ID PLXB1_HUMAN Reviewed; 2135 AA. AC O43157; A6H8Y2; Q6NY20; Q9UIV7; Q9UJ92; Q9UJ93; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 3. DT 13-FEB-2019, entry version 172. DE RecName: Full=Plexin-B1; DE AltName: Full=Semaphorin receptor SEP; DE Flags: Precursor; GN Name=PLXNB1; Synonyms=KIAA0407, PLXN5, SEP; 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] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9455477; DOI=10.1093/dnares/4.5.307; RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VIII. RT 78 new cDNA clones from brain which code for large proteins in RT vitro."; RL DNA Res. 4:307-313(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PHOSPHORYLATION, RP SUBCELLULAR LOCATION, AND INTERACTION WITH SEMA4D; NRP1 AND NRP2. RC TISSUE=Gastric carcinoma; RX PubMed=10520995; DOI=10.1016/S0092-8674(00)80063-X; RA Tamagnone L., Artigiani S., Chen H., He Z., Ming G.-L., Song H.-L., RA Chedotal A., Winberg M.L., Goodman C.S., Poo M.-M., RA Tessier-Lavigne M., Comoglio P.M.; RT "Plexins are a large family of receptors for transmembrane, secreted RT and GPI-anchored semaphorins in vertebrates."; RL Cell 99:71-80(1999). RN [3] RP ERRATUM. RA Tamagnone L., Artigiani S., Chen H., He Z., Ming G.-L., Song H.-L., RA Chedotal A., Winberg M.L., Goodman C.S., Poo M.-M., RA Tessier-Lavigne M., Comoglio P.M.; RL Cell 104:321-321(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=8570614; DOI=10.1073/pnas.93.2.674; RA Maestrini E., Tamagnone L., Longati P., Cremona O., Gulisano M., RA Bione S., Tamanini F., Neel B.G., Toniolo D., Comoglio P.M.; RT "A family of transmembrane proteins with homology to the MET- RT hepatocyte growth factor receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 93:674-678(1996). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [7] RP INTERACTION WITH RAC1. RX PubMed=11035813; DOI=10.1073/pnas.220421797; RA Vikis H.G., Li W., He Z., Guan K.-L.; RT "The semaphorin receptor plexin-B1 specifically interacts with active RT Rac in a ligand-dependent manner."; RL Proc. Natl. Acad. Sci. U.S.A. 97:12457-12462(2000). RN [8] RP INTERACTION WITH SEMA4D AND MET, AND FUNCTION. RX PubMed=12198496; DOI=10.1038/ncb843; RA Giordano S., Corso S., Conrotto P., Artigiani S., Gilestro G., RA Barberis D., Tamagnone L., Comoglio P.M.; RT "The semaphorin 4D receptor controls invasive growth by coupling with RT Met."; RL Nat. Cell Biol. 4:720-724(2002). RN [9] RP INTERACTION WITH ARHGEF11 AND ARHGEF12, AND FUNCTION. RX PubMed=12196628; DOI=10.1073/pnas.142433199; RA Aurandt J., Vikis H.G., Gutkind J.S., Ahn N., Guan K.-L.; RT "The semaphorin receptor plexin-B1 signals through a direct RT interaction with the Rho-specific nucleotide exchange factor, LARG."; RL Proc. Natl. Acad. Sci. U.S.A. 99:12085-12090(2002). RN [10] RP HETERODIMERIZATION WITH PLXNB2, MUTAGENESIS OF 1302-ARG--ARG-1305, RP 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 [11] RP INTERACTION WITH RND1. RX PubMed=12730235; DOI=10.1074/jbc.M303047200; RA Oinuma I., Katoh H., Harada A., Negishi M.; RT "Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF- RT