PLXB1_HUMAN
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 03-AUG-2022, entry version 193.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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. 78
RT new cDNA clones from brain which code for large proteins in 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., Tessier-Lavigne M.,
RA Comoglio P.M.;
RT "Plexins are a large family of receptors for transmembrane, secreted and
RT GPI-anchored semaphorins in vertebrates.";
RL Cell 99:71-80(1999).
RN [3]
RP ERRATUM OF PUBMED:10520995.
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., Tessier-Lavigne M.,
RA 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., Bione S.,
RA Tamanini F., Neel B.G., Toniolo D., Comoglio P.M.;
RT "A family of transmembrane proteins with homology to the MET-hepatocyte
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 Rac
RT 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., Barberis D.,
RA 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 interaction
RT 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 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-mediated
RT Rho activation by Plexin-B1 and induces cell contraction in 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 tyrosine
RT 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 invasive
RT 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., Moore R.J.,
RA 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 multiple
RT 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-linked
RT 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT 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., Shen L.,
RA Park H.W., Buck M.;
RT "Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif
RT 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 domain
RT from leukemia-associated Rho guanine nucleotide exchange 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 RND1,
RP FUNCTION, SUBUNIT, INTERACTION WITH SEMA4D; RND1; RAC1 AND RRAS, AND
RP 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., Alviani R.S.,
RA Shen L., He H., Tempel W., Tamagnone L., Park H.W., 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 SEMA4D,
RP FUNCTION, SUBUNIT, MUTAGENESIS OF ASP-139, GLYCOSYLATION AT ASN-334, AND
RP DISULFIDE BONDS.
RX PubMed=20877282; DOI=10.1038/nature09468;
RA Janssen B.J., Robinson R.A., Perez-Branguli F., Bell C.H., Mitchell K.J.,
RA 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 RAC1,
RP 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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal 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 (By
CC similarity). Mediates SEMA4A- and SEMA4D-dependent inhibitory synapse
CC development (By similarity). Plays a role in RHOA activation and
CC subsequent changes of the actin cytoskeleton (PubMed:12196628,
CC PubMed:15210733). Plays a role in axon guidance, invasive growth and
CC cell migration (PubMed:12198496). {ECO:0000250|UniProtKB:Q8CJH3,
CC ECO:0000269|PubMed:12196628, ECO:0000269|PubMed:12198496,
CC ECO:0000269|PubMed:15210733, ECO:0000269|PubMed:19843518,
CC ECO:0000269|PubMed:20877282, 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, PubMed:21912513).
CC Binds RAC1 that has been activated by GTP binding (PubMed:11035813,
CC PubMed:17916560, PubMed:18275816, PubMed:19843518). Interaction with
CC SEMA4D promotes binding of cytoplasmic ligands (PubMed:10520995,
CC PubMed:12198496, PubMed:19843518). Interacts with PLXNA1 (By
CC similarity). Interacts with ARHGEF11 and ARHGEF12 (PubMed:12196628).
CC Interacts with ERBB2 (PubMed:15210733). Interacts with MET
CC (PubMed:12198496, PubMed:15184888). Interacts with MST1R
CC (PubMed:15184888). Interacts with RRAS (PubMed:19843518). Interacts
CC with RHOD (PubMed:17916560). Interacts with RND1 (PubMed:12730235,
CC PubMed:17916560, PubMed:18275816, PubMed:19843518). Interacts with NRP1
CC 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 O43157; P08581: MET; NbExp=7; IntAct=EBI-1111488, EBI-1039152;
CC O43157; Q04912: MST1R; NbExp=3; IntAct=EBI-1111488, EBI-2637518;
CC O43157; Q92730: RND1; NbExp=4; IntAct=EBI-1111488, EBI-448618;
CC O43157; P52198: RND2; NbExp=2; IntAct=EBI-1111488, EBI-1111436;
CC O43157; P61587: RND3; NbExp=3; IntAct=EBI-1111488, EBI-1111534;
CC O43157-1; Q92730: RND1; NbExp=2; IntAct=EBI-15880891, EBI-448618;
CC O43157-1; 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 slightly
CC lower levels in fetal brain, lung and liver.
CC {ECO:0000269|PubMed:8570614}.
CC -!- PTM: Phosphorylated on tyrosine residues by ERBB2 and MET upon SEMA4D
CC binding. {ECO:0000269|PubMed:10520995, ECO:0000269|PubMed:15210733}.
CC -!- PTM: Proteolytic processing favors heterodimerization with PLXNB2 and
CC 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=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC 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 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 AlphaFoldDB; O43157; -.
DR BMRB; O43157; -.
DR SMR; O43157; -.
DR BioGRID; 111377; 36.
DR CORUM; O43157; -.
DR DIP; DIP-36742N; -.
DR IntAct; O43157; 23.
DR MINT; O43157; -.
DR STRING; 9606.ENSP00000351338; -.
DR GlyConnect; 1612; 7 N-Linked glycans (2 sites).
