EGLN_MOUSE
ID EGLN_MOUSE Reviewed; 653 AA.
AC Q63961; Q61520; Q8K100;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Endoglin;
DE AltName: Full=Cell surface MJ7/18 antigen;
DE AltName: CD_antigen=CD105 {ECO:0000303|PubMed:10625534};
DE Flags: Precursor;
GN Name=Eng; Synonyms=Edg;
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], AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=8125301; DOI=10.1016/0378-1119(94)90808-7;
RA Ge A.Z., Butcher E.C.;
RT "Cloning and expression of a cDNA encoding mouse endoglin, an endothelial
RT cell TGF-beta ligand.";
RL Gene 138:201-206(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBUNIT, AND INTERACTION
RP WITH TGFB1.
RC STRAIN=CD-1; TISSUE=Placenta;
RX PubMed=8194490; DOI=10.1210/endo.134.6.8194490;
RA St Jacques S., Cymerman U., Pece N., Letarte M.;
RT "Molecular characterization and in situ localization of murine endoglin
RT reveal that it is a transforming growth factor-beta binding protein of
RT endothelial and stromal cells.";
RL Endocrinology 134:2645-2657(1994).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [6]
RP FUNCTION.
RX PubMed=17540773; DOI=10.1074/jbc.m700176200;
RA Lee N.Y., Blobe G.C.;
RT "The interaction of endoglin with beta-arrestin2 regulates transforming
RT growth factor-beta-mediated ERK activation and migration in endothelial
RT cells.";
RL J. Biol. Chem. 282:21507-21517(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=10625534; DOI=10.1006/dbio.1999.9534;
RA Arthur H.M., Ure J., Smith A.J., Renforth G., Wilson D.I., Torsney E.,
RA Charlton R., Parums D.V., Jowett T., Marchuk D.A., Burn J., Diamond A.G.;
RT "Endoglin, an ancillary TGFbeta receptor, is required for extraembryonic
RT angiogenesis and plays a key role in heart development.";
RL Dev. Biol. 217:42-53(2000).
RN [8]
RP PHOSPHORYLATION AT SER-641 AND SER-644.
RX PubMed=20042635; DOI=10.1093/carcin/bgp327;
RA Ray B.N., Lee N.Y., How T., Blobe G.C.;
RT "ALK5 phosphorylation of the endoglin cytoplasmic domain regulates
RT Smad1/5/8 signaling and endothelial cell migration.";
RL Carcinogenesis 31:435-441(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH GDF2 AND BMP10.
RX PubMed=21737454; DOI=10.1074/jbc.m111.260133;
RA Castonguay R., Werner E.D., Matthews R.G., Presman E., Mulivor A.W.,
RA Solban N., Sako D., Pearsall R.S., Underwood K.W., Seehra J., Kumar R.,
RA Grinberg A.V.;
RT "Soluble endoglin specifically binds bone morphogenetic proteins 9 and 10
RT via its orphan domain, inhibits blood vessel formation, and suppresses
RT tumor growth.";
RL J. Biol. Chem. 286:30034-30046(2011).
RN [11]
RP FUNCTION.
RX PubMed=23300529; DOI=10.1371/journal.pone.0050920;
RA Nolan-Stevaux O., Zhong W., Culp S., Shaffer K., Hoover J.,
RA Wickramasinghe D., Ruefli-Brasse A.;
RT "Endoglin requirement for BMP9 signaling in endothelial cells reveals new
RT mechanism of action for selective anti-endoglin antibodies.";
RL PLoS ONE 7:E50920-E50920(2012).
RN [12]
RP FUNCTION.
RX PubMed=28530658; DOI=10.1038/ncb3528;
RA Sugden W.W., Meissner R., Aegerter-Wilmsen T., Tsaryk R., Leonard E.V.,
RA Bussmann J., Hamm M.J., Herzog W., Jin Y., Jakobsson L., Denz C.,
RA Siekmann A.F.;
RT "Endoglin controls blood vessel diameter through endothelial cell shape
RT changes in response to haemodynamic cues.";
RL Nat. Cell Biol. 19:653-665(2017).
CC -!- FUNCTION: Vascular endothelium glycoprotein that plays an important
CC role in the regulation of angiogenesis (PubMed:10625534). Required for
CC normal structure and integrity of adult vasculature (By similarity).
CC Regulates the migration of vascular endothelial cells
CC (PubMed:17540773). Required for normal extraembryonic angiogenesis and
CC for embryonic heart development (PubMed:10625534). May regulate
CC endothelial cell shape changes in response to blood flow, which drive
CC vascular remodeling and establishment of normal vascular morphology
CC during angiogenesis (PubMed:28530658). May play a role in the binding
CC of endothelial cells to integrins. Acts as TGF-beta coreceptor and is
CC involved in the TGF-beta/BMP signaling cascade that ultimately leads to
CC the activation of SMAD transcription factors (PubMed:23300529).
CC Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and
CC modulates TGFB1 signaling through SMAD3 (By similarity).
