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   24-JAN-2024, entry version 179.
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; 13.
DR   MINT; Q9ULL4; -.
DR   STRING; 9606.ENSP00000442736; -.
DR   GlyConnect; 1614; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q9ULL4; 8 sites, 1 glycan.
DR   GlyGen; Q9ULL4; 8 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q9ULL4; -.
DR   PhosphoSitePlus; Q9ULL4; -.
DR   SwissPalm; Q9ULL4; -.
DR   BioMuta; PLXNB3; -.
DR   DMDM; 51701857; -.
DR   EPD; Q9ULL4; -.
DR   jPOST; Q9ULL4; -.
DR   MassIVE; Q9ULL4; -.
DR   PaxDb; 9606-ENSP00000442736; -.
DR   PeptideAtlas; Q9ULL4; -.
DR   ProteomicsDB; 27401; -.
DR   ProteomicsDB; 85069; -. [Q9ULL4-1]
DR   Antibodypedia; 369; 122 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   AGR; HGNC:9105; -.
DR   CTD; 5365; -.
DR   DisGeNET; 5365; -.
DR   GeneCards; PLXNB3; -.
DR   HGNC; HGNC:9105; PLXNB3.
DR   HPA; ENSG00000198753; Tissue enhanced (brain, intestine).
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; LCYTTGG; -.
DR   OrthoDB; 1387371at2759; -.
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 767 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 94 other cell types or tissues.
DR   ExpressionAtlas; Q9ULL4; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:ParkinsonsUK-UCL.
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:0008360; P:regulation of cell shape; 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   CDD; cd01180; IPT_plexin_repeat1; 1.
DR   CDD; cd01179; IPT_plexin_repeat2; 1.
DR   CDD; cd12791; RasGAP_plexin_B3; 1.
DR   CDD; cd11277; Sema_plexin_B3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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; IPR046800; Plexin_RBD.
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; PLEXIN; 1.
DR   PANTHER; PTHR22625:SF33; PLEXIN-B3; 1.
DR   Pfam; PF08337; Plexin_cytopl; 1.
DR   Pfam; PF20170; Plexin_RBD; 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; SSF81296; E set domains; 4.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF103575; Plexin repeat; 1.
DR   SUPFAM; SSF101912; Sema domain; 1.
DR   PROSITE; PS51004; SEMA; 1.
DR   Genevisible; Q9ULL4; HS.
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
//