PLXC1_MOUSE
ID PLXC1_MOUSE Reviewed; 1574 AA.
AC Q9QZC2; Q8CGW1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Plexin-C1;
DE AltName: Full=Virus-encoded semaphorin protein receptor;
DE AltName: CD_antigen=CD232;
DE Flags: Precursor;
GN Name=Plxnc1; Synonyms=Vespr;
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 [MRNA].
RA Bradshaw J.D., Comeau M.C., Spriggs M.K.;
RT "Mouse homolog of human viral-encoded semaphorin protein receptor
RT (VESPR).";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1205.
RC STRAIN=129/Sv;
RX PubMed=9806843; DOI=10.1006/geno.1998.5540;
RA Horvat S., Medrano J.F.;
RT "A 500-kb YAC and BAC contig encompassing the high-growth deletion in mouse
RT chromosome 10 and identification of the murine Raidd/Cradd gene in the
RT candidate region.";
RL Genomics 54:159-164(1998).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=15967782; DOI=10.1093/intimm/dxh274;
RA Walzer T., Galibert L., De Smedt T.;
RT "Dendritic cell function in mice lacking Plexin C1.";
RL Int. Immunol. 17:943-950(2005).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15611227; DOI=10.4049/jimmunol.174.1.51;
RA Walzer T., Galibert L., Comeau M.R., De Smedt T.;
RT "Plexin C1 engagement on mouse dendritic cells by viral semaphorin A39R
RT induces actin cytoskeleton rearrangement and inhibits integrin-mediated
RT adhesion and chemokine-induced migration.";
RL J. Immunol. 174:51-59(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor for SEMA7A, for vaccinia virus semaphorin A39R and
CC for herpesvirus Sema protein. Binding of semaphorins triggers cellular
CC responses leading to the rearrangement of the cytoskeleton and to
CC secretion of IL6 and IL8 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:15611227}.
CC -!- SUBUNIT: Monomer. Homodimer. Interacts with SEMA7A (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected on dendritic cells, skin Langerhans cells
CC and neutrophils (at protein level). {ECO:0000269|PubMed:15611227}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:15967782}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; AF190578; AAF01334.1; -; mRNA.
DR EMBL; AE016773; AAN84620.1; -; Genomic_DNA.
DR CCDS; CCDS48676.1; -.
DR RefSeq; NP_061267.1; NM_018797.2.
DR AlphaFoldDB; Q9QZC2; -.
DR SMR; Q9QZC2; -.
DR BioGRID; 207723; 2.
DR STRING; 10090.ENSMUSP00000096939; -.
DR GlyConnect; 2596; 12 N-Linked glycans (9 sites).
DR GlyGen; Q9QZC2; 14 sites, 12 N-linked glycans (9 sites).
DR iPTMnet; Q9QZC2; -.
DR PhosphoSitePlus; Q9QZC2; -.
DR EPD; Q9QZC2; -.
DR jPOST; Q9QZC2; -.
DR MaxQB; Q9QZC2; -.
DR PaxDb; Q9QZC2; -.
DR PeptideAtlas; Q9QZC2; -.
DR PRIDE; Q9QZC2; -.
DR ProteomicsDB; 289943; -.
DR Antibodypedia; 30073; 121 antibodies from 22 providers.
DR DNASU; 54712; -.
DR Ensembl; ENSMUST00000099337; ENSMUSP00000096939; ENSMUSG00000074785.
DR GeneID; 54712; -.
DR KEGG; mmu:54712; -.
DR UCSC; uc007gvz.3; mouse.
DR CTD; 10154; -.
DR MGI; MGI:1890127; Plxnc1.
DR VEuPathDB; HostDB:ENSMUSG00000074785; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_004205_0_0_1; -.
DR InParanoid; Q9QZC2; -.
DR OMA; LFHGENK; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; Q9QZC2; -.
DR TreeFam; TF312962; -.
DR Reactome; R-MMU-416700; Other semaphorin interactions.
DR BioGRID-ORCS; 54712; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Plxnc1; mouse.
DR PRO; PR:Q9QZC2; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9QZC2; protein.
DR Bgee; ENSMUSG00000074785; Expressed in habenula and 231 other tissues.
DR ExpressionAtlas; Q9QZC2; baseline and differential.
DR Genevisible; Q9QZC2; MM.
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:0017154; F:semaphorin receptor activity; IBA:GO_Central.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
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:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR CDD; cd11246; Sema_plexin_C1; 1.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR041853; Plexin-C1_Sema.