mediated Rho activation by Plexin-B1 and induces cell contraction in RT COS-7 cells."; RL J. Biol. Chem. 278:25671-25677(2003). RN [12] RP INTERACTION WITH ERBB2, PHOSPHORYLATION, AND FUNCTION. RX PubMed=15210733; DOI=10.1083/jcb.200312094; RA Swiercz J.M., Kuner R., Offermanns S.; RT "Plexin-B1/RhoGEF-mediated RhoA activation involves the receptor RT tyrosine kinase ErbB-2."; RL J. Cell Biol. 165:869-880(2004). RN [13] RP INTERACTION WITH MET AND MST1R. 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 [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1253. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1253 AND ASN-1330. 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 [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1253. 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 [17] RP IDENTIFICATION BY MASS 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). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1743-1862, SUBUNIT, AND RP INTERACTION WITH RAC1; RND1 AND RHOD. RX PubMed=17916560; DOI=10.1074/jbc.M703800200; RA Tong Y., Chugha P., Hota P.K., Alviani R.S., Li M., Tempel W., RA Shen L., Park H.W., Buck M.; RT "Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction RT motif destabilizes dimerization of the plexin-B1 effector domain."; RL J. Biol. Chem. 282:37215-37224(2007). RN [19] RP STRUCTURE BY NMR OF 2128-2135 IN COMPLEX WITH ARHGEF12, AND SUBUNIT. RX PubMed=18411422; DOI=10.1110/ps.073416508; RA Liu J., Zhang J., Yang Y., Huang H., Shen W., Hu Q., Wang X., Wu J., RA Shi Y.; RT "Conformational change upon ligand binding and dynamics of the PDZ RT domain from leukemia-associated Rho guanine nucleotide exchange RT factor."; RL Protein Sci. 17:1003-1014(2008). RN [20] RP STRUCTURE BY NMR OF 1743-1862, MUTAGENESIS OF LEU-1815, SUBUNIT, AND RP INTERACTION WITH RAC1 AND RND1. RX PubMed=18275816; DOI=10.1016/j.str.2007.12.012; RA Tong Y., Hota P.K., Hamaneh M.B., Buck M.; RT "Insights into oncogenic mutations of plexin-B1 based on the solution RT structure of the Rho GTPase binding domain."; RL Structure 16:246-258(2008). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1511-2135 IN COMPLEX WITH RP RND1, FUNCTION, SUBUNIT, INTERACTION WITH SEMA4D; RND1; RAC1 AND RRAS, RP AND MUTAGENESIS OF 1884-TRP-HIS-1885. RX PubMed=19843518; DOI=10.1074/jbc.M109.056275; RA Tong Y., Hota P.K., Penachioni J.Y., Hamaneh M.B., Kim S., RA Alviani R.S., Shen L., He H., Tempel W., Tamagnone L., Park H.W., RA Buck M.; RT "Structure and function of the intracellular region of the plexin-B1 RT transmembrane receptor."; RL J. Biol. Chem. 284:35962-35972(2009). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 20-535 IN COMPLEX WITH RP SEMA4D, FUNCTION, SUBUNIT, MUTAGENESIS OF ASP-139, GLYCOSYLATION AT RP ASN-334, AND DISULFIDE BONDS. RX PubMed=20877282; DOI=10.1038/nature09468; RA Janssen B.J., Robinson R.A., Perez-Branguli F., Bell C.H., RA Mitchell K.J., Siebold C., Jones E.Y.; RT "Structural basis of semaphorin-plexin signalling."; RL Nature 467:1118-1122(2010). RN [23] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1533-2135 IN COMPLEX WITH RP RAC1, SUBUNIT, AND FUNCTION. RX PubMed=21912513; DOI=10.1371/journal.pbio.1001134; RA Bell C.H., Aricescu A.R., Jones E.Y., Siebold C.; RT "A dual binding mode for RhoGTPases in plexin signalling."; RL PLoS Biol. 9:E1001134-E1001134(2011). RN [24] RP VARIANT [LARGE SCALE ANALYSIS] VAL-1891. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Receptor for SEMA4D (PubMed:19843518, PubMed:20877282, CC PubMed:21912513). Plays a role in GABAergic synapse development CC (By similarity). Mediates SEMA4A- and SEMA4D-dependent inhibitory CC synapse development (By similarity). Plays a role in RHOA CC activation and subsequent changes of the actin cytoskeleton CC (PubMed:12196628, PubMed:15210733). Plays a role in axon guidance, CC invasive growth and cell migration (PubMed:12198496). CC {ECO:0000250|UniProtKB:Q8CJH3, ECO:0000269|PubMed:12196628, CC ECO:0000269|PubMed:12198496, ECO:0000269|PubMed:15210733, CC ECO:0000269|PubMed:19843518, ECO:0000269|PubMed:20877282, CC ECO:0000269|PubMed:21912513}. CC -!- SUBUNIT: Monomer, and heterodimer with PLXNB2 after proteolytic CC processing (PubMed:12533544, PubMed:17916560, PubMed:18411422, CC PubMed:18275816, PubMed:19843518, PubMed:20877282, CC PubMed:21912513). Binds RAC1 that has been activated by GTP CC binding (PubMed:11035813, PubMed:17916560, PubMed:18275816, CC PubMed:19843518). Interaction with SEMA4D promotes binding of CC cytoplasmic ligands (PubMed:10520995, PubMed:12198496, CC PubMed:19843518). Interacts with PLXNA1 (By similarity). Interacts CC with ARHGEF11 and ARHGEF12 (PubMed:12196628). Interacts with ERBB2 CC (PubMed:15210733). Interacts with MET (PubMed:12198496, CC PubMed:15184888). Interacts with MST1R (PubMed:15184888). CC Interacts with RRAS (PubMed:19843518). Interacts with RHOD CC (PubMed:17916560). Interacts with RND1 (PubMed:12730235, CC PubMed:17916560, PubMed:18275816, PubMed:19843518). Interacts with CC NRP1 and NRP2 (PubMed:10520995). {ECO:0000250|UniProtKB:Q8CJH3, CC ECO:0000269|PubMed:10520995, ECO:0000269|PubMed:11035813, CC ECO:0000269|PubMed:12196628, ECO:0000269|PubMed:12198496, CC ECO:0000269|PubMed:12533544, ECO:0000269|PubMed:12730235, CC ECO:0000269|PubMed:15184888, ECO:0000269|PubMed:15210733, CC ECO:0000269|PubMed:17916560, ECO:0000269|PubMed:18275816, CC ECO:0000269|PubMed:18411422, ECO:0000269|PubMed:19843518, CC ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:21912513}. CC -!- INTERACTION: CC P08581:MET; NbExp=7; IntAct=EBI-1111488, EBI-1039152; CC Q04912:MST1R; NbExp=3; IntAct=EBI-1111488, EBI-2637518; CC Q92730:RND1; NbExp=2; IntAct=EBI-1111488, EBI-448618; CC Q92854-1:SEMA4D; NbExp=3; IntAct=EBI-15880891, EBI-15880903; CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane CC {ECO:0000269|PubMed:12533544}; Single-pass type I membrane protein CC {ECO:0000255}. CC -!- SUBCELLULAR LOCATION: Isoform 2: Secreted CC {ECO:0000269|PubMed:10520995}. CC -!