PLXB3_HUMAN
ID PLXB3_HUMAN Reviewed; 1909 AA.
AC Q9ULL4; B7Z3E6; F5H773; Q9HDA4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Plexin-B3;
DE Flags: Precursor;
GN Name=PLXNB3; Synonyms=KIAA1206, PLXN6;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Veske A., Michelson P., Finckh U., Gal A.;
RT "Cloning and characterization of the new human plexin family member, plexin
RT related protein.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ILE-598;
RP ASP-1156 AND THR-1535.
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15218527; DOI=10.1038/sj.embor.7400189;
RA Artigiani S., Conrotto P., Fazzari P., Gilestro G.F., Barberis D.,
RA Giordano S., Comoglio P.M., Tamagnone L.;
RT "Plexin-B3 is a functional receptor for semaphorin 5A.";
RL EMBO Rep. 5:710-714(2004).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16122393; DOI=10.1186/1471-2202-6-53;
RA Hartwig C., Veske A., Krejcova S., Rosenberger G., Finckh U.;
RT "Plexin B3 promotes neurite outgrowth, interacts homophilically, and
RT interacts with Rin.";
RL BMC Neurosci. 6:53-53(2005).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20696765; DOI=10.1074/jbc.m110.120451;
RA Li X., Lee A.Y.;
RT "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through
RT RhoGDIalpha-mediated inactivation of Rac1 GTPase.";
RL J. Biol. Chem. 285:32436-32445(2010).
RN [9]
RP FUNCTION, INTERACTION WITH FSCN1, AND TISSUE SPECIFICITY.
RX PubMed=21706053; DOI=10.1038/onc.2011.256;
RA Li X., Law J.W., Lee A.Y.;
RT "Semaphorin 5A and plexin-B3 regulate human glioma cell motility and
RT morphology through Rac1 and the actin cytoskeleton.";
RL Oncogene 31:595-610(2012).
RN [10]
RP VARIANT GLN-550.
RX PubMed=28119487; DOI=10.1136/jmedgenet-2016-104468;
RA Lehalle D., Mosca-Boidron A.L., Begtrup A., Boute-Benejean O., Charles P.,
RA Cho M.T., Clarkson A., Devinsky O., Duffourd Y., Duplomb-Jego L.,
RA Gerard B., Jacquette A., Kuentz P., Masurel-Paulet A., McDougall C.,
RA Moutton S., Olivie H., Park S.M., Rauch A., Revencu N., Riviere J.B.,
RA Rubin K., Simonic I., Shears D.J., Smol T., Taylor Tavares A.L., Terhal P.,
RA Thevenon J., Van Gassen K., Vincent-Delorme C., Willemsen M.H.,
RA Wilson G.N., Zackai E., Zweier C., Callier P., Thauvin-Robinet C.,
RA Faivre L.;
RT "STAG1 mutations cause a novel cohesinopathy characterised by unspecific
RT syndromic intellectual disability.";
RL J. Med. Genet. 54:479-488(2017).
CC -!- FUNCTION: Receptor for SEMA5A that plays a role in axon guidance,
CC invasive growth and cell migration. Stimulates neurite outgrowth and
CC mediates Ca(2+)/Mg(2+)-dependent cell aggregation. In glioma cells,
CC SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin
CC stress fibers, disruption of focal adhesions and cellular collapse as
CC well as inhibition of cell migration and invasion through ARHGDIA-
CC mediated inactivation of RAC1. {ECO:0000269|PubMed:15218527,
CC ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:21706053}.
CC -!- SUBUNIT: Interacts (via cytoplasmic domain) with RAC1 and ARHGDIA (By
CC similarity). Binds MET and MST1R. Interacts (via cytoplasmic domain)
CC with FSCN1. Interacts with RIT2/RIN. May form homodimers (via Sema
CC domain). {ECO:0000250, ECO:0000269|PubMed:15184888,
CC ECO:0000269|PubMed:16122393, ECO:0000269|PubMed:21706053}.
CC -!- INTERACTION:
CC Q9ULL4; Q16658: FSCN1; NbExp=2; IntAct=EBI-311073, EBI-351076;
CC Q9ULL4; P08581: MET; NbExp=2; IntAct=EBI-311073, EBI-1039152;
CC Q9ULL4; Q04912: MST1R; NbExp=2; IntAct=EBI-311073, EBI-2637518;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15218527,
CC ECO:0000269|PubMed:16122393}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:15218527, ECO:0000269|PubMed:16122393}.
CC Note=Colocalizes with RIT2/RIN at the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULL4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULL4-2; Sequence=VSP_044467;
CC -!- TISSUE SPECIFICITY: Expression detected in Purkinje and granular cells
CC in cerebellum, and in brain neocortex but not in corpus callosum.
CC Expressed in glioma cells and embryonic kidney cells (at protein
CC level). Expressed in brain, liver, pancreas and placenta, with weak
CC expression detected also in lung and kidney. Expressed in several
CC glioma cell lines. {ECO:0000269|PubMed:16122393,
CC ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:21706053}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86520.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF149019; AAG01376.1; -; mRNA.
DR EMBL; AB033032; BAA86520.1; ALT_INIT; mRNA.
DR EMBL; AK295762; BAH12182.1; -; mRNA.
DR EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14729.1; -. [Q9ULL4-1]
DR CCDS; CCDS55536.1; -. [Q9ULL4-2]
DR RefSeq; NP_001156729.1; NM_001163257.1. [Q9ULL4-2]
DR RefSeq; NP_005384.2; NM_005393.2. [Q9ULL4-1]
DR AlphaFoldDB; Q9ULL4; -.
DR SMR; Q9ULL4; -.
DR BioGRID; 111378; 12.
DR IntAct; Q9ULL4; 11.
DR MINT; Q9ULL4; -.
DR STRING; 9606.ENSP00000442736; -.
DR GlyConnect; 1614; 1 N-Linked glycan (1 site).
DR GlyGen; Q9ULL4; 8 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9ULL4; -.
DR PhosphoSitePlus; Q9ULL4; -.
DR BioMuta; PLXNB3; -.
DR DMDM; 51701857; -.
DR EPD; Q9ULL4; -.
DR jPOST; Q9ULL4; -.
DR MassIVE; Q9ULL4; -.
DR PaxDb; Q9ULL4; -.
DR PeptideAtlas; Q9ULL4; -.
DR PRIDE; Q9ULL4; -.
DR ProteomicsDB; 27401; -.
DR ProteomicsDB; 85069; -. [Q9ULL4-1]
DR Antibodypedia; 369; 100 antibodies from 15 providers.
DR DNASU; 5365; -.
DR Ensembl; ENST00000361971.10; ENSP00000355378.5; ENSG00000198753.12. [Q9ULL4-1]
DR Ensembl; ENST00000538966.5; ENSP00000442736.1; ENSG00000198753.12. [Q9ULL4-2]
DR GeneID; 5365; -.
DR KEGG; hsa:5365; -.
DR MANE-Select; ENST00000361971.10; ENSP00000355378.5; NM_005393.3; NP_005384.2.
DR UCSC; uc004fii.3; human. [Q9ULL4-1]
DR CTD; 5365; -.
DR DisGeNET; 5365; -.
DR GeneCards; PLXNB3; -.
DR HGNC; HGNC:9105; PLXNB3.
DR HPA; ENSG00000198753; Tissue enriched (brain).
DR MIM; 300214; gene.
DR neXtProt; NX_Q9ULL4; -.
DR OpenTargets; ENSG00000198753; -.
DR PharmGKB; PA33431; -.
DR VEuPathDB; HostDB:ENSG00000198753; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_1_1_1; -.
DR InParanoid; Q9ULL4; -.
DR OMA; CPSGENI; -.
