ID PLXB2_HUMAN Reviewed; 1838 AA. AC O15031; A6QRH0; Q7KZU3; Q9BSU7; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 3. DT 13-FEB-2019, entry version 162. DE RecName: Full=Plexin-B2; DE AltName: Full=MM1; DE Flags: Precursor; GN Name=PLXNB2; Synonyms=KIAA0315; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=9205841; DOI=10.1093/dnares/4.2.141; RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VII. RT The complete sequences of 100 new cDNA clones from brain which can RT code for large proteins in vitro."; RL DNA Res. 4:141-150(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1364-1838. RC TISSUE=Ovary; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1369-1838. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP INTERACTION WITH ARHGEF11 AND ARHGEF12, AND FUNCTION. RX PubMed=12183458; DOI=10.1074/jbc.M206005200; RA Perrot V., Vazquez-Prado J., Gutkind J.S.; RT "Plexin B regulates Rho through the guanine nucleotide exchange RT factors leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF."; RL J. Biol. Chem. 277:43115-43120(2002). RN [6] RP SUBUNIT, HETERODIMERIZATION WITH PLXNB1, MUTAGENESIS OF RP 1161-ARG--ARG-1164, PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION. RX PubMed=12533544; DOI=10.1074/jbc.M210156200; RA Artigiani S., Barberis D., Fazzari P., Longati P., Angelini P., RA van de Loo J.-W., Comoglio P.M., Tamagnone L.; RT "Functional regulation of semaphorin receptors by proprotein RT convertases."; RL J. Biol. Chem. 278:10094-10101(2003). RN [7] RP INTERACTION WITH MET AND MST1R, AND FUNCTION. RX PubMed=15184888; DOI=10.1038/sj.onc.1207650; RA Conrotto P., Corso S., Gamberini S., Comoglio P.M., Giordano S.; RT "Interplay between scatter factor receptors and B plexins controls RT invasive growth."; RL Oncogene 23:5131-5137(2004). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127 AND ASN-733. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP VARIANT [LARGE SCALE ANALYSIS] GLU-318, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Cell surface receptor for SEMA4C, SEMA4D and SEMA4G that CC plays an important role in cell-cell signaling (By similarity). CC Plays a role in glutamatergic synapse development and is required CC for SEMA4A-mediated excitatory synapse development (By CC similarity). Binding to class 4 semaphorins promotes downstream CC activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248' (By CC similarity). Required for normal differentiation and migration of CC neuronal cells during brain corticogenesis and for normal CC embryonic brain development (By similarity). Regulates the CC migration of cerebellar granule cells in the developing brain (By CC similarity). Plays a role in RHOA activation and subsequent CC changes of the actin cytoskeleton (PubMed:12183458). Plays a role CC in axon guidance, invasive growth and cell migration CC (PubMed:15184888). May modulate the activity of RAC1 and CDC42 (By CC similarity). {ECO:0000250|UniProtKB:B2RXS4, CC ECO:0000269|PubMed:12183458, ECO:0000269|PubMed:15184888}. CC -!