PLXB3_RAT
ID PLXB3_RAT Reviewed; 1902 AA.
AC D3ZLH5;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Plexin-B3 {ECO:0000303|PubMed:20696765};
DE AltName: Full=Protein Plxnb3;
DE Flags: Precursor;
GN Name=Plxnb3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH ARHGDIA.
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).
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:20696765}.
CC -!- SUBUNIT: Binds MET and MST1R. Interacts with RIT2/RIN. Interacts (via
CC cytoplasmic domain) with FSCN1 and RAC1. May form homodimers (via Sema
CC domain) (By similarity). Interacts (via cytoplasmic domain) with
CC ARHGDIA. {ECO:0000250|UniProtKB:Q9QY40, ECO:0000250|UniProtKB:Q9ULL4,
CC ECO:0000269|PubMed:20696765}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ULL4};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9ULL4}.
CC Note=Colocalizes with RIT2/RIN at the plasma membrane.
CC {ECO:0000250|UniProtKB:Q9ULL4}.
CC -!- TISSUE SPECIFICITY: Expressed in glioma cells (at protein level).
CC Expressed in glioma cells and oligodendrocyte precursor cells.
CC {ECO:0000269|PubMed:20696765}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000255}.
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; AC096338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001129350.1; NM_001135878.1.
DR RefSeq; XP_006229649.1; XM_006229587.3.
DR AlphaFoldDB; D3ZLH5; -.
DR SMR; D3ZLH5; -.
DR STRING; 10116.ENSRNOP00000053235; -.
DR GlyGen; D3ZLH5; 9 sites.
DR PaxDb; D3ZLH5; -.
DR PeptideAtlas; D3ZLH5; -.
DR PRIDE; D3ZLH5; -.
DR Ensembl; ENSRNOT00000080088; ENSRNOP00000072671; ENSRNOG00000061731.
DR GeneID; 363517; -.
DR KEGG; rno:363517; -.
DR CTD; 5365; -.
DR RGD; 1560615; Plxnb3.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_1_1_1; -.
DR InParanoid; D3ZLH5; -.
DR OMA; CPSGENI; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; D3ZLH5; -.
DR TreeFam; TF312962; -.
DR Reactome; R-RNO-416700; Other semaphorin interactions.
DR PRO; PR:D3ZLH5; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000061731; Expressed in cerebellum and 6 other tissues.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
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:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISS:UniProtKB.
DR GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; ISO:RGD.
DR GO; GO:0017154; F:semaphorin receptor activity; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0010593; P:negative regulation of lamellipodium assembly; IMP: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:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
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; IMP: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..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1902
FT /note="Plexin-B3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420128"
FT TOPO_DOM 35..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 35..461
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000305"
FT DOMAIN 463..515
FT /note="PSI 1"
FT /evidence="ECO:0000255"
FT DOMAIN 609..671
FT /note="PSI 2"
FT /evidence="ECO:0000255"
FT DOMAIN 776..822
FT /note="PSI 3"
FT /evidence="ECO:0000255"
FT DOMAIN 824..913
FT /note="IPT/TIG 1"
FT /evidence="ECO:0000255"
FT DOMAIN 915..1001
FT /note="IPT/TIG 2"
FT /evidence="ECO:0000255"
FT DOMAIN 1003..1134
FT /note="IPT/TIG 3"
