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Q8CJH3 (PLXB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plexin-B1
Gene names
Name:Plxnb1
Synonyms:Kiaa0407
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2119 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for SEMA4D. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Ref.5

Subunit structure

Monomer, and heterodimer with PLXNB2 after proteolytic processing. Binds RAC1 that has been activated by GTP binding. Interaction with SEMA4D promotes binding of cytoplasmic ligands. Interacts with RRAS, ARHGEF11, ARHGEF12, ERBB2, MET, MST1R, RND1, RHOD, NRP1 and NRP2 By similarity. Binds PLXNA1. Ref.1

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Tissue specificity

Detected in brain, heart, lung, liver, kidney, stomach, testis, uterus and placenta. Ref.1

Post-translational modification

Phosphorylated on tyrosine residues by ERBB2 and MET upon SEMA4D binding By similarity.

Proteolytic processing favors heterodimerization with PLXNB2 and SEMA4D binding By similarity.

Sequence similarities

Belongs to the plexin family.

Contains 3 IPT/TIG domains.

Contains 1 Sema domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainCoiled coil
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of osteoblast proliferation

Inferred from mutant phenotype PubMed 22019888. Source: BHF-UCL

neuron projection morphogenesis

Inferred from mutant phenotype Ref.5. Source: UniProtKB

ossification involved in bone maturation

Inferred from mutant phenotype PubMed 22019888. Source: BHF-UCL

positive regulation of Rho GTPase activity

Inferred from mutant phenotype Ref.5. Source: UniProtKB

positive regulation of axonogenesis

Inferred from genetic interaction PubMed 15330859. Source: MGI

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype Ref.5. Source: UniProtKB

regulation of cell shape

Inferred from mutant phenotype Ref.5. Source: UniProtKB

regulation of cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

semaphorin-plexin signaling pathway

Inferred from mutant phenotype Ref.5. Source: UniProtKB

semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis

Inferred from mutant phenotype PubMed 22019888. Source: BHF-UCL

   Cellular_componentintegral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular

Inferred from electronic annotation. Source: InterPro

semaphorin receptor complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGTPase activating protein binding

Inferred from physical interaction PubMed 22019888. Source: BHF-UCL

semaphorin receptor activity

Inferred from mutant phenotype Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Arhgef11Q68FM75EBI-2637650,EBI-2365869
Arhgef12Q8R4H22EBI-2637650,EBI-8046267

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 21192100Plexin-B1
PRO_0000024672

Regions

Topological domain20 – 14741455Extracellular Potential
Transmembrane1475 – 149521Helical; Potential
Topological domain1496 – 2119624Cytoplasmic Potential
Domain20 – 479460Sema
Domain1068 – 115891IPT/TIG 1
Domain1160 – 124788IPT/TIG 2
Domain1250 – 1359110IPT/TIG 3
Coiled coil1492 – 152332 Potential
Compositional bias678 – 835158Pro-rich

Sites

Site17991Important for interaction with RAC1 and RND1 By similarity

Amino acid modifications

Glycosylation311N-linked (GlcNAc...) Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation3341N-linked (GlcNAc...) Potential
Glycosylation3491N-linked (GlcNAc...) Potential
Glycosylation5431N-linked (GlcNAc...) Ref.6
Glycosylation12511N-linked (GlcNAc...) Ref.6
Glycosylation13141N-linked (GlcNAc...) Potential
Disulfide bond79 ↔ 88 By similarity
Disulfide bond111 ↔ 119 By similarity
Disulfide bond252 ↔ 377 By similarity
Disulfide bond268 ↔ 322 By similarity
Disulfide bond340 ↔ 364 By similarity
Disulfide bond482 ↔ 499 By similarity
Disulfide bond488 ↔ 533 By similarity
Disulfide bond491 ↔ 508 By similarity
Disulfide bond502 ↔ 514 By similarity
Disulfide bond570 ↔ 588 By similarity

Experimental info

Sequence conflict361Q → L in BAC22660. Ref.1
Sequence conflict17771P → L in BAC97943. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8CJH3 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 08FB5ECD2E6DE342

FASTA2,119231,376
        10         20         30         40         50         60 
MSVLGPVLLQ VFWAGCVVTL RSPLPAAFTA NGTHLQHLAR DPTTGTLYVG ATNFLFQLSP 

        70         80         90        100        110        120 
GLQLEAVVST GPVNDSRDCL PPVIPDECPQ AQPTNNPNQL LLVSPEALVV CGSVHQGICE 

       130        140        150        160        170        180 
LRSLGQIRQL LLRPERPGDT QYVAANDPAV STVGLVAQGL VGEPLLFVGR GYTSRGVGGG 

       190        200        210        220        230        240 
IPPITTRALR PPDPQAAFSY EETAKLAVGR LSEYSHHFVS AFVRGASAYF LFLRRDLKAP 