- SUBUNIT: Monomer, and heterodimer with PLXNB1 (PubMed:12533544). CC Interacts with SEMA4C, SEMA4D and SEMA4G (By similarity). CC Interacts with MET (PubMed:15184888). Interacts with ARHGEF11 and CC ARHGEF12 (PubMed:12183458). May also interact with MST1R CC (PubMed:15184888). {ECO:0000250|UniProtKB:B2RXS4, CC ECO:0000269|PubMed:12183458, ECO:0000269|PubMed:12533544, CC ECO:0000269|PubMed:15184888}. CC -!- INTERACTION: CC P08581:MET; NbExp=2; IntAct=EBI-722004, EBI-1039152; CC Q04912:MST1R; NbExp=2; IntAct=EBI-722004, EBI-2637518; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12533544}; CC Single-pass type I membrane protein {ECO:0000255}. CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA21571.1; Type=Erroneous initiation; 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; AB002313; BAA21571.1; ALT_INIT; mRNA. DR EMBL; AL022328; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX649592; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC004542; AAH04542.2; -; mRNA. DR EMBL; BT006887; AAP35533.1; -; mRNA. DR CCDS; CCDS43035.1; -. DR RefSeq; NP_036533.2; NM_012401.3. DR RefSeq; XP_005261966.1; XM_005261909.1. DR RefSeq; XP_005261967.1; XM_005261910.2. DR RefSeq; XP_005261968.1; XM_005261911.4. DR RefSeq; XP_006724476.1; XM_006724413.2. DR RefSeq; XP_016884192.1; XM_017028703.1. DR RefSeq; XP_016884193.1; XM_017028704.1. DR UniGene; Hs.3989; -. DR UniGene; Hs.736016; -. DR PDB; 4E71; X-ray; 2.26 A; A=1452-1562. DR PDBsum; 4E71; -. DR ProteinModelPortal; O15031; -. DR SMR; O15031; -. DR BioGrid; 117178; 44. DR IntAct; O15031; 22. DR MINT; O15031; -. DR STRING; 9606.ENSP00000352288; -. DR GlyConnect; 1613; -. DR iPTMnet; O15031; -. DR PhosphoSitePlus; O15031; -. DR SwissPalm; O15031; -. DR BioMuta; PLXNB2; -. DR EPD; O15031; -. DR jPOST; O15031; -. DR MaxQB; O15031; -. DR PaxDb; O15031; -. DR PeptideAtlas; O15031; -. DR PRIDE; O15031; -. DR ProteomicsDB; 48388; -. DR DNASU; 23654; -. DR Ensembl; ENST00000359337; ENSP00000352288; ENSG00000196576. DR Ensembl; ENST00000449103; ENSP00000409171; ENSG00000196576. DR GeneID; 23654; -. DR KEGG; hsa:23654; -. DR UCSC; uc003bkv.4; human. DR CTD; 23654; -. DR DisGeNET; 23654; -. DR EuPathDB; HostDB:ENSG00000196576.14; -. DR GeneCards; PLXNB2; -. DR HGNC; HGNC:9104; PLXNB2. DR HPA; HPA003100; -. DR MIM; 604293; gene. DR neXtProt; NX_O15031; -. DR OpenTargets; ENSG00000196576; -. DR PharmGKB; PA33430; -. DR eggNOG; ENOG410IN3E; Eukaryota. DR eggNOG; ENOG411131Q; LUCA. DR GeneTree; ENSGT00940000153516; -. DR HOGENOM; HOG000231376; -. DR HOVERGEN; HBG053404; -. DR InParanoid; O15031; -. DR KO; K06821; -. DR OMA; EDSCPQF; -. DR OrthoDB; 753479at2759; -. DR PhylomeDB; O15031; -. DR TreeFam; TF312962; -. DR ChiTaRS; PLXNB2; human. DR GeneWiki; PLXNB2; -. DR GenomeRNAi; 23654; -. DR PRO; PR:O15031; -. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; ENSG00000196576; Expressed in 218 organ(s), highest expression level in right uterine tube. DR ExpressionAtlas; O15031; baseline and differential. DR Genevisible; O15031; HS. DR GO; GO:0009986; C:cell surface; HDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB. DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central. DR GO; GO:0017154; F:semaphorin receptor activity; ISS:UniProtKB. DR GO; GO:0007420; P:brain development; ISS:UniProtKB. DR GO; GO:1904861; P:excitatory synapse assembly; ISS:UniProtKB. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:ParkinsonsUK-UCL. DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central. DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB. DR GO; GO:0007405; P:neuroblast proliferation; ISS:UniProtKB. DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central. DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ParkinsonsUK-UCL. DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB. DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB. DR GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB. DR GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB. DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB. DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central. DR Gene3D; 2.130.10.10; -; 1. DR Gene3D; 2.60.40.10; -; 3. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR002909; IPT_dom. DR InterPro; IPR031148; Plexin. DR InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom. DR InterPro; IPR002165; Plexin_repeat. DR InterPro; IPR016201; PSI. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR001627; Semap_dom. DR InterPro; IPR036352; Semap_dom_sf. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR PANTHER; PTHR22625; PTHR22625; 1. DR Pfam; PF08337; Plexin_cytopl; 1. DR Pfam; PF01437; PSI; 1. DR Pfam; PF01403; Sema; 1. DR Pfam; PF01833; TIG; 3. DR SMART; SM00429; IPT; 3. DR SMART; SM00423; PSI; 3. DR SMART; SM00630; Sema; 1. DR SUPFAM; SSF101912; SSF101912; 1. DR SUPFAM; SSF48350; SSF48350; 1. DR SUPFAM; SSF81296; SSF81296; 3. DR PROSITE; PS51004; SEMA; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Developmental protein; KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; KW Receptor; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 1838 Plexin-B2. FT /FTId=PRO_0000024673. FT TOPO_DOM 20 1197 Extracellular. {ECO:0000255}. FT TRANSMEM 1198 1218 Helical. {ECO:0000255}. FT TOPO_DOM 1219 1838 Cytoplasmic. {ECO:0000255}. FT DOMAIN 20 466 Sema. {ECO:0000255|PROSITE- FT ProRule:PRU00352}. FT DOMAIN 803 893 IPT/TIG 1. FT DOMAIN 895 980 IPT/TIG 2. FT DOMAIN 983 1092 IPT/TIG 3. FT SITE 1164 1165 Cleavage; by proprotein convertases. FT MOD_RES 1236 1236 Phosphoserine. FT {ECO:0000250|UniProtKB:B2RXS4}. FT MOD_RES 1244 1244 Phosphoserine. FT {ECO:0000250|UniProtKB:B2RXS4}. FT MOD_RES 1570 1570 Phosphoserine. FT {ECO:0000250|UniProtKB:B2RXS4}. FT CARBOHYD 127 127 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19349973}. FT CARBOHYD 242 242 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 391 391 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 402 402 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 528 528 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 733 733 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 759 759 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 795 795 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 844 844 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1002 1002 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1049 1049 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1068 1068 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1099 1099 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 78 87 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 112 120 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 