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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PTHR22625; 1.
DR Pfam; PF08337; Plexin_cytopl; 2.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01833; TIG; 2.
DR SMART; SM00429; IPT; 2.
DR SMART; SM00423; PSI; 2.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1574
FT /note="Plexin-C1"
FT /id="PRO_0000232750"
FT TOPO_DOM 35..950
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 951..971
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 972..1574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..452
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT MOD_RES 984
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 156..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 283..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 455..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 461..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 464..481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 475..487
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
SQ SEQUENCE 1574 AA; 176474 MW; FA8B5E5C6239FFEA CRC64;
MEVSRRKTPP RPPYPAAPLP LIAYLLALAA PARGADEPVW RSEQAIGAIA ASRADGVFVA
SGSCLDQLDY SLKNRLSRLY RDQAGNCTEP VSLAPPARPR PGSSFSKLLL PYREGATGLE
GLLLTGWTFD RGACEVRPLG NLNRSSLRNG TEVVSCHPQG STAGVVYRAS GTDLWYLAVA
ATYVLPEPET ANRCNPAASD RDTAIALKNT EGRSLATQEL GRLKLRGSAG SLHFVDAFLW
NGSVYFPYYP YNYTSGAATG WPSMARIAQS TEVLFQGQAA LDCDHGHPEG RRLLLSSSLV
EAVDIWAGVF SAATGEGQER RSPATTALCL FRMSEIQAHA RSCSWDFQAT EHNCKEGDRP
ERVQPIASST LIHSDLTSVY GTVVMNRTVL FLGTGDGQLL KVVLGENLTS NCPEVIYEIK
EETPVFYKLV PHPMKNIYIY LTAGKEVRRI PVANCSKRKS CSECLAAADP HCGWCLPLQR
CTFQGDCTHA GSFENWLDIS SGPKKCPKIQ ILRSLRERTT VTIVGSISAR HSECVVKNAD
TGKLLCQGRS QLNWTCACNI PSRPSYNVLV VNATFSFPSW NLSERFNFTN CASLKECPAC
IRSGCAWCKR DKKCIHPFTP CEPSDYERNQ ELCQVAVEKS PKDSGGGRVK ESKRNRTDGA
VQVFYIKAIE PQKISTLGKS NVIVTGANFT QASNITMILR GTSTCERDVI RVSHVLNDTH
MKFSLPSSRK EMKDVCIQFD GGTCSSAGAL SYIALPHCSL IVPATTWISG GQNITIMGRN
FDVIDNLIIS HELKGNANVN INVSEYCAAT FCRFLAPNLK SSKVRTNVAV KLRVQDTYLD
CGTLQYLEDP RFTGYRVESE IDTELEVKIQ KENDNFNISK DDIDITLFHG ENKQFNCSFE
NITRNQDLTT ILCKIKSIKN ANTIASSSKK VRVKLGNLEL YVEQESVPST WYFLIALPIL
LAIVIVVAVV VTRYKSKELS RKQSQQLELL ESELRKEIRD GFAELQMDKL DVVDSFGTVP
FLDYKHFALR TFFPESGGFT HIFTEDMHNR DANDKNESLT ALDALICNKS FLVTVIHTLE
KQKNFSVKDR CLFASFLTIA LQTKLVYLTS ILEVLTRDLM EQCSNMQPKL MLRRTESVVE
KLLTNWMSVC LSGFLRETVG EPFYLLVTTL NQKINKGPVD VITCKALYTL NEDWLLWQVP
EFNTVALNVV FEKIPENESA DVCRNISVNV LDCDTIGQAK EKVFQAFLSK NGSPYGLQLN
EIGLELQVGT RQKELLDIDS SSVILEDGIT KLNTIGHYEI SNGSTIKVFK KIANFTSDVE
YSDDHCHLIL PDSEAFQVVQ GKRHRGKHKF KVKEMYLTKL LSTKVAIHSV LEKLFRSIWS
LPNSRAPFAI KYFFDFLDAQ AENKKITDPD VVHIWKTNSL PLRFWVNILK NPQFVFDIKK
TPHIDSCLSV IAQAFMDAFS LTEQQLGKEA PTNKLLYAKD IPTYKEEVKS YYKAIRDLPP
LSSLEMEEFL TQESKKHENE FNEEVALTEI YKYIVKYFDE ILNKLERERG LEEAQKQLLH
VKVLFDEKKK CKWM