- SUBCELLULAR LOCATION: Isoform 3: Secreted CC {ECO:0000269|PubMed:10520995}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O43157-1; Sequence=Displayed; CC Name=2; Synonyms=Isoform R; CC IsoId=O43157-2; Sequence=VSP_011514; CC Name=3; CC IsoId=O43157-3; Sequence=VSP_011513, VSP_011515; CC -!- TISSUE SPECIFICITY: Highly expressed in fetal kidney, and at CC slightly lower levels in fetal brain, lung and liver. CC {ECO:0000269|PubMed:8570614}. CC -!- PTM: Phosphorylated on tyrosine residues by ERBB2 and MET upon CC SEMA4D binding. {ECO:0000269|PubMed:10520995, CC ECO:0000269|PubMed:15210733}. CC -!- PTM: Proteolytic processing favors heterodimerization with PLXNB2 CC and SEMA4D binding. {ECO:0000269|PubMed:12533544}. CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA23703.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/PLXNB1ID43413ch3p21.html"; 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; AB007867; BAA23703.2; ALT_INIT; mRNA. DR EMBL; AJ011414; CAB56221.1; -; mRNA. DR EMBL; AJ011415; CAB56222.1; -; mRNA. DR EMBL; X87904; CAB57277.1; -; mRNA. DR EMBL; CH471055; EAW64865.1; -; Genomic_DNA. DR EMBL; BC146793; AAI46794.1; -; mRNA. DR CCDS; CCDS2765.1; -. [O43157-1] DR RefSeq; NP_001123554.1; NM_001130082.2. [O43157-1] DR RefSeq; NP_002664.2; NM_002673.5. [O43157-1] DR RefSeq; XP_016862120.1; XM_017006631.1. [O43157-1] DR UniGene; Hs.476209; -. DR PDB; 2JPH; NMR; -; A=1743-1862. DR PDB; 2OS6; NMR; -; B=2128-2135. DR PDB; 2R2O; X-ray; 2.00 A; A/B=1743-1862. DR PDB; 2REX; X-ray; 2.30 A; A/C=1743-1862. DR PDB; 3HM6; X-ray; 2.40 A; X=1511-2135. DR PDB; 3OL2; X-ray; 2.99 A; B=20-535. DR PDB; 3SU8; X-ray; 3.20 A; X=1533-2135. DR PDB; 3SUA; X-ray; 4.39 A; D/E/F=1511-2135. DR PDB; 5B4W; X-ray; 2.60 A; A/B/C/D/E/F=20-535. DR PDBsum; 2JPH; -. DR PDBsum; 2OS6; -. DR PDBsum; 2R2O; -. DR PDBsum; 2REX; -. DR PDBsum; 3HM6; -. DR PDBsum; 3OL2; -. DR PDBsum; 3SU8; -. DR PDBsum; 3SUA; -. DR PDBsum; 5B4W; -. DR ProteinModelPortal; O43157; -. DR SMR; O43157; -. DR BioGrid; 111377; 22. DR CORUM; O43157; -. DR DIP; DIP-36742N; -. DR IntAct; O43157; 19. DR MINT; O43157; -. DR STRING; 9606.ENSP00000296440; -. DR GlyConnect; 1612; -. DR iPTMnet; O43157; -. DR PhosphoSitePlus; O43157; -. DR BioMuta; PLXNB1; -. DR EPD; O43157; -. DR jPOST; O43157; -. DR MaxQB; O43157; -. DR PaxDb; O43157; -. DR PeptideAtlas; O43157; -. DR PRIDE; O43157; -. DR ProteomicsDB; 48777; -. DR ProteomicsDB; 48778; -. [O43157-2] DR ProteomicsDB; 48779; -. [O43157-3] DR Ensembl; ENST00000296440; ENSP00000296440; ENSG00000164050. [O43157-1] DR Ensembl; ENST00000358536; ENSP00000351338; ENSG00000164050. [O43157-1] DR Ensembl; ENST00000449094; ENSP00000395987; ENSG00000164050. [O43157-3] DR Ensembl; ENST00000456774; ENSP00000414199; ENSG00000164050. [O43157-2] DR GeneID; 5364; -. DR KEGG; hsa:5364; -. DR UCSC; uc003csu.3; human. [O43157-1] DR CTD; 5364; -. DR DisGeNET; 5364; -. DR EuPathDB; HostDB:ENSG00000164050.12; -. DR GeneCards; PLXNB1; -. DR HGNC; HGNC:9103; PLXNB1. DR HPA; HPA040586; -. DR MIM; 601053; gene. DR neXtProt; NX_O43157; -. DR OpenTargets; ENSG00000164050; -. DR PharmGKB; PA33429; -. DR eggNOG; KOG3610; Eukaryota. DR