       250        260        270        280        290        300 
SRAFRAYVSR VCLQDQHYYS YVELPLACQG GRYGLIQAAA VATSKEVARG DVLFAAFSSV 

       310        320        330        340        350        360 
APPTVDWPLS ASTGASGTSV LCAFPLDEVD QLANYTRDAC YTREGRAENG TKVADIAYDV 

       370        380        390        400        410        420 
LSDCAQLPVD TPDAFPCGSD HTPSPMVSCV PLEATPILEL PGVQLTAVAV TMEDGHTIAF 

       430        440        450        460        470        480 
LGDSQGQLHR VYLGPGRSAA PYSKQSIQPG SPVNRDLTFD GTFEHLYVAT QTTLVKVPVA 

       490        500        510        520        530        540 
PCAQHLDCDS CLAHRDPYCG WCVLLGRCSR RSECSRDQGP EQWLWSFQPE LGCLRVVAVS 

       550        560        570        580        590        600 
PANISREERR EVFLSVPGLP SLWPGESYFC YFGDQQSPAL LTSSGVMCPS PDPSEAPVLQ 

       610        620        630        640        650        660 
RGADHISVNV ELRFGAVVIA STSLSFYDCV AVTASSPSAP CRACVSSRWG CNWCVWQQLC 

       670        680        690        700        710        720 
THKASCDAGP MVASQQSPLL PLIPPARDEL TPFPPTVPQT TVTPTPNSFP IEPRAPSTAS 

       730        740        750        760        770        780 
DVLPGAKPSR LSLWGPWAGP GPILSPTSTE SPLHEKPLPP DPPTIPGTTV PAPTGLGPST 

       790        800        810        820        830        840 
TPEDLLASYP FPSDAAAVSP AEPGPEALPS MVALDQPPGT VPDTTFPGAP GSMKPVLDWL 

       850        860        870        880        890        900 
TKGGGELPEA DEWMGGDTPA FSTSTLLSGD GDSAEHEGPP APLILLSSLD YQYDTPGLWE 

       910        920        930        940        950        960 
LGEVNQRVSS CPCVETVQGS LLIPVHVERE VQLRGRNLWL FQDGPRSSEC VLELGSREVA 

       970        980        990       1000       1010       1020 
VEAQVECAPP PDVWCHIKCQ QHQFSYEALK PELQVGLFLR WAGGLRVDSA DGLHVVLYDC 

      1030       1040       1050       1060       1070       1080 
SVGHGDCSRC QTAMPQYDCV WCEGERPRCV AREACNEAET VATQCPAPLI HSVDPLTGPI 

      1090       1100       1110       1120       1130       1140 
DGGTRVTIRG SNLGQHVQDV LDMVRVAGVP CAVDAGEYDV SSSLVCITGA SGEEVTGTVA 

      1150       1160       1170       1180       1190       1200 
VEVPGRGHGV SEFSFAYQDP KVHSIFPARG PRAGGTRLTL HGSKLLTGRL EDIRVVVGDQ 

      1210       1220       1230       1240       1250       1260 
PCHLLLEQQS EQLHCETGPY PVPAELPVTV LFGATERRLQ HGQFKYTSDP NVTSVGPSKS 

      1270       1280       1290       1300       1310       1320 
FFSGGREIWV RGQDLDVVQR PRIRVTVVPR QHGQGLAQKQ HVVPEKFEEP CLVNSSHLLM 

      1330       1340       1350       1360       1370       1380 
CRTPALPGPP WDSGVQVEFI LDNMVFDFAA LSPTPFSYEA DPTLRSLNPE DPSTPFRHKP 

      1390       1400       1410       1420       1430       1440 
GSVFSVEGEN LDLAMSKEEV VAMIGDGPCV VKTLTRNHLY CEPPVEQPLP HPHALREAPD 

      1450       1460       1470       1480       1490       1500 
ALPEFTVQMG NLRFSLGHVQ YDGESPVAFP VAAQVGLGVG TSLLALGVII IVLIYRRKSK 

      1510       1520       1530       1540       1550       1560 
QALRDYKKVQ IQLENLESSV RDRCKKEFTD LMTEMTDLTS DLLGSGIPFL DYKVYAERVF 

      1570       1580       1590       1600       1610       1620 
FPGYRESPLH RDLGVPDSRR PTVEQGLGQL SNLLNSKLFL TKFIHTLESQ RTFSARDRAY 

      1630       1640       1650       1660       1670       1680 
VASLLTVALH GKLEYFTDIL RTLLSDLVAQ YVAKNPKLML RRTETVVEKL LTNWMSICLY 

      1690       1700       1710       1720       1730       1740 
TFVRDSVGEP LYMLFRGIKH QVDKGPVDSV TGKAKYTLND NRLLREDVEY RPLTLNALLA 