DR PhylomeDB; Q9ULL4; -.
DR TreeFam; TF312962; -.
DR PathwayCommons; Q9ULL4; -.
DR Reactome; R-HSA-416700; Other semaphorin interactions.
DR SignaLink; Q9ULL4; -.
DR SIGNOR; Q9ULL4; -.
DR BioGRID-ORCS; 5365; 10 hits in 691 CRISPR screens.
DR ChiTaRS; PLXNB3; human.
DR GeneWiki; PLXNB3; -.
DR GenomeRNAi; 5365; -.
DR Pharos; Q9ULL4; Tbio.
DR PRO; PR:Q9ULL4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9ULL4; protein.
DR Bgee; ENSG00000198753; Expressed in C1 segment of cervical spinal cord and 93 other tissues.
DR ExpressionAtlas; Q9ULL4; baseline and differential.
DR Genevisible; Q9ULL4; HS.
DR GO; GO:0009986; C:cell surface; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IPI:ParkinsonsUK-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; IEA:Ensembl.
DR GO; GO:0017154; F:semaphorin receptor activity; IDA:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; IDA: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; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0010593; P:negative regulation of lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB.
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; IBA:GO_Central.
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 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; 4.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Neurogenesis; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..1909
FT /note="Plexin-B3"
FT /id="PRO_0000024674"
FT TOPO_DOM 45..1255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1256..1276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1277..1909
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..471
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 473..526
FT /note="PSI 1"
FT DOMAIN 620..682
FT /note="PSI 2"
FT DOMAIN 787..833
FT /note="PSI 3"
FT DOMAIN 835..925
FT /note="IPT/TIG 1"
FT DOMAIN 927..1012
FT /note="IPT/TIG 2"
FT DOMAIN 1015..1145
FT /note="IPT/TIG 3"
FT DOMAIN 1159..1244
FT /note="IPT/TIG 4"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 132..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 267..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 283..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 333..357
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 474..491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 480..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 483..500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 494..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 562..580
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VAR_SEQ 1..15
FT /note="MCHAAQETPLLHHFM -> MELTPASSLTCSLLSPRLPGSFPQLRRVPPCSR
FT PWLPK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044467"
FT VARIANT 126
FT /note="A -> T (in dbSNP:rs34360382)"
FT /id="VAR_050601"
FT VARIANT 550
FT /note="R -> Q (in dbSNP:rs782213788)"