eggNOG; ENOG410XR88; LUCA. DR GeneTree; ENSGT00940000154080; -. DR HOGENOM; HOG000231376; -. DR HOVERGEN; HBG053404; -. DR InParanoid; O43157; -. DR KO; K06821; -. DR OMA; GHVQYDG; -. DR OrthoDB; 90434at2759; -. DR PhylomeDB; O43157; -. DR TreeFam; TF312962; -. DR Reactome; R-HSA-416482; G alpha (12/13) signalling events. DR Reactome; R-HSA-416550; Sema4D mediated inhibition of cell attachment and migration. DR Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse. DR SIGNOR; O43157; -. DR ChiTaRS; PLXNB1; human. DR EvolutionaryTrace; O43157; -. DR GeneWiki; PLXNB1; -. DR GenomeRNAi; 5364; -. DR PRO; PR:O43157; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000164050; Expressed in 189 organ(s), highest expression level in right uterine tube. DR Genevisible; O43157; HS. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0002116; C:semaphorin receptor complex; IDA:UniProtKB. DR GO; GO:0032794; F:GTPase activating protein binding; ISS:BHF-UCL. DR GO; GO:0005096; F:GTPase activator activity; TAS:Reactome. DR GO; GO:0017154; F:semaphorin receptor activity; IDA:UniProtKB. DR GO; GO:0030215; F:semaphorin receptor binding; TAS:UniProtKB. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB. DR GO; GO:0016477; P:cell migration; NAS:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome. DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB. DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB. DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISS:BHF-UCL. DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB. DR GO; GO:0043931; P:ossification involved in bone maturation; ISS:BHF-UCL. DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central. DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB. DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB. DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB. DR GO; GO:0051493; P:regulation of cytoskeleton organization; IDA:UniProtKB. DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central. DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IDA:UniProtKB. DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central. DR GO; GO:1900220; P:semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis; ISS:BHF-UCL. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR Gene3D; 2.130.10.10; -; 1. DR Gene3D; 2.60.40.10; -; 4. 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; Alternative splicing; Cell membrane; Coiled coil; KW Complete proteome; Disulfide bond; Glycoprotein; Membrane; KW Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; KW Secreted; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 2135 Plexin-B1. FT /FTId=PRO_0000024671. FT TOPO_DOM 20 1490 Extracellular. {ECO:0000255}. FT TRANSMEM 1491 1511 Helical. {ECO:0000255}. FT TOPO_DOM 1512 2135 Cytoplasmic. {ECO:0000255}. FT DOMAIN 20 479 Sema. {ECO:0000255|PROSITE- FT ProRule:PRU00352}. FT DOMAIN 1070 1160 IPT/TIG 1. FT DOMAIN 1162 1249 IPT/TIG 2. FT DOMAIN 1252 1375 IPT/TIG 3. FT COILED 1507 1539 {ECO:0000255}. FT COMPBIAS 678 829 Pro-rich. FT COMPBIAS 1302 1305 Poly-Arg. FT SITE 