      1750       1760       1770       1780       1790       1800 
VGPGAGEAQC VPVKVLDCDT ISQAKEKMLD QLYKGVPLAQ RPDSCTLDVE WRSGVAGHLI 

      1810       1820       1830       1840       1850       1860 
LSDEDVTSEL QGLWRRLNTL QHYKVPDGAT VALVPCLTKH ILRENQDYVP GERTPMLEDV 

      1870       1880       1890       1900       1910       1920 
DEGGIRPWHL VKPSDEPEPP RPRRGSLRGG ERERAKAIPE IYLTRLLSMK GTLQKFVDDL 

      1930       1940       1950       1960       1970       1980 
FQVILSTSRP VPLAVKYFFD LLDEQAQQHG ISDQDTIHIW KTNSLPLRFW INIIKNPQFV 

      1990       2000       2010       2020       2030       2040 
FDVQTSDNMD AVLLVIAQTF MDACTLADHK LGRDSPINKL LYARDIPRYK QMVERYYADI 

      2050       2060       2070       2080       2090       2100 
RQTVPASDQE MNSVLAELSR NCSADLGARV ALHELYKYIN KYYDQIITAL EEDGTAQKMQ 

      2110 
LGYRLQQIAA AVENKVTDL 

« Hide

References

« Hide 'large scale' references
[1]"Plexin-A1 and plexin-B1 specifically interact at their cytoplasmic domains."
Usui H., Taniguchi M., Yokomizo T., Shimizu T.
Biochem. Biophys. Res. Commun. 300:927-931(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH PLXNA1.
Tissue: Brain.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 913-2119.
Tissue: Embryonic tail.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1885-2119.
Tissue: Eye.
[5]"The semaphorin 4D-plexin-B signalling complex regulates dendritic and axonal complexity in developing neurons via diverse pathways."
Vodrazka P., Korostylev A., Hirschberg A., Swiercz J.M., Worzfeld T., Deng S., Fazzari P., Tamagnone L., Offermanns S., Kuner R.
Eur. J. Neurosci. 30:1193-1208(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-543 AND ASN-1251.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB072381 mRNA. Translation: BAC22660.1.
AC140383 Genomic DNA. No translation available.
AC174646 Genomic DNA. No translation available.
AK129133 mRNA. Translation: BAC97943.1.
BC043322 mRNA. Translation: AAH43322.1.
RefSeqNP_766363.2. NM_172775.2.
XP_006512138.1. XM_006512075.1.
XP_006512139.1. XM_006512076.1.
XP_006512140.1. XM_006512077.1.
XP_006512141.1. XM_006512078.1.
XP_006512142.1. XM_006512079.1.
XP_006512143.1. XM_006512080.1.
UniGeneMm.53862.

3D structure databases

ProteinModelPortalQ8CJH3.
SMRQ8CJH3. Positions 25-533, 1544-2113.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8CJH3. 4 interactions.
MINTMINT-1791147.

PTM databases

PhosphoSiteQ8CJH3.

Proteomic databases

PaxDbQ8CJH3.
PRIDEQ8CJH3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072093; ENSMUSP00000071966; ENSMUSG00000053646.
GeneID235611.
KEGGmmu:235611.
UCSCuc009rrz.2. mouse.

Organism-specific databases

CTD5364.
MGIMGI:2154238. Plxnb1.
RougeSearch...

Phylogenomic databases

eggNOGNOG254546.
GeneTreeENSGT00600000084313.
HOGENOMHOG000231376.
HOVERGENHBG053404.
InParanoidQ8CJH3.
KOK06821.
OMAGVMCPSP.
OrthoDBEOG7Q8CM9.
TreeFamTF312962.

Gene expression databases

ArrayExpressQ8CJH3.
BgeeQ8CJH3.
CleanExMM_PLXNB1.
GenevestigatorQ8CJH3.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
2.60.40.10. 4 hits.
InterProIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR016201. Plexin-like_fold.
IPR013548. Plexin_cytoplasmic_RasGAP_dom.
IPR002165. Plexin_repeat.
IPR008936. Rho_GTPase_activation_prot.
IPR001627. Semap_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamPF08337. Plexin_cytopl. 1 hit.
PF01437. PSI. 1 hit.
PF01403. Sema. 1 hit.
PF01833. TIG. 3 hits.
[Graphical view]
SMARTSM00429. IPT. 3 hits.
SM00423. PSI. 3 hits.
SM00630. Sema. 1 hit.
[Graphical view]
SUPFAMSSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 1 hit.
SSF48350. SSF48350. 2 hits.
SSF81296. SSF81296. 3 hits.
PROSITEPS51004. SEMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio382789.
PROQ8CJH3.
SOURCESearch...

Entry information

Entry namePLXB1_MOUSE
AccessionPrimary (citable) accession number: Q8CJH3
Secondary accession number(s): E9QKS4, Q6ZQC3, Q80ZZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot