GPER1_MACMU
ID GPER1_MACMU Reviewed; 375 AA.
AC F7EQ49;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=G-protein coupled estrogen receptor 1;
DE AltName: Full=G protein-coupled estrogen receptor 1;
DE AltName: Full=G-protein coupled receptor 30;
GN Name=GPER1; Synonyms=GPER, GPR30;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19131510; DOI=10.1210/me.2008-0299;
RA Noel S.D., Keen K.L., Baumann D.I., Filardo E.J., Terasawa E.;
RT "Involvement of G protein-coupled receptor 30 (GPR30) in rapid action of
RT estrogen in primate LHRH neurons.";
RL Mol. Endocrinol. 23:349-359(2009).
CC -!- FUNCTION: G-protein coupled estrogen receptor that binds to 17-beta-
CC estradiol (E2) with high affinity, leading to rapid and transient
CC activation of numerous intracellular signaling pathways. Stimulates
CC cAMP production, calcium mobilization and tyrosine kinase Src inducing
CC the release of heparin-bound epidermal growth factor (HB-EGF) and
CC subsequent transactivation of the epidermal growth factor receptor
CC (EGFR), activating downstream signaling pathways such as PI3K/Akt and
CC ERK/MAPK. Mediates pleiotropic functions among others in the
CC cardiovascular, endocrine, reproductive, immune and central nervous
CC systems. Has a role in cardioprotection by reducing cardiac hypertrophy
CC and perivascular fibrosis in a RAMP3-dependent manner. Regulates
CC arterial blood pressure by stimulating vasodilation and reducing
CC vascular smooth muscle and microvascular endothelial cell
CC proliferation. Plays a role in blood glucose homeostasis contributing
CC to the insulin secretion response by pancreatic beta cells. Triggers
CC mitochondrial apoptosis during pachytene spermatocyte differentiation.
CC Stimulates uterine epithelial cell proliferation. Enhances uterine
CC contractility in response to oxytocin. Contributes to thymic atrophy by
CC inducing apoptosis. Attenuates TNF-mediated endothelial expression of
CC leukocyte adhesion molecules. Promotes neuritogenesis in developing
CC hippocampal neurons. Plays a role in acute neuroprotection against
CC NMDA-induced excitotoxic neuronal death. Inhibits early osteoblast
CC proliferation at growth plate during skeletal development. Inhibits
CC mature adipocyte differentiation and lipid accumulation. Involved in
CC the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in
CC epithelial cells. Functions also as a receptor for aldosterone
CC mediating rapid regulation of vascular contractibility through the
CC PI3K/ERK signaling pathway. Involved in cancer progression regulation.
CC Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid
CC genomic response through the EGFR/ERK transduction pathway. Associated
CC with EGFR, may act as a transcription factor activating growth
CC regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1
CC and fibronectin (FN) matrix assembly in breast cancer cells (By
CC similarity). Increases firing activity and intracellular calcium
CC oscillations in luteinizing hormone-releasing hormone (LHRH) neurons.
CC {ECO:0000250, ECO:0000269|PubMed:19131510}.
CC -!- SUBUNIT: Homodimer. Heterodimer; heterodimerizes with other G-protein-
CC coupled receptor (GPCRs) like CRHR1, HTR1A and PAQR8. Interacts with
CC RAMP3. Interacts with KRT7 and KRT8. Interacts with EGFR; the
CC interaction increases after agonist-induced stimulation in cancer-
CC associated fibroblasts (CAF). Interacts with EGFR and ESR1. Interacts
CC (via C-terminus tail motif) with DLG4 (via N-terminus tandem pair of
CC PDZ domains); the interaction is direct and induces the increase of
CC GPER1 protein levels residing at the plasma membrane surface in a
CC estradiol-independent manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Basolateral cell membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic
CC reticulum membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome
CC {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}.
CC Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell
CC projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cell projection, axon {ECO:0000250}.
CC Postsynaptic density {ECO:0000250}. Mitochondrion membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Note=Endocytosed in a agonist- and arrestin-independent manner.
CC Colocalized with RAMP3 and clathrin-coated pits at the plasma membrane.
CC Colocalized with transferrin receptor at the plasma membrane and
CC perinuclear region. Accumulated and colocalized with RAB11 proteins in
CC recycling endosomes and trans-Golgi network (TGN), but does neither
CC recycle back to the cell surface nor traffics to late endosome or
CC lysosome. Colocalized with calnexin in the endoplasmic reticulum.
