PLXB3_MOUSE
ID PLXB3_MOUSE Reviewed; 1902 AA.
AC Q9QY40; A2AFF9; Q80TH8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Plexin-B3;
DE AltName: Full=Plexin-6;
DE Flags: Precursor;
GN Name=Plxnb3; Synonyms=Kiaa1206, Plxn6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A., Rosenthal A.;
RT "Comparative sequence analysis of the mouse L1cam locus and the
RT corresponding region of human Xq28.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 352-1902.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=15147296; DOI=10.1111/j.0953-816x.2004.03401.x;
RA Worzfeld T., Puschel A.W., Offermanns S., Kuner R.;
RT "Plexin-B family members demonstrate non-redundant expression patterns in
RT the developing mouse nervous system: an anatomical basis for morphogenetic
RT effects of Sema4D during development.";
RL Eur. J. Neurosci. 19:2622-2632(2004).
RN [7]
RP 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 DISRUPTION PHENOTYPE.
RX PubMed=19699796; DOI=10.1016/j.mcn.2009.08.008;
RA Worzfeld T., Rauch P., Karram K., Trotter J., Kuner R., Offermanns S.;
RT "Mice lacking Plexin-B3 display normal CNS morphology and behaviour.";
RL Mol. Cell. Neurosci. 42:372-381(2009).
RN [9]
RP FUNCTION, AND INTERACTION WITH ARHGDIA AND RAC1.
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 [10]
RP INTERACTION WITH FSCN1.
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).
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 (By similarity). Seem to be non-essential
CC for normal development and function of the central nervous system.
CC {ECO:0000250, ECO:0000269|PubMed:15218527,
CC ECO:0000269|PubMed:20696765}.
CC -!- SUBUNIT: Binds MET and MST1R. Interacts with RIT2/RIN. May form
CC homodimers (via Sema domain) (By similarity). Interacts (via
CC cytoplasmic domain) with FSCN1, ARHGDIA and RAC1. {ECO:0000250,
CC ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:21706053}.
CC -!- INTERACTION:
CC Q9QY40; Q61553: Fscn1; NbExp=3; IntAct=EBI-6271317, EBI-2308857;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Note=Colocalizes with RIT2/RIN at the
CC plasma membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level). In
CC cerebellum, strongest expression detected in Purkinje and granular
CC cells. Detected at very low levels in several fetal tissues, including
CC dorsal root ganglia (DRG), heart, lung, optic bulb, brain and liver.
CC {ECO:0000269|PubMed:15218527, ECO:0000269|PubMed:16122393}.
CC -!- DEVELOPMENTAL STAGE: In brain, detected first perinatally, with
CC expression reaching maximal levels at postnatal day 9 (P9). In the
CC developing nervous system, barely detectable until birth, and
CC postnatally expressed in white matter tracks including the corpus
CC callosum, external capsule, fimbria hippocampi and corticospinal
CC tracts. In spinal cord, not detected until birth, and postnatally
CC expressed in spinal white matter. In cerebellum, expressed only in
CC cerebellar white matter cells, with expression detected first shortly
CC after birth in the cerebellar peduncle and increasing progressively in
CC the white matter tracts of the cerebellar lobes until P10.
CC {ECO:0000269|PubMed:15147296}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are viable and fertile and display no
CC obvious morphological abnormalities in the brain or spinal cord.
CC {ECO:0000269|PubMed:19699796}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65749.2; Type=Erroneous gene model prediction; Note=Contains intronic sequences.; Evidence={ECO:0000305};
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DR EMBL; AF133093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122467; BAC65749.2; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS41013.1; -.
DR RefSeq; NP_062533.2; NM_019587.2.
DR RefSeq; XP_006527842.1; XM_006527779.1.
DR RefSeq; XP_006527843.1; XM_006527780.2.
DR AlphaFoldDB; Q9QY40; -.
DR SMR; Q9QY40; -.
DR BioGRID; 228284; 6.
DR IntAct; Q9QY40; 2.
DR MINT; Q9QY40; -.
DR STRING; 10090.ENSMUSP00000002079; -.
DR GlyConnect; 2595; 1 N-Linked glycan (1 site).
DR GlyGen; Q9QY40; 10 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9QY40; -.
DR PhosphoSitePlus; Q9QY40; -.
DR jPOST; Q9QY40; -.
DR PaxDb; Q9QY40; -.
DR PeptideAtlas; Q9QY40; -.
DR PRIDE; Q9QY40; -.
DR ProteomicsDB; 289844; -.
DR Antibodypedia; 369; 100 antibodies from 15 providers.
DR Ensembl; ENSMUST00000002079; ENSMUSP00000002079; ENSMUSG00000031385.
DR GeneID; 140571; -.
DR KEGG; mmu:140571; -.
DR UCSC; uc009tmn.2; mouse.
DR CTD; 5365; -.
DR MGI; MGI:2154240; Plxnb3.
DR VEuPathDB; HostDB:ENSMUSG00000031385; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_1_1_1; -.
DR InParanoid; Q9QY40; -.
DR OMA; CPSGENI; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; Q9QY40; -.
DR TreeFam; TF312962; -.
DR Reactome; R-MMU-416700; Other semaphorin interactions.
DR BioGRID-ORCS; 140571; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Plxnb3; mouse.
DR PRO; PR:Q9QY40; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9QY40; protein.
DR Bgee; ENSMUSG00000031385; Expressed in cerebellar nuclear complex and 165 other tissues.
DR Genevisible; Q9QY40; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISS:UniProtKB.
DR GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; IPI:UniProtKB.