FT /evidence="ECO:0000269|PubMed:28119487"
FT /id="VAR_079495"
FT VARIANT 598
FT /note="V -> I (in dbSNP:rs2266879)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_019681"
FT VARIANT 1156
FT /note="E -> D (in dbSNP:rs6643791)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_061538"
FT VARIANT 1535
FT /note="M -> T (in dbSNP:rs5987155)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_019682"
FT VARIANT 1651
FT /note="E -> A (in dbSNP:rs34762690)"
FT /id="VAR_068807"
FT CONFLICT 149
FT /note="A -> V (in Ref. 3; BAH12182)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="L -> P (in Ref. 3; BAH12182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1909 AA; 206847 MW; 11753CD58C7AC226 CRC64;
MCHAAQETPL LHHFMAPVMA RWPPFGLCLL LLLLSPPPLP LTGAHRFSAP NTTLNHLALA
PGRGTLYVGA VNRLFQLSPE LQLEAVAVTG PVIDSPDCVP FRDPAECPQA QLTDNANQLL
LVSSRAQELV ACGQVRQGVC ETRRLGDVAE VLYQAEDPGD GQFVAANTPG VATVGLVVPL
PGRDLLLVAR GLAGKLSAGV PPLAIRQLAG SQPFSSEGLG RLVVGDFSDY NNSYVGAFAD
ARSAYFVFRR RGARAQAEYR SYVARVCLGD TNLYSYVEVP LACQGQGLIQ AAFLAPGTLL
GVFAAGPRGT QAALCAFPMV ELGASMEQAR RLCYTAGGRG PSGAEEATVE YGVTSRCVTL
PLDSPESYPC GDEHTPSPIA GRQPLEVQPL LKLGQPVSAV AALQADGHMI AFLGDTQGQL
YKVFLHGSQG QVYHSQQVGP PGSAISPDLL LDSSGSHLYV LTAHQVDRIP VAACPQFPDC
ASCLQAQDPL CGWCVLQGRC TRKGQCGRAG QLNQWLWSYE EDSHCLHIQS LLPGHHPRQE
QGQVTLSVPR LPILDADEYF HCAFGDYDSL AHVEGPHVAC VTPPQDQVPL NPPGTDHVTV
PLALMFEDVT VAATNFSFYD CSAVQALEAA APCRACVGSI WRCHWCPQSS HCVYGEHCPE
GERTIYSAQE VDIQVRGPGA CPQVEGLAGP HLVPVGWESH LALRVRNLQH FRGLPASFHC
WLELPGELRG LPATLEETAG DSGLIHCQAH QFYPSMSQRE LPVPIYVTQG EAQRLDNTHA
LYVILYDCAM GHPDCSHCQA ANRSLGCLWC ADGQPACRYG PLCPPGAVEL LCPAPSIDAV
EPLTGPPEGG LALTILGSNL GRAFADVQYA VSVASRPCNP EPSLYRTSAR IVCVTSPAPN
GTTGPVRVAI KSQPPGISSQ HFTYQDPVLL SLSPRWGPQA GGTQLTIRGQ HLQTGGNTSA
FVGGQPCPIL EPVCPEAIVC RTRPQAAPGE AAVLVVFGHA QRTLLASPFR YTANPQLVAA
EPSASFRGGG RLIRVRGTGL DVVQRPLLSV WLEADAEVQA SRAQPQDPQP RRSCGAPAAD
PQACIQLGGG LLQCSTVCSV NSSSLLLCRS PAVPDRAHPQ RVFFTLDNVQ VDFASASGGQ
GFLYQPNPRL APLSREGPAR PYRLKPGHVL DVEGEGLNLG ISKEEVRVHI GRGECLVKTL
TRTHLYCEPP AHAPQPANGS GLPQFVVQMG NVQLALGPVQ YEAEPPLSAF PVEAQAGVGM
GAAVLIAAVL LLTLMYRHKS KQALRDYQKV LVQLESLETG VGDQCRKEFT DLMTEMTDLS
SDLEGSGIPF LDYRTYAERA FFPGHGGCPL QPKPEGPGED GHCATVRQGL TQLSNLLNSK
LFLLTLIHTL EEQPSFSQRD RCHVASLLSL ALHGKLEYLT DIMRTLLGDL AAHYVHRNPK
LMLRRTETMV EKLLTNWLSI CLYAFLREVA GEPLYMLFRA IQYQVDKGPV DAVTGKAKRT
LNDSRLLRED VEFQPLTLMV LVGPGAGGAA GSSEMQRVPA RVLDTDTITQ VKEKVLDQVY
KGTPFSQRPS VHALDLEWRS GLAGHLTLSD EDLTSVTQNH WKRLNTLQHY KVPDGATVGL
VPQLHRGSTI SQSLAQRCPL GENIPTLEDG EEGGVCLWHL VKATEEPEGA KVRCSSLRER
EPARAKAIPE IYLTRLLSMK GTLQKFVDDT FQAILSVNRP IPIAVKYLFD LLDELAEKHG
IEDPGTLHIW KTNSLLLRFW VNALKNPQLI FDVRVSDNVD AILAVIAQTF IDSCTTSEHK
VGRDSPVNKL LYAREIPRYK QMVERYYADI RQSSPASYQE MNSALAELSG NYTSAPHCLE
ALQELYNHIH RYYDQIISAL EEDPVGQKLQ LACRLQQVAA LVENKVTDL