CC Traffics to intracellular sites via cytokeratin intermediate filaments
CC like KRT7 and KRT8 after constitutive endocytosis in epithelial cells.
CC Colocalized with EGFR in the nucleus of agonist-induced cancer-
CC associated fibroblasts (CAF) (By similarity). Colocalized with BSN to
CC the active zone of presynaptic density. Colocalized with DLG4/PSD95 and
CC neurabin-2 PPP1R9B in neuronal synaptosomes (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in olfactory placode and LH-releasing
CC hormone (LHRH) neurons (at protein level). Expressed in hypothalamus,
CC cerebellum, olfactory placode and uterus.
CC {ECO:0000269|PubMed:19131510}.
CC -!- PTM: Ubiquitinated; ubiquitination occurs at the plasma membrane and
CC leads to proteasome-mediated degradation. {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; CM001255; EHH17092.1; -; Genomic_DNA.
DR RefSeq; XP_001084531.1; XM_001084531.3.
DR AlphaFoldDB; F7EQ49; -.
DR SMR; F7EQ49; -.
DR STRING; 9544.ENSMMUP00000009453; -.
DR Ensembl; ENSMMUT00000010070; ENSMMUP00000009453; ENSMMUG00000007209.
DR Ensembl; ENSMMUT00000070839; ENSMMUP00000049453; ENSMMUG00000007209.
DR GeneID; 696625; -.
DR KEGG; mcc:696625; -.
DR CTD; 2852; -.
DR VEuPathDB; HostDB:ENSMMUG00000007209; -.
DR VGNC; VGNC:73132; GPER1.
DR eggNOG; ENOG502QU56; Eukaryota.
DR GeneTree; ENSGT00940000154307; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; F7EQ49; -.
DR OMA; FRTKQHA; -.
DR OrthoDB; 736624at2759; -.
DR TreeFam; TF333506; -.
DR Proteomes; UP000006718; Chromosome 3.
DR Proteomes; UP000013456; Chromosome 3.
DR Bgee; ENSMMUG00000007209; Expressed in dorsolateral prefrontal cortex and 17 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
DR GO; GO:0044327; C:dendritic spine head; ISS:UniProtKB.
DR GO; GO:0032591; C:dendritic spine membrane; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0045095; C:keratin filament; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0038054; F:G protein-coupled estrogen receptor activity; ISS:UniProtKB.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; ISS:UniProtKB.
DR GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
DR GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030263; P:apoptotic chromosome condensation; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0071389; P:cellular response to mineralocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010948; P:negative regulation of cell cycle process; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0002695; P:negative regulation of leukocyte activation; ISS:UniProtKB.
DR GO; GO:0051055; P:negative regulation of lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0019228; P:neuronal action potential; IDA:UniProtKB.
DR GO; GO:0030264; P:nuclear fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2000724; P:positive regulation of cardiac vascular smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IDA:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0070474; P:positive regulation of uterine smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0043401; P:steroid hormone mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0042311; P:vasodilation; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Cell cycle; Cell membrane; Cell projection;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Differentiation;
KW Disulfide bond; Endoplasmic reticulum; Endosome;
KW G-protein coupled receptor; Glycoprotein; Golgi apparatus; Immunity;
KW Inflammatory response; Innate immunity; Membrane; Mitochondrion;
KW Neurogenesis; Nucleus; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Synapse; Transducer; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..375
FT /note="G-protein coupled estrogen receptor 1"
FT /id="PRO_0000424543"
FT TOPO_DOM 1..66
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q99527"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 130..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 375 AA; 42326 MW; 400DA0A3AD7CFA02 CRC64;
MEVTSQARGM GLEMYPGTMQ PAAPNTTSPE LNLSHPLLGA SLANGTGELS EHQQYVIGLF
LSCLYTIFLF PIGFVGNILI LVVNISFREK MTIPDLYFIN LAVADLILVA DSLIEVFNLH
EQYYDIAVLC TFMSLFLQVN MYSSVFFLTW MSFDRYIALA RAMRCSLFRT KHHARLSCGL
IWMASVSATL VPFTAVHLQH TDEACFCFAD VREVQWLEVT LGFIVPFAII GLCYSLIVRV
LVRAHRHRGL RPRRQKALRM ILAVVLVFFV CWLPENVFIS VHLLQRTQPG AAPCKQSFRH
AHPLTGHIVN LAAFSNSCLN PLIYSFLGET FREKLRLYIE QKTNLPALNR FCHAALKAVI
PDSTEQSDVR FSSAV