CC {ECO:0000250|UniProtKB:P17813, ECO:0000269|PubMed:10625534,
CC ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:23300529,
CC ECO:0000269|PubMed:28530658}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:8194490). Forms a
CC heteromeric complex with the signaling receptors for transforming
CC growth factor-beta: TGFBR1 and/or TGFBR2. Interacts with TGFB1
CC (PubMed:8194490). It is able to bind TGFB1 and TGFB2 with high
CC affinity, but not TGFB3. Interacts with GDF2, forming a heterotetramer
CC with a 2:2 stoichiometry. Interacts with ACVRL1. Can form a heteromeric
CC complex with GDF2 and ACVRL1. Interacts with BMP10. Interacts with
CC DYNLT4. Interacts with ARRB2. {ECO:0000250|UniProtKB:P17813,
CC ECO:0000269|PubMed:8194490}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8125301};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:8125301}.
CC -!- TISSUE SPECIFICITY: Detected on blood vessels (at protein level)
CC (PubMed:8194490). Detected on adult pulmonary artery, capillaries
CC supporting the heart muscle and lung alveolar capillary endothelial
CC cells (PubMed:10625534). Endoglin is restricted to endothelial cells in
CC all tissues except bone marrow and is also found in stromal cells
CC within the connective tissue of intestine, stomach, heart, skeletal
CC muscle, uterus, ovary, oviduct, testis and thymus (PubMed:8194490).
CC {ECO:0000269|PubMed:8194490}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryo (at protein level). Detected in
CC endothelium from yolk sac vessels. {ECO:0000269|PubMed:10625534}.
CC -!- DOMAIN: The ZP domain mediates dimerization.
CC {ECO:0000250|UniProtKB:P17813}.
CC -!- DOMAIN: The N-terminal OR region is composed of two intertwined domains
CC (OR1 and OR2) with a common, novel fold. Each contains 12 beta-strands
CC that form a parallel beta-helix-like structure, plus a single alpha-
CC helix. The OR1 region mediates interaction with GDF2.
CC {ECO:0000250|UniProtKB:P17813}.
CC -!- DISRUPTION PHENOTYPE: Full embryonic lethality at about 10.5 dpc. At
CC 9.5 dpc, embryos display abnormal yolk sac vasculature and yolk sac
CC anemia. Mutant embryos are also anemic, probably due to defective
CC hematopoiesis in the yolk sac. In contrast, the embryonic vasculature
CC appears grossly normal in most cases, but heart development is
CC abnormal, and nearly all mutant embryos had enlarged ventricles and
CC dilated outflow tracts. Besides, many had abnormal cardiac looping and
CC displayed pericardial effusion. Heterozygous mice have occasionally
CC abnormally convoluted and dilated blood vessels with disorganized
CC smooth muscle cells surrounding them; these blood vessels are very
CC fragile and rupture easily. {ECO:0000269|PubMed:10625534}.
CC -!- MISCELLANEOUS: Lacks a RGD motif, contrary to the human protein.
CC {ECO:0000305}.
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DR EMBL; S69407; AAB30196.1; -; mRNA.
DR EMBL; X77952; CAA54917.1; -; mRNA.
DR EMBL; AL772271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08562.1; -; Genomic_DNA.
DR EMBL; BC029080; AAH29080.1; -; mRNA.
DR CCDS; CCDS15925.1; -.
DR PIR; I48341; I48341.
DR RefSeq; NP_031958.2; NM_007932.2.
DR AlphaFoldDB; Q63961; -.
DR SMR; Q63961; -.
DR BioGRID; 199450; 2.
DR DIP; DIP-47636N; -.
DR IntAct; Q63961; 6.
DR MINT; Q63961; -.
DR STRING; 10090.ENSMUSP00000009705; -.
DR GlyGen; Q63961; 5 sites.
DR iPTMnet; Q63961; -.
DR PhosphoSitePlus; Q63961; -.
DR EPD; Q63961; -.
DR jPOST; Q63961; -.
DR MaxQB; Q63961; -.
DR PaxDb; Q63961; -.
DR PRIDE; Q63961; -.
DR ProteomicsDB; 277565; -.
DR Antibodypedia; 2321; 2452 antibodies from 53 providers.
DR DNASU; 13805; -.
DR Ensembl; ENSMUST00000009705; ENSMUSP00000009705; ENSMUSG00000026814.
DR GeneID; 13805; -.
DR KEGG; mmu:13805; -.
DR UCSC; uc008jgk.2; mouse.
DR CTD; 2022; -.
DR MGI; MGI:95392; Eng.
DR VEuPathDB; HostDB:ENSMUSG00000026814; -.
DR eggNOG; ENOG502RZQ9; Eukaryota.
DR GeneTree; ENSGT00530000063861; -.
DR InParanoid; Q63961; -.
DR OMA; YIYLHTR; -.
DR OrthoDB; 1263397at2759; -.
DR PhylomeDB; Q63961; -.