DR GlyGen; O43157; 10 sites, 10 N-linked glycans (2 sites), 2 O-linked glycans (4 sites).
DR iPTMnet; O43157; -.
DR PhosphoSitePlus; O43157; -.
DR BioMuta; PLXNB1; -.
DR EPD; O43157; -.
DR jPOST; O43157; -.
DR MassIVE; O43157; -.
DR MaxQB; O43157; -.
DR PaxDb; O43157; -.
DR PeptideAtlas; O43157; -.
DR PRIDE; O43157; -.
DR ProteomicsDB; 48777; -. [O43157-1]
DR ProteomicsDB; 48778; -. [O43157-2]
DR ProteomicsDB; 48779; -. [O43157-3]
DR Antibodypedia; 49406; 286 antibodies from 31 providers.
DR DNASU; 5364; -.
DR Ensembl; ENST00000296440.11; ENSP00000296440.6; ENSG00000164050.13. [O43157-1]
DR Ensembl; ENST00000358536.8; ENSP00000351338.4; ENSG00000164050.13. [O43157-1]
DR Ensembl; ENST00000449094.5; ENSP00000395987.1; ENSG00000164050.13. [O43157-3]
DR Ensembl; ENST00000456774.5; ENSP00000414199.1; ENSG00000164050.13. [O43157-2]
DR GeneID; 5364; -.
DR KEGG; hsa:5364; -.
DR MANE-Select; ENST00000296440.11; ENSP00000296440.6; NM_001130082.3; NP_001123554.1.
DR UCSC; uc003csu.3; human. [O43157-1]
DR CTD; 5364; -.
DR DisGeNET; 5364; -.
DR GeneCards; PLXNB1; -.
DR HGNC; HGNC:9103; PLXNB1.
DR HPA; ENSG00000164050; Low tissue specificity.
DR MIM; 601053; gene.
DR neXtProt; NX_O43157; -.
DR OpenTargets; ENSG00000164050; -.
DR PharmGKB; PA33429; -.
DR VEuPathDB; HostDB:ENSG00000164050; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_1_1_1; -.
DR InParanoid; O43157; -.
DR OMA; DAFPCGS; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; O43157; -.
DR TreeFam; TF312962; -.
DR PathwayCommons; O43157; -.
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 Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR SignaLink; O43157; -.
DR SIGNOR; O43157; -.
DR BioGRID-ORCS; 5364; 14 hits in 1082 CRISPR screens.
DR ChiTaRS; PLXNB1; human.
DR EvolutionaryTrace; O43157; -.
DR GeneWiki; PLXNB1; -.
DR GenomeRNAi; 5364; -.
DR Pharos; O43157; Tbio.
DR PRO; PR:O43157; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O43157; protein.
DR Bgee; ENSG00000164050; Expressed in right uterine tube and 168 other tissues.
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:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0016477; P:cell migration; NAS:UniProtKB.
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 Gene3D; 1.10.506.10; -; 2.
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; IPR041019; TIG1_plexin.
DR InterPro; IPR041362; TIG2_plexin.
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 Pfam; PF18020; TIG_2; 1.
DR Pfam; PF17960; TIG_plexin; 1.
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 Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2135
FT /note="Plexin-B1"
FT /id="PRO_0000024671"
FT TOPO_DOM 20..1490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1491..1511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1512..2135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..479
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 1070..1160
FT /note="IPT/TIG 1"
FT DOMAIN 1162..1249
FT /note="IPT/TIG 2"
FT DOMAIN 1252..1375
FT /note="IPT/TIG 3"
FT REGION 671..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1883..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1507..1539
FT /evidence="ECO:0000255"
FT COMPBIAS 683..701
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..769
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..819
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1305..1306
FT /note="Cleavage; by proprotein convertases"
FT SITE 1815
FT /note="Important for interaction with RAC1 and RND1"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT CARBOHYD 1330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 79..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 111..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 252..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 268..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 340..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 482..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 488..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 491..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 502..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 570..588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VAR_SEQ 677..729
FT /note="SPLVSPDPPARGGPSPSPPTAPKALATPAPDTLPVEPGAPSTATASDISPGA
FT S -> VMETQQSLRALPPPSSSRPASTTSMTPPGSGSWKRRPWGQAPAPVWRAFRAPR
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10520995"
FT /id="VSP_011513"
FT VAR_SEQ 688..870
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10520995"
FT /id="VSP_011514"
FT VAR_SEQ 730..2135
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10520995"
FT /id="VSP_011515"
FT VARIANT 389
FT /note="R -> W (in dbSNP:rs34050056)"
FT /id="VAR_050598"
FT VARIANT 753
FT /note="S -> L (in dbSNP:rs35592743)"
FT /id="VAR_050599"
FT VARIANT 1891
FT /note="D -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036074"
FT MUTAGEN 139
FT /note="D->K: Strongly reduced interaction with SEMA4D."