DR GO; GO:0017154; F:semaphorin receptor activity; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0010593; P:negative regulation of lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0050918; P:positive chemotaxis; ISS:UniProtKB.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
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; ISS: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; 3.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Neurogenesis;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..1902
FT /note="Plexin-B3"
FT /id="PRO_0000024675"
FT TOPO_DOM 37..1245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1246..1266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1267..1902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..461
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 463..515
FT /note="PSI 1"
FT DOMAIN 609..671
FT /note="PSI 2"
FT DOMAIN 776..822
FT /note="PSI 3"
FT DOMAIN 823..914
FT /note="IPT/TIG 1"
FT DOMAIN 915..1001
FT /note="IPT/TIG 2"
FT DOMAIN 1003..1134
FT /note="IPT/TIG 3"
FT DOMAIN 1154..1221
FT /note="IPT/TIG 4"
FT REGION 353..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 946
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 122..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 257..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 273..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 323..347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 464..481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 470..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 473..490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 484..496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 551..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 352
FT /note="P -> V (in Ref. 4; BAC65749)"
FT /evidence="ECO:0000305"
FT CONFLICT 1566..1601
FT /note="Missing (in Ref. 4; BAC65749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1902 AA; 208366 MW; 25F8DE49B6C98071 CRC64;
MLTDFLQAPV MAPWSPFSLH LLLLFLPLLP LTRVHRFSVP NTSFNHLVLA PDQGKLYVGA
VNHLFQLSPE LKMESVAVTG PVIDSPDCVP FRDLAECPQA QLTDNANQLL LVSSRTQELV
ACGQVKQGVC EKRRLGDVTQ VLYQAEDPGD GQFVAANTLG VTTVGLVVPL PGRDLLLVAR
GLAGKLSAGV PPLTVRQLAG PQPFSSEGLG RLVVGDFSDY NNSYVGAFSD AHSAYFVFRR
RGARAQTEYR SYVARVCLRD VNLYSYVEMP LTCHGQGLIQ AAFLTPDTLL GAFSAGTSQA
QAALCAFPLA DLDRSMEQAR RLCYTTGGQG PSGMEEATVE YGVTSRCVTL PPDSPESYPC
GDEHTPSPIA GRQPLEAQPL LQLGQSISAV AALQTDGHTI AFLGDTQGQL HKVFLNSSHG
QVYHSQQVGP PGSAISPDLL VDSNGDHLYV LTAQQVDRIL VAACPQFPNC TTCLQARDPL
CGWCILQGRC TRRGECGRAA QPNHWLWSYE DNHCPYIQSL LPAQHPRQEQ GQIILSVPRL
PTLAMDEYFH CAFGGYNSLA QVEEPHVVCT TPPQDQMPPN PPGSDHVTLP LALMFEDVVL
TATTFSFYDC SAVQALEVAA PCRACVSSLW RCHWCPQSSH CIYGEHCPEG EKAVYSAQEV
DILVRGPEAC PQVEGLASPQ LVPVGWESHV TLHIQNLHYF QGLPALYHCW LELPGKLQKL
PASLEETSRD SGLIHCQAQQ FYPSMSQWEL PVPIYVTRGE IQRLDNAGDL HVTLYDCAMG
HPDCSHCQAA NGSLSCLWCG DGQPACRYGP LCPPGAVEQL CPIPSIDVIE PLTGPPEGGL
AITILGSNLG QAFNDVRNAV TVAGQPCNPD PSLYRISARI VCVTSPAPNG TAGPVQVAIK
SRPPGISTQN FTYQDPVLLS LNPQWGPQAG GTQLTIHGQY LQTGGNISVF VGDQPCPIQE
PVCPEAIICH TMPQTEPGEA VVLIVFGHVE RKLLTTPFRY TANPQLVEAE PSVSFRGGGR
VIRVRGTGLD VVWQPLLSVW LEDEPKVKAL GVQAQDANPR RSCGAPAADP QACIHLESGL
LQCSTLCSVN SSSLLLCHSP AVPDGALPKR VFFALDNMQV DFASASGGQG FLYQPNPRLA
PLSHEGITHP YHLKPGHVLD VEGEGLNLGI SKEEVQVHIG DGECLVKTLT LTHLYCEPPP
QAPQPTNGSG TLPQFVVQMG NLRLALGPVQ YEAESMMSTF PVEAQLGLGM GAAVLIAAVL
LLTLMYRHKS KKALRDYQKV LVQLENLETG VGDQCRKEFT DLMTEMTDLT SDLEASGIPF
LDYRTYAERA FFPGHVGCPL QPGLEGLGEE GRSVTVRQGL TQLSNLLNSK LFLLTLIHTL
EEQPSFSQRD RCHVASLLSL ALHSKLEYLT DIMRTLLGDL AAHYVHKNPK LMLRRTETMV
EKLLTNWLSI CLYTFLKEVA GEPLYMLFRA IKYQVDKGPV DAVTGKAKRT LNDSHLLRED
VEFQPLTLMA LVGPEADRAA GNSGVHRVPA RVLDTDTITQ VKEKVLDQIY KGTPFSQRPS
VHSLDLEWRS GLAGHLTLSD EDLTSVTQNH WKRLNTLQHY KVPDGATVVL IPQVHNGGTV
SQSLGQTGCP SGENTPMLED GEEGGVRLWH LVKATEEAEG AKVRRSSLRD RERERSRAKA
IPEIYLTRLL SMKGTLQKFV DDTFQAILSM NRPVPIAVKY LFDFLDELAE KHGIEDPETL
HIWKTNSLLL RFWVNVLKNP QLIFDVQVSD NEDAILAVIA QTFIDSCMVS EHKVGRDSPV
NKLLYAREIP RYKQMVEKYY ADIRQSSPAS YQEMNSALAE LSGNYSSAPH CLEALRELYN
HIHRYYDQII SALEEDPVAQ KMQLACRLQQ VAALVEYKVT DL