1305 1306 Cleavage; by proprotein convertases. FT SITE 1815 1815 Important for interaction with RAC1 and FT RND1. FT CARBOHYD 31 31 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 334 334 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 543 543 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1183 1183 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1253 1253 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19349973}. FT CARBOHYD 1330 1330 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT DISULFID 79 88 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 111 119 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 252 377 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 268 322 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 340 364 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 482 499 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 488 533 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 491 508 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 502 514 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 570 588 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT VAR_SEQ 677 729 SPLVSPDPPARGGPSPSPPTAPKALATPAPDTLPVEPGAPS FT TATASDISPGAS -> VMETQQSLRALPPPSSSRPASTTSM FT TPPGSGSWKRRPWGQAPAPVWRAFRAPR (in isoform FT 3). {ECO:0000303|PubMed:10520995}. FT /FTId=VSP_011513. FT VAR_SEQ 688 870 Missing (in isoform 2). FT {ECO:0000303|PubMed:10520995}. FT /FTId=VSP_011514. FT VAR_SEQ 730 2135 Missing (in isoform 3). FT {ECO:0000303|PubMed:10520995}. FT /FTId=VSP_011515. FT VARIANT 389 389 R -> W (in dbSNP:rs34050056). FT /FTId=VAR_050598. FT VARIANT 753 753 S -> L (in dbSNP:rs35592743). FT /FTId=VAR_050599. FT VARIANT 1891 1891 D -> V (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036074. FT MUTAGEN 139 139 D->K: Strongly reduced interaction with FT SEMA4D. {ECO:0000269|PubMed:20877282}. FT MUTAGEN 1302 1305 RRRR->AAAA: Abolishes cleavage by FT proprotein convertases. FT {ECO:0000269|PubMed:12533544}. FT MUTAGEN 1815 1815 L->F,P: Abolishes interaction with RAC1 FT and RND1. {ECO:0000269|PubMed:18275816}. FT MUTAGEN 1884 1885 WH->SS: Loss of cytoskeleton remodeling FT in response to SEMA4D. FT {ECO:0000269|PubMed:19843518}. FT CONFLICT 1297 1297 S -> N (in Ref. 4; CAB57277). FT {ECO:0000305}. FT CONFLICT 1625 1625 S -> T (in Ref. 4; CAB57277). FT {ECO:0000305}. FT STRAND 26 28 {ECO:0000244|PDB:3OL2}. FT STRAND 35 40 {ECO:0000244|PDB:5B4W}. FT TURN 42 44 {ECO:0000244|PDB:5B4W}. FT STRAND 47 51 {ECO:0000244|PDB:5B4W}. FT STRAND 54 58 {ECO:0000244|PDB:5B4W}. FT STRAND 64 69 {ECO:0000244|PDB:5B4W}. FT STRAND 73 75 {ECO:0000244|PDB:5B4W}. FT TURN 85 87 {ECO:0000244|PDB:5B4W}. FT STRAND 92 94 {ECO:0000244|PDB:5B4W}. FT STRAND 98 103 {ECO:0000244|PDB:5B4W}. FT STRAND 105 114 {ECO:0000244|PDB:5B4W}. FT HELIX 115 117 {ECO:0000244|PDB:5B4W}. FT STRAND 119 122 {ECO:0000244|PDB:5B4W}. FT STRAND 129 132 {ECO:0000244|PDB:5B4W}. FT HELIX 139 141 {ECO:0000244|PDB:3OL2}. FT STRAND 152 158 {ECO:0000244|PDB:5B4W}. FT STRAND 164 170 {ECO:0000244|PDB:5B4W}. FT STRAND 