250 364 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 266 312 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 330 351 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 469 486 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 475 518 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 478 495 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 489 501 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 555 574 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT VARIANT 318 318 K -> E (in dbSNP:rs28379706). FT {ECO:0000244|PubMed:24275569}. FT /FTId=VAR_050600. FT VARIANT 823 823 I -> V (in dbSNP:rs11547731). FT /FTId=VAR_061537. FT MUTAGEN 1161 1164 RQKR->AQKA: Abolishes cleavage by FT proprotein convertases. FT {ECO:0000269|PubMed:12533544}. FT CONFLICT 1535 1535 R -> Q (in Ref. 3; AAH04542 and 4; FT AAP35533). {ECO:0000305}. FT STRAND 1462 1469 {ECO:0000244|PDB:4E71}. FT STRAND 1477 1482 {ECO:0000244|PDB:4E71}. FT HELIX 1487 1498 {ECO:0000244|PDB:4E71}. FT STRAND 1512 1517 {ECO:0000244|PDB:4E71}. FT HELIX 1545 1548 {ECO:0000244|PDB:4E71}. FT STRAND 1555 1560 {ECO:0000244|PDB:4E71}. SQ SEQUENCE 1838 AA; 205127 MW; 4AE43003828BC769 CRC64; MALQLWALTL LGLLGAGASL RPRKLDFFRS EKELNHLAVD EASGVVYLGA VNALYQLDAK LQLEQQVATG PALDNKKCTP PIEASQCHEA EMTDNVNQLL LLDPPRKRLV ECGSLFKGIC ALRALSNISL RLFYEDGSGE KSFVASNDEG VATVGLVSST GPGGDRVLFV GKGNGPHDNG IIVSTRLLDR TDSREAFEAY TDHATYKAGY LSTNTQQFVA AFEDGPYVFF VFNQQDKHPA RNRTLLARMC REDPNYYSYL EMDLQCRDPD IHAAAFGTCL AASVAAPGSG RVLYAVFSRD SRSSGGPGAG LCLFPLDKVH AKMEANRNAC YTGTREARDI FYKPFHGDIQ CGGHAPGSSK SFPCGSEHLP YPLGSRDGLR GTAVLQRGGL NLTAVTVAAE NNHTVAFLGT SDGRILKVYL TPDGTSSEYD SILVEINKRV KRDLVLSGDL GSLYAMTQDK VFRLPVQECL SYPTCTQCRD SQDPYCGWCV VEGRCTRKAE CPRAEEASHW LWSRSKSCVA VTSAQPQNMS RRAQGEVQLT VSPLPALSEE DELLCLFGES PPHPARVEGE AVICNSPSSI PVTPPGQDHV AVTIQLLLRR GNIFLTSYQY PFYDCRQAMS LEENLPCISC VSNRWTCQWD LRYHECREAS PNPEDGIVRA HMEDSCPQFL GPSPLVIPMN HETDVNFQGK NLDTVKGSSL HVGSDLLKFM EPVTMQESGT FAFRTPKLSH DANETLPLHL YVKSYGKNID SKLHVTLYNC SFGRSDCSLC RAANPDYRCA WCGGQSRCVY EALCNTTSEC PPPVITRIQP ETGPLGGGIR ITILGSNLGV QAGDIQRISV AGRNCSFQPE RYSVSTRIVC VIEAAETPFT GGVEVDVFGK LGRSPPNVQF TFQQPKPLSV EPQQGPQAGG TTLTIHGTHL DTGSQEDVRV TLNGVPCKVT KFGAQLQCVT GPQATRGQML LEVSYGGSPV PNPGIFFTYR ENPVLRAFEP LRSFASGGRS INVTGQGFSL IQRFAMVVIA EPLQSWQPPR EAESLQPMTV VGTDYVFHND TKVVFLSPAV PEEPEAYNLT VLIEMDGHRA LLRTEAGAFE YVPDPTFENF TGGVKKQVNK LIHARGTNLN KAMTLQEAEA FVGAERCTMK TLTETDLYCE PPEVQPPPKR RQKRDTTHNL PEFIVKFGSR EWVLGRVEYD TRVSDVPLSL ILPLVIVPMV VVIAVSVYCY WRKSQQAERE YEKIKSQLEG LEESVRDRCK KEFTDLMIEM EDQTNDVHEA GIPVLDYKTY TDRVFFLPSK DGDKDVMITG KLDIPEPRRP VVEQALYQFS NLLNSKSFLI NFIHTLENQR EFSARAKVYF ASLLTVALHG KLEYYTDIMH TLFLELLEQY VVAKNPKLML RRSETVVERM LSNWMSICLY QYLKDSAGEP LYKLFKAIKH QVEKGPVDAV QKKAKYTLND TGLLGDDVEY APLTVSVIVQ DEGVDAIPVK VLNCDTISQV KEKIIDQVYR GQPCSCWPRP DSVVLEWRPG STAQILSDLD LTSQREGRWK RVNTLMHYNV RDGATLILSK VGVSQQPEDS QQDLPGERHA LLEEENRVWH LVRPTDEVDE GKSKRGSVKE KERTKAITEI YLTRLLSVKG TLQQFVDNFF QSVLAPGHAV PPAVKYFFDF LDEQAEKHNI QDEDTIHIWK TNSLPLRFWV NILKNPHFIF DVHVHEVVDA SLSVIAQTFM DACTRTEHKL SRDSPSNKLL YAKEISTYKK MVEDYYKGIR QMVQVSDQDM NTHLAEISRA HTDSLNTLVA LHQLYQYTQK YYDEIINALE EDPAAQKMQL AFRLQQIAAA LENKVTDL //