FT /evidence="ECO:0000255"
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 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:0000250|UniProtKB:P70207,
FT ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 122..130
FT /evidence="ECO:0000250|UniProtKB:P70207,
FT ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 257..360
FT /evidence="ECO:0000250|UniProtKB:P70207,
FT ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 273..305
FT /evidence="ECO:0000250|UniProtKB:P70207,
FT ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 323..347
FT /evidence="ECO:0000250|UniProtKB:P70207,
FT ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 464..481
FT /evidence="ECO:0000250|UniProtKB:P70207,
FT ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 470..514
FT /evidence="ECO:0000250|UniProtKB:P70207,
FT ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 473..490
FT /evidence="ECO:0000250|UniProtKB:P70207,
FT ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 484..496
FT /evidence="ECO:0000250|UniProtKB:P70207,
FT ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 551..569
FT /evidence="ECO:0000250|UniProtKB:P70207,
FT ECO:0000255|PROSITE-ProRule:PRU00352"
SQ SEQUENCE 1902 AA; 208487 MW; 1884F43ADB4DDBDE CRC64;
MLTDFLQAPV MAPWSPFSLH LLLLFLLLLP LTRAHRFSVP NASFNHLVLA PDQGKLYVGA
VNHLFQLSPE LEMESVAITG PVIDSPDCVP FRDLAECPQA QLTDNANQLL LVSSRAQELV
ACGQVRQGVC EKRRLGDVTQ VLYQAEDPGD GQFVAANTLG VTTVGLVVPL PGRDLLLVAR
GLAGKLSAGV PPLTVRQLAG PQPFSSEGLG RLVVGDFSDY NNSYVGAFSD AHSAYFVFRR
RGARAQTEYR SYVARVCLGD VNLYSYVEVP LTCHGQGLIQ AAFLAPDTLL GAFSAGTSQA
QAALCAFPLA DLDGSMEQAR RLCYTTGGQG PNGMEEATVE YGVTSRCVTL PPDSPESYPC
GDEHTPSPIA GRQPLEAQPL LQLGQPISAV AALQTDGHTI AFLGDTEGQL HKVFLNSSHG
QVYHSQQVGP PGSAISPDLL VDNSGDYLYV LTAQQVDRIL VAACPQFPNC TTCLQARDPL
CGWCILQGRC TRRAECGRAV QPNQWLWSYE DNHCLHIQSL LPAQHPRQEH GQITLSVPGL
PNLAMDEYFY CAFGDYNSLA QVEEHHVVCA TPPQDRMPPN PPGSDHVTLP LALMFEDVVL
AATTFSFYDC SAIQALEVAA PCRTCVSSLW RCHWCPQSSH CVYGERCPEG EKAVYSAQEV
DILVRGPEAC PQVKGLASPQ LVPVGWESHV TLHIENLHYF RGLPALYYCW LELPGKLRKL
PAFLEETSRN SGLIHCQAQQ FHPSMSQWEL PVPIYVTRGE IQRLDNTGDL HVTLYDCAMG
HPDCSHCQAA NGSLSCLWCG DGQPACRYGP LCPPGAVEQL CPIPSIDVIE PLTGPPEGGL
AITILGSNLG QAFNDVRNAV TVAGQPCNPD PSLYRISARI VCVTSPAPNG TSGPVQVAIK
SRPPGISAQH FTYQDPVLLS LNPQWGPQAG GTQLTIHGQY LQTGGNVSAF VGDQPCPIQE
PVCPEAIICH TMPQMEPGEA VVFVVFGHVE RKLLTTPFRY TANPQLVEAE PSVSFRGGGR
VIRVRGTGLD VVWQPLLSVW LEDEFQVKAL GVQAQDVNPR RSCGAPAADP QACIHLESGL
LQCSTLCSVN SSSLLLCHSP AVPDGALPKR VFFALDNMQV DFASASGGQG FLYQPNPRLA
PLSHEGITHP YRLKPGHVLD VEGEGLNLGI SKEEVQVHIG DGKCLVKTLT LTHLYCEPPQ
QAPQPTNGSG TLPQFVVQMG NVRLALGPVQ YEAEPMISTF PVEAQVGLGM GAAMLIAAVL
LLTLMYRHKS KQALRDYQKV LVQLENLETG VGDQCRKEFT DLMTEMTDLT SDLEASGIPF
LDYRTYAERA FFPGHVGCPL QPGLEGPGEE GRRVTVCQGL TQLSNLLNSK LFLLTLIHTL
EEQPSFSQRD RCHVASLLSL ALHSKLEYLT DIMRTLLGDL AAHYVHKNPK LMLRRTETMV
EKLLTNWLSI CLYAFLKEVA GEPLYMLFRA IKYQVDKGPV DAVTGKAKRT LNDSHLLRED
VEFRPLTLMA LVGPGAGGAA GNSEVHRVPA RVLDTDTITQ VKEKVLDQIY KGTPFSQRPS
VHSLDLEWRS GLAGHLTLSD EDLTSVTQNH WKRLNTLQHY KVPDGATVVL IPQLHNGGTV
SQSLEQTGCH SGENTPMLED GEEGGVRLWH LVKATEETEG AKVRRSSLRE RERERARAKA
IPEIYLTRLL SMKGTLQKFV DDTFQAILSM NRPVPIAVKY LFDFLDELAE KHGIEDPETL
HIWKTNSLLL RFWVNALKNP QLIFDVRVSD NEDAILAVIA QTFIDSCMVS EHKVGRDSPV
NKLLYAREIP RYKQMVEKYY ADIRQSSPAS YQEMNSALAE LSGNYTSAPN CLEALRELYN
HIHRYYDQII SALEEDPVAQ KMQLACRLQQ VAALVEYKVT DL