183 190 {ECO:0000244|PDB:5B4W}. FT HELIX 194 196 {ECO:0000244|PDB:5B4W}. FT STRAND 200 205 {ECO:0000244|PDB:5B4W}. FT HELIX 211 214 {ECO:0000244|PDB:5B4W}. FT STRAND 217 224 {ECO:0000244|PDB:5B4W}. FT STRAND 227 235 {ECO:0000244|PDB:5B4W}. FT STRAND 239 241 {ECO:0000244|PDB:5B4W}. FT STRAND 244 252 {ECO:0000244|PDB:5B4W}. FT TURN 253 255 {ECO:0000244|PDB:5B4W}. FT STRAND 262 268 {ECO:0000244|PDB:5B4W}. FT TURN 269 272 {ECO:0000244|PDB:5B4W}. FT STRAND 275 281 {ECO:0000244|PDB:5B4W}. FT STRAND 291 298 {ECO:0000244|PDB:5B4W}. FT STRAND 310 313 {ECO:0000244|PDB:5B4W}. FT HELIX 314 316 {ECO:0000244|PDB:3OL2}. FT STRAND 319 325 {ECO:0000244|PDB:5B4W}. FT HELIX 326 342 {ECO:0000244|PDB:5B4W}. FT TURN 344 346 {ECO:0000244|PDB:3OL2}. FT STRAND 348 350 {ECO:0000244|PDB:3OL2}. FT STRAND 354 356 {ECO:0000244|PDB:5B4W}. FT HELIX 370 374 {ECO:0000244|PDB:5B4W}. FT STRAND 380 382 {ECO:0000244|PDB:5B4W}. FT STRAND 385 390 {ECO:0000244|PDB:5B4W}. FT STRAND 392 394 {ECO:0000244|PDB:5B4W}. FT STRAND 397 400 {ECO:0000244|PDB:5B4W}. FT STRAND 405 413 {ECO:0000244|PDB:5B4W}. FT STRAND 416 423 {ECO:0000244|PDB:5B4W}. FT STRAND 426 432 {ECO:0000244|PDB:5B4W}. FT STRAND 434 436 {ECO:0000244|PDB:3OL2}. FT STRAND 442 448 {ECO:0000244|PDB:5B4W}. FT STRAND 463 469 {ECO:0000244|PDB:5B4W}. FT STRAND 474 479 {ECO:0000244|PDB:5B4W}. FT HELIX 482 484 {ECO:0000244|PDB:5B4W}. FT HELIX 488 493 {ECO:0000244|PDB:5B4W}. FT STRAND 499 502 {ECO:0000244|PDB:5B4W}. FT TURN 503 506 {ECO:0000244|PDB:5B4W}. FT STRAND 507 510 {ECO:0000244|PDB:5B4W}. FT HELIX 511 513 {ECO:0000244|PDB:5B4W}. FT STRAND 523 526 {ECO:0000244|PDB:5B4W}. FT HELIX 1568 1576 {ECO:0000244|PDB:3HM6}. FT STRAND 1580 1582 {ECO:0000244|PDB:3SU8}. FT HELIX 1593 1595 {ECO:0000244|PDB:3HM6}. FT HELIX 1596 1610 {ECO:0000244|PDB:3HM6}. FT HELIX 1613 1625 {ECO:0000244|PDB:3HM6}. FT STRAND 1627 1629 {ECO:0000244|PDB:3SU8}. FT HELIX 1631 1644 {ECO:0000244|PDB:3HM6}. FT TURN 1645 1647 {ECO:0000244|PDB:3HM6}. FT HELIX 1649 1668 {ECO:0000244|PDB:3HM6}. FT HELIX 1672 1674 {ECO:0000244|PDB:3HM6}. FT STRAND 1677 1679 {ECO:0000244|PDB:3SU8}. FT HELIX 1682 1701 {ECO:0000244|PDB:3HM6}. FT HELIX 1704 1719 {ECO:0000244|PDB:3HM6}. FT TURN 1725 1727 {ECO:0000244|PDB:3HM6}. FT STRAND 1730 1732 {ECO:0000244|PDB:3HM6}. FT STRAND 1736 1739 {ECO:0000244|PDB:3HM6}. FT STRAND 1748 1755 {ECO:0000244|PDB:2R2O}. FT STRAND 1757 1759 {ECO:0000244|PDB:2REX}. FT STRAND 1767 1772 {ECO:0000244|PDB:2R2O}. FT HELIX 1777 1788 {ECO:0000244|PDB:2R2O}. FT TURN 1789 1791 {ECO:0000244|PDB:2R2O}. FT HELIX 1794 1796 {ECO:0000244|PDB:2R2O}. FT HELIX 1800 1802 {ECO:0000244|PDB:2R2O}. FT STRAND 1803 1808 {ECO:0000244|PDB:2R2O}. FT STRAND 1810 1812 {ECO:0000244|PDB:2R2O}. FT STRAND 1814 1817 {ECO:0000244|PDB:2R2O}. FT STRAND 1819 1821 {ECO:0000244|PDB:2R2O}. FT STRAND 1825 1827 {ECO:0000244|PDB:3SU8}. FT STRAND 1830 1832 {ECO:0000244|PDB:2R2O}. FT HELIX 1836 1839 {ECO:0000244|PDB:2R2O}. FT STRAND 1846 1851 {ECO:0000244|PDB:2R2O}. FT STRAND 1882 1887 {ECO:0000244|PDB:3HM6}. FT HELIX 1916 1941 {ECO:0000244|PDB:3HM6}. FT STRAND 1943 1945 {ECO:0000244|PDB:3HM6}. FT HELIX 1949 1964 {ECO:0000244|PDB:3HM6}. FT HELIX 1970 1980 {ECO:0000244|PDB:3HM6}. FT TURN 1981 1985 {ECO:0000244|PDB:3HM6}. FT HELIX 1986 1991 {ECO:0000244|PDB:3HM6}. FT HELIX 1993 1995 {ECO:0000244|PDB:3HM6}. FT HELIX 2003 2020 {ECO:0000244|PDB:3HM6}. FT HELIX 2033 2037 {ECO:0000244|PDB:3HM6}. FT TURN 2038 2041 {ECO:0000244|PDB:3HM6}. FT HELIX 2042 2058 {ECO:0000244|PDB:3HM6}. FT HELIX 2064 2076 {ECO:0000244|PDB:3HM6}. FT HELIX 2084 2097 {ECO:0000244|PDB:3HM6}. FT HELIX 2099 2107 {ECO:0000244|PDB:3HM6}. FT HELIX 2110 2114 {ECO:0000244|PDB:3HM6}. FT HELIX 2117 2128 {ECO:0000244|PDB:3HM6}. FT STRAND 2132 2134 {ECO:0000244|PDB:2OS6}. SQ SEQUENCE 2135 AA; 232298 MW; 12A81B68AF1D340F CRC64; MPALGPALLQ ALWAGWVLTL QPLPPTAFTP NGTYLQHLAR DPTSGTLYLG ATNFLFQLSP GLQLEATVST GPVLDSRDCL PPVMPDECPQ AQPTNNPNQL LLVSPGALVV CGSVHQGVCE QRRLGQLEQL LLRPERPGDT QYVAANDPAV STVGLVAQGL AGEPLLFVGR GYTSRGVGGG IPPITTRALW PPDPQAAFSY EETAKLAVGR LSEYSHHFVS AFARGASAYF LFLRRDLQAQ SRAFRAYVSR VCLRDQHYYS YVELPLACEG GRYGLIQAAA VATSREVAHG EVLFAAFSSA APPTVGRPPS AAAGASGASA LCAFPLDEVD RLANRTRDAC YTREGRAEDG TEVAYIEYDV NSDCAQLPVD TLDAYPCGSD HTPSPMASRV PLEATPILEW PGIQLTAVAV TMEDGHTIAF LGDSQGQLHR VYLGPGSDGH PYSTQSIQQG SAVSRDLTFD GTFEHLYVMT QSTLLKVPVA SCAQHLDCAS CLAHRDPYCG WCVLLGRCSR RSECSRGQGP EQWLWSFQPE LGCLQVAAMS PANISREETR EVFLSVPDLP PLWPGESYSC HFGEHQSPAL LTGSGVMCPS PDPSEAPVLP RGADYVSVSV ELRFGAVVIA KTSLSFYDCV AVTELRPSAQ CQACVSSRWG CNWCVWQHLC THKASCDAGP MVASHQSPLV SPDPPARGGP SPSPPTAPKA LATPAPDTLP VEPGAPSTAT ASDISPGASP SLLSPWGPWA GSGSISSPGS TGSPLHEEPS PPSPQNGPGT AVPAPTDFRP SATPEDLLAS PLSPSEVAAV PPADPGPEAL HPTVPLDLPP ATVPATTFPG AMGSVKPALD WLTREGGELP EADEWTGGDA PAFSTSTLLS GDGDSAELEG PPAPLILPSS LDYQYDTPGL WELEEATLGA SSCPCVESVQ GSTLMPVHVE REIRLLGRNL HLFQDGPGDN ECVMELEGLE VVVEARVECE PPPDTQCHVT CQQHQLSYEA LQPELRVGLF LRRAGRLRVD SAEGLHVVLY DCSVGHGDCS RCQTAMPQYG CVWCEGERPR CVTREACGEA EAVATQCPAP LIHSVEPLTG PVDGGTRVTI RGSNLGQHVQ DVLGMVTVAG VPCAVDAQEY EVSSSLVCIT GASGEEVAGA TAVEVPGRGR GVSEHDFAYQ DPKVHSIFPA RGPRAGGTRL TLNGSKLLTG RLEDIRVVVG DQPCHLLPEQ QSEQLRCETS PRPTPATLPV AVWFGATERR LQRGQFKYTL DPNITSAGPT KSFLSGGREI CVRGQNLDVV QTPRIRVTVV SRMLQPSQGL GRRRRVVPET ACSLGPSCSS QQFEEPCHVN SSQLITCRTP ALPGLPEDPW VRVEFILDNL VFDFATLNPT PFSYEADPTL QPLNPEDPTM PFRHKPGSVF SVEGENLDLA MSKEEVVAMI GDGPCVVKTL TRHHLYCEPP VEQPLPRHHA LREAPDSLPE FTVQMGNLRF SLGHVQYDGE SPGAFPVAAQ VGLGVGTSLL ALGVIIIVLM YRRKSKQALR DYKKVQIQLE NLESSVRDRC KKEFTDLMTE MTDLTSDLLG SGIPFLDYKV YAERIFFPGH RESPLHRDLG VPESRRPTVE QGLGQLSNLL NSKLFLTKFI HTLESQRTFS ARDRAYVASL LTVALHGKLE YFTDILRTLL SDLVAQYVAK NPKLMLRRTE TVVEKLLTNW MSICLYTFVR DSVGEPLYML FRGIKHQVDK GPVDSVTGKA KYTLNDNRLL REDVEYRPLT LNALLAVGPG AGEAQGVPVK VLDCDTISQA KEKMLDQLYK GVPLTQRPDP RTLDVEWRSG VAGHLILSDE DVTSEVQGLW RRLNTLQHYK VPDGATVALV PCLTKHVLRE NQDYVPGERT PMLEDVDEGG IRPWHLVKPS DEPEPPRPRR GSLRGGERER AKAIPEIYLT RLLSMKGTLQ KFVDDLFQVI LSTSRPVPLA VKYFFDLLDE QAQQHGISDQ DTIHIWKTNS LPLRFWINII KNPQFVFDVQ TSDNMDAVLL VIAQTFMDAC TLADHKLGRD SPINKLLYAR DIPRYKRMVE RYYADIRQTV PASDQEMNSV LAELSWNYSG DLGARVALHE LYKYINKYYD QIITALEEDG TAQKMQLGYR LQQIAAAVEN KVTDL //