DR TreeFam; TF337375; -.
DR BioGRID-ORCS; 13805; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Eng; mouse.
DR PRO; PR:Q63961; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q63961; protein.
DR Bgee; ENSMUSG00000026814; Expressed in gonadal fat pad and 253 other tissues.
DR ExpressionAtlas; Q63961; baseline and differential.
DR Genevisible; Q63961; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0072563; C:endothelial microparticle; IDA:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0036122; F:BMP binding; ISO:MGI.
DR GO; GO:0015026; F:coreceptor activity; ISO:MGI.
DR GO; GO:0005534; F:galactose binding; ISO:MGI.
DR GO; GO:0005539; F:glycosaminoglycan binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0050431; F:transforming growth factor beta binding; IDA:BHF-UCL.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; IBA:GO_Central.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISO:MGI.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0048844; P:artery morphogenesis; IMP:BHF-UCL.
DR GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR GO; GO:1905222; P:atrioventricular canal morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003209; P:cardiac atrium morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003208; P:cardiac ventricle morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0003273; P:cell migration involved in endocardial cushion formation; IMP:MGI.
DR GO; GO:0048870; P:cell motility; ISO:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0022009; P:central nervous system vasculogenesis; ISO:MGI.
DR GO; GO:0070483; P:detection of hypoxia; ISO:MGI.
DR GO; GO:0035912; P:dorsal aorta morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IBA:GO_Central.
DR GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
DR GO; GO:0070278; P:extracellular matrix constituent secretion; IEA:Ensembl.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISO:MGI.
DR GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IGI:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IGI:MGI.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:MGI.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:1905065; P:positive regulation of vascular associated smooth muscle cell differentiation; IMP:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0031960; P:response to corticosteroid; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0048745; P:smooth muscle tissue development; IMP:BHF-UCL.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0097084; P:vascular associated smooth muscle cell development; IMP:BHF-UCL.
DR GO; GO:0001570; P:vasculogenesis; IMP:BHF-UCL.
DR GO; GO:0048845; P:venous blood vessel morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
DR GO; GO:0042060; P:wound healing; ISO:MGI.
DR InterPro; IPR001507; ZP_dom.
DR Pfam; PF00100; Zona_pellucida; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..653
FT /note="Endoglin"
FT /id="PRO_0000021157"
FT TOPO_DOM 27..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 363..510
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 27..337
FT /note="Required for interaction with GDF2"
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT REGION 27..47
FT /note="OR1, N-terminal part"
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT REGION 48..201
FT /note="OR2"
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT REGION 202..330
FT /note="OR1, C-terminal part"
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT REGION 270..282
FT /note="Essential for interaction with GDF2"
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT REGION 624..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 641
FT /note="Phosphoserine; by TGFBR1"
FT /evidence="ECO:0000269|PubMed:20042635"
FT MOD_RES 644
FT /note="Phosphoserine; by TGFBR1"
FT /evidence="ECO:0000269|PubMed:20042635"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..209
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 54..184
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 244..330
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 350..382
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 363..442
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 394..412
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 493..549
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 516
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT CONFLICT 94
FT /note="Q -> R (in Ref. 2; CAA54917)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="V -> D (in Ref. 1; AAB30196)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="I -> V (in Ref. 2; CAA54917)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 70021 MW; AD9DD2F823FB06A1 CRC64;
MDRGVLPLPI TLLFVIYSFV PTTGLAERVG CDLQPVDPTR GEVTFTTSQV SEGCVAQAAN
AVREVHVLFL DFPGMLSHLE LTLQASKQNG TETQEVFLVL VSNKNVFVKF QAPEIPLHLA
YDSSLVIFQG QPRVNITVLP SLTSRKQILD WAATKGAITS IAALDDPQSI VLQLGQDPKA
PFLCLPEAHK DMGATLEWQP RAQTPVQSCR LEGVSGHKEA YILRILPGSE AGPRTVTVMM
ELSCTSGDAI LILHGPPYVS WFIDINHSMQ ILTTGEYSVK IFPGSKVKGV ELPDTPQGLI
AEARKLNASI VTSFVELPLV SNVSLRASSC GGVFQTTPAP VVTTPPKDTC SPVLLMSLIQ
PKCGNQVMTL ALNKKHVQTL QCTITGLTFW DSSCQAEDTD DHLVLSSAYS SCGMKVTAHV
VSNEVIISFP SGSPPLRKKV QCIDMDSLSF QLGLYLSPHF LQASNTIELG QQAFVQVSVS
PLTSEVTVQL DSCHLDLGPE GDMVELIQSR TAKGSCVTLL SPSPEGDPRF SFLLRVYMVP
TPTAGTLSCN LALRPSTLSQ EVYKTVSMRL NIVSPDLSGK GLVLPSVLGI TFGAFLIGAL
LTAALWYIYS HTRGPSKREP VVAVAAPASS ESSSTNHSIG STQSTPCSTS SMA