FT /evidence="ECO:0000269|PubMed:20877282"
FT MUTAGEN 1302..1305
FT /note="RRRR->AAAA: Abolishes cleavage by proprotein
FT convertases."
FT /evidence="ECO:0000269|PubMed:12533544"
FT MUTAGEN 1815
FT /note="L->F,P: Abolishes interaction with RAC1 and RND1."
FT /evidence="ECO:0000269|PubMed:18275816"
FT MUTAGEN 1884..1885
FT /note="WH->SS: Loss of cytoskeleton remodeling in response
FT to SEMA4D."
FT /evidence="ECO:0000269|PubMed:19843518"
FT CONFLICT 1297
FT /note="S -> N (in Ref. 4; CAB57277)"
FT /evidence="ECO:0000305"
FT CONFLICT 1625
FT /note="S -> T (in Ref. 4; CAB57277)"
FT /evidence="ECO:0000305"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3OL2"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:5B4W"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5B4W"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:5B4W"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:5B4W"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3OL2"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:5B4W"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:5B4W"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:5B4W"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:5B4W"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:5B4W"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:3OL2"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:5B4W"
FT HELIX 326..342
FT /evidence="ECO:0007829|PDB:5B4W"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:3OL2"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:3OL2"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:5B4W"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 405..413
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 416..423
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:3OL2"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 463..469
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 474..479
FT /evidence="ECO:0007829|PDB:5B4W"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:5B4W"
FT HELIX 488..493
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:5B4W"
FT TURN 503..506
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:5B4W"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:5B4W"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:5B4W"
FT HELIX 1568..1576
FT /evidence="ECO:0007829|PDB:3HM6"
FT STRAND 1580..1582
FT /evidence="ECO:0007829|PDB:3SU8"
FT HELIX 1593..1595
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 1596..1610
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 1613..1625
FT /evidence="ECO:0007829|PDB:3HM6"
FT STRAND 1627..1629
FT /evidence="ECO:0007829|PDB:3SU8"
FT HELIX 1631..1644
FT /evidence="ECO:0007829|PDB:3HM6"
FT TURN 1645..1647
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 1649..1668
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 1672..1674
FT /evidence="ECO:0007829|PDB:3HM6"
FT STRAND 1677..1679
FT /evidence="ECO:0007829|PDB:3SU8"
FT HELIX 1682..1701
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 1704..1719
FT /evidence="ECO:0007829|PDB:3HM6"
FT TURN 1725..1727
FT /evidence="ECO:0007829|PDB:3HM6"
FT STRAND 1730..1732
FT /evidence="ECO:0007829|PDB:3HM6"
FT STRAND 1736..1739
FT /evidence="ECO:0007829|PDB:3HM6"
FT STRAND 1748..1755
FT /evidence="ECO:0007829|PDB:2R2O"
FT STRAND 1757..1759
FT /evidence="ECO:0007829|PDB:2REX"
FT STRAND 1767..1772
FT /evidence="ECO:0007829|PDB:2R2O"
FT HELIX 1777..1788
FT /evidence="ECO:0007829|PDB:2R2O"
FT TURN 1789..1791
FT /evidence="ECO:0007829|PDB:2R2O"
FT HELIX 1794..1796
FT /evidence="ECO:0007829|PDB:2R2O"
FT HELIX 1800..1802
FT /evidence="ECO:0007829|PDB:2R2O"
FT STRAND 1803..1808
FT /evidence="ECO:0007829|PDB:2R2O"
FT STRAND 1810..1812
FT /evidence="ECO:0007829|PDB:2R2O"
FT STRAND 1814..1817
FT /evidence="ECO:0007829|PDB:2R2O"
FT STRAND 1819..1821
FT /evidence="ECO:0007829|PDB:2R2O"
FT STRAND 1825..1827
FT /evidence="ECO:0007829|PDB:3SU8"
FT STRAND 1830..1832
FT /evidence="ECO:0007829|PDB:2R2O"
FT HELIX 1836..1839
FT /evidence="ECO:0007829|PDB:2R2O"
FT STRAND 1846..1851
FT /evidence="ECO:0007829|PDB:2R2O"
FT STRAND 1882..1887
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 1916..1941
FT /evidence="ECO:0007829|PDB:3HM6"
FT STRAND 1943..1945
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 1949..1964
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 1970..1980
FT /evidence="ECO:0007829|PDB:3HM6"
FT TURN 1981..1985
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 1986..1991
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 1993..1995
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 2003..2020
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 2033..2037
FT /evidence="ECO:0007829|PDB:3HM6"
FT TURN 2038..2041
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 2042..2058
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 2064..2076
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 2084..2097
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 2099..2107
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 2110..2114
FT /evidence="ECO:0007829|PDB:3HM6"
FT HELIX 2117..2128
FT /evidence="ECO:0007829|PDB:3HM6"
FT STRAND 2132..2134
FT /evidence="ECO:0007829|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
