interacts with UBE1C CC and AKAP13. Interacts with DNTTIP2 (By similarity). Interacts with CC CCDC62 in the presence of estradiol/E2; this interaction seems to CC enhance the transcription of target genes. Interacts with PRMT2. CC Interacts with CCAR2 (via N-terminus) in a ligand-independent manner CC (By similarity). Interacts with DNAAF4. Interacts with RBM39, in the CC presence of estradiol (E2) (By similarity). Interacts with STUB1/CHIP CC (PubMed:21808025). {ECO:0000250|UniProtKB:O08537, CC ECO:0000250|UniProtKB:Q92731, ECO:0000269|PubMed:11818503, CC ECO:0000269|PubMed:19423554, ECO:0000269|PubMed:21808025}. CC -!- INTERACTION: CC Q62986; P62989: Ubb; NbExp=2; IntAct=EBI-15938489, EBI-7038538; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92731}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=Beta1; CC IsoId=Q62986-1; Sequence=Displayed; CC Name=2; Synonyms=Beta2; CC IsoId=Q62986-2; Sequence=VSP_003699; CC Name=3; Synonyms=Beta1-delta3; CC IsoId=Q62986-3; Sequence=VSP_003697; CC Name=4; Synonyms=Beta2-delta3; CC IsoId=Q62986-4; Sequence=VSP_003697, VSP_003699; CC Name=5; Synonyms=Beta1-delta4; CC IsoId=Q62986-5; Sequence=VSP_003698; CC -!- TISSUE SPECIFICITY: Expressed in the CA1 region of the hippocampus, CC expression decreases with age (at protein level) (PubMed:21808025). CC Expressed in prostate, ovary, lung, liver, kidney, fat, bone, brain, CC uterus and testis (PubMed:9600083). {ECO:0000269|PubMed:21808025, CC ECO:0000269|PubMed:9600083}. 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: Phosphorylation at Ser-87 and Ser-105 recruits NCOA1. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA05631.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U57439; AAC52602.1; -; mRNA. DR EMBL; AB012721; BAA25431.1; -; mRNA. DR EMBL; AJ002602; CAA05631.1; ALT_INIT; Genomic_DNA. DR EMBL; AJ002603; CAA05632.1; -; Genomic_DNA. DR EMBL; AF042058; AAB97424.1; -; mRNA. DR EMBL; AF042059; AAB97425.1; -; mRNA. DR EMBL; AF042060; AAB97426.1; -; mRNA. DR EMBL; AF042061; AAB97427.1; -; mRNA. DR EMBL; AF161187; AAD47637.1; -; mRNA. DR PIR; JW0046; JW0046. DR RefSeq; NP_036886.1; NM_012754.1. DR PDB; 1HJ1; X-ray; 2.30 A; A=255-509. DR PDB; 1QKN; X-ray; 2.25 A; A=255-509. DR PDB; 2J7X; X-ray; 2.10 A; A=255-509. DR PDB; 2J7Y; X-ray; 1.80 A; A=255-509. DR PDBsum; 1HJ1; -. DR PDBsum; 1QKN; -. DR PDBsum; 2J7X; -. DR PDBsum; 2J7Y; -. DR AlphaFoldDB; Q62986; -. DR SMR; Q62986; -. DR BioGRID; 247214; 6. DR DIP; DIP-60383N; -. DR IntAct; Q62986; 2. DR STRING; 10116.ENSRNOP00000043144; -. DR BindingDB; Q62986; -. DR ChEMBL; CHEMBL3021; -. DR DrugCentral; Q62986; -. DR GuidetoPHARMACOLOGY; 621; -. DR GlyCosmos; Q62986; 1 site, No reported glycans. DR GlyGen; Q62986; 1 site. DR PhosphoSitePlus; Q62986; -. DR PaxDb; 10116-ENSRNOP00000043144; -. DR GeneID; 25149; -. DR KEGG; rno:25149; -. DR UCSC; RGD:2582; rat. [Q62986-1] DR AGR; RGD:2582; -. DR CTD; 2100; -. DR RGD; 2582; Esr2. DR eggNOG; KOG3575; Eukaryota. DR InParanoid; Q62986; -. DR OrthoDB; 5387678at2759; -. DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling. DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway. DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-RNO-8939211; ESR-mediated signaling. DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling. DR EvolutionaryTrace; Q62986; -. DR PRO; PR:Q62986; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0043204; C:perikaryon; IDA:RGD. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD. DR GO; GO:0032993; C:protein-DNA complex; IDA:RGD. DR GO; GO:0003677; F:DNA binding; ISO:RGD. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0019899; F:enzyme binding; IPI:RGD. DR GO; GO:1903924; F:estradiol binding; IPI:RGD. DR GO; GO:0099130; F:estrogen binding; IPI:RGD. DR GO; GO:0034056; F:estrogen response element binding; IDA:RGD. DR GO; GO:1901363; F:heterocyclic compound binding; IPI:RGD. DR GO; GO:0042562; F:hormone binding; IDA:RGD. DR GO; GO:0030284; F:nuclear estrogen receptor activity; ISO:RGD. DR GO; GO:0004879; F:nuclear receptor activity; ISO:RGD. DR GO; GO:0003707; F:nuclear steroid receptor activity; IDA:RGD. DR GO; GO:0097159; F:organic cyclic compound binding; IPI:RGD. DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:RGD. DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:RGD. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD. DR GO; GO:0005496; F:steroid binding; IDA:UniProtKB. DR GO; GO:1990239; F:steroid hormone binding; IPI:RGD. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0021764; P:amygdala development; IEP:RGD. DR GO; GO:0030521; P:androgen receptor signaling pathway; ISO:RGD. DR GO; GO:0001662; P:behavioral fear response; IDA:RGD. DR GO; GO:0007420; P:brain development; ISO:RGD. DR GO; GO:0008283; P:cell population proliferation; ISO:RGD. DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD. DR GO; GO:0071391; P:cellular response to estrogen stimulus; IBA:GO_Central. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:RGD. DR GO; GO:0071259; P:cellular response to magnetism; IEP:RGD. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0021549; P:cerebellum development; IEP:RGD. DR GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; ISO:RGD. DR GO; GO:0050673; P:epithelial cell proliferation; ISO:RGD. DR GO; GO:0044849; P:estrous cycle; IMP:RGD. DR GO; GO:0008585; P:female gonad development; IEP:RGD. DR GO; GO:0008628; P:hormone-mediated apoptotic signaling pathway; ISO:RGD. DR GO; GO:0021854; P:hypothalamus development; IEP:RGD. DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISO:RGD. DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:RGD. DR GO; GO:0007611; P:learning or memory; IMP:RGD. DR GO; GO:0008584; P:male gonad development; IEP:RGD. DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:RGD. DR GO; GO:0048521; P:negative regulation of behavior; IDA:RGD. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:RGD. DR GO; GO:2000252; P:negative regulation of feeding behavior; IMP:RGD. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD. DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:RGD. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD. DR GO; GO:0001764; P:neuron migration; ISO:RGD. DR GO; GO:0001541; P:ovarian follicle development; IEP:RGD. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:RGD. DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:RGD. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0030850; P:prostate gland development; IEP:RGD. DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; ISO:RGD. DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0014823; P:response to activity; IEP:RGD. DR GO; GO:1903925; P:response to bisphenol A; IEP:RGD. DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD. DR GO; GO:0032355; P:response to estradiol; IEP:RGD. DR GO; GO:0043627; P:response to estrogen; IEP:RGD. DR GO; GO:0045471; P:response to ethanol; IEP:RGD. DR GO; GO:0033595; P:response to genistein; IEP:RGD. DR GO; GO:0009725; P:response to hormone; IEP:RGD. DR GO; GO:0044752; P:response to human chorionic gonadotropin; IEP:RGD. DR GO; GO:0017085; P:response to insecticide; IEP:RGD. DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD. DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD. DR GO; GO:1902074; P:response to salt; IEP:RGD. DR GO; GO:0033574; P:response to testosterone; IMP:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0060009; P:Sertoli cell development; IEP:RGD. DR GO; GO:0060011; P:Sertoli cell proliferation; IMP:RGD. DR GO; GO:0060065; P:uterus development; ISO:RGD. DR GO; GO:0060068; P:vagina development; ISO:RGD. DR GO; GO:0042311; P:vasodilation; IMP:RGD. DR CDD; cd07171; NR_DBD_ER; 1. DR CDD; cd06949; NR_LBD_ER; 1. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1. DR InterPro; IPR021064; ER-beta-like_N. DR InterPro; IPR028355; ER-beta/gamma. DR InterPro; IPR024178; Est_rcpt/est-rel_rcp. DR InterPro; IPR035500; NHR-like_dom_sf. DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd. DR InterPro; IPR001723; Nuclear_hrmn_rcpt. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR PANTHER; PTHR48092:SF12; ESTROGEN RECEPTOR BETA; 1. DR PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1. DR Pfam; PF12497; ERbeta_N; 1. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF00105; zf-C4; 1. DR PIRSF; PIRSF500102; ER-b; 1. DR PIRSF; PIRSF002527; ER-like_NR; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 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 3D-structure; Activator; Alternative splicing; DNA-binding; Glycoprotein; KW Lipid-binding; Metal-binding; Nucleus; Phosphoprotein; Receptor; KW Reference proteome; Steroid-binding; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..530 FT /note="Estrogen receptor beta" FT /id="PRO_0000053646" FT DOMAIN 264..498 FT /note="NR LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT DNA_BIND 149..214 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 149..169 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 185..209 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT REGION 1..148 FT /note="Modulating" FT REGION 506..530 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 61 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000250|UniProtKB:O08537" FT MOD_RES 87 FT /note="Phosphoserine; by MAPK" FT /evidence="ECO:0000250|UniProtKB:O08537" FT MOD_RES 105 FT /note="Phosphoserine; by MAPK" FT /evidence="ECO:0000250|UniProtKB:O08537" FT CARBOHYD 61 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250" FT VAR_SEQ 179..217 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_003697" FT VAR_SEQ 219..318 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_003698" FT VAR_SEQ 364 FT /note="R -> RSSEDPHWHVAQMKSAAPR (in isoform 2 and isoform FT 4)" FT /evidence="ECO:0000303|PubMed:9600083" FT /id="VSP_003699" FT CONFLICT 72 FT /note="L -> Q (in Ref. 3 and 4)" FT /evidence="ECO:0000305" FT CONFLICT 150 FT /note="P -> A (in Ref. 3 and 4)" FT /evidence="ECO:0000305" FT CONFLICT 165 FT /note="S -> P (in Ref. 3; CAA05631)" FT /evidence="ECO:0000305" FT CONFLICT 505 FT /note="S -> P (in Ref. 3; CAA05631)" FT /evidence="ECO:0000305" FT HELIX 265..274 FT /evidence="ECO:0007829|PDB:2J7Y" FT HELIX 291..315 FT /evidence="ECO:0007829|PDB:2J7Y" FT HELIX 319..321 FT /evidence="ECO:0007829|PDB:2J7Y" FT HELIX 324..347 FT /evidence="ECO:0007829|PDB:2J7Y" FT STRAND 353..357 FT /evidence="ECO:0007829|PDB:2J7Y" FT STRAND 360..363 FT /evidence="ECO:0007829|PDB:2J7Y" FT HELIX 364..369 FT /evidence="ECO:0007829|PDB:2J7Y" FT HELIX 373..390 FT /evidence="ECO:0007829|PDB:2J7Y" FT HELIX 394..405 FT /evidence="ECO:0007829|PDB:2J7Y" FT TURN 406..409 FT /evidence="ECO:0007829|PDB:2J7Y" FT HELIX 421..443 FT /evidence="ECO:0007829|PDB:2J7Y" FT HELIX 448..481 FT /evidence="ECO:0007829|PDB:2J7Y" FT HELIX 489..496 FT /evidence="ECO:0007829|PDB:2J7Y" SQ SEQUENCE 530 AA; 59152 MW; 36F269D9FD773DA9 CRC64; MEIKNSPSSL SSPASYNCSQ SILPLEHGPI YIPSSYVDNR HEYSAMTFYS PAVMNYSVPG STSNLDGGPV RLSTSPNVLW PTSGHLSPLA THCQSSLLYA EPQKSPWCEA RSLEHTLPVN RETLKRKLSG SSCASPVTSP NAKRDAHFCP VCSDYASGYH YGVWSCEGCK AFFKRSIQGH NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRIVR RQRSSSEQVH CLSKAKRNGG HAPRVKELLL STLSPEQLVL TLLEAEPPNV LVSRPSMPFT EASMMMSLTK LADKELVHMI GWAKKIPGFV ELSLLDQVRL LESCWMEVLM VGLMWRSIDH PGKLIFAPDL VLDRDEGKCV EGILEIFDML LATTSRFREL KLQHKEYLCV KAMILLNSSM YPLASANQEA ESSRKLTHLL NAVTDALVWV IAKSGISSQQ QSVRLANLLM LLSHVRHISN KGMEHLLSMK CKNVVPVYDL LLEMLNAHTL RGYKSSISGS ECSSTEDSKN KESSQNLQSQ //