ID PLXC1_HUMAN Reviewed; 1568 AA. AC O60486; Q59H25; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 13-APR-2016, entry version 120. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, RP GLYCOSYLATION, INTERACTION WITH VACCINIA VIRUS PROTEIN A39R AND RP HERPESVIRUS SEMA, AND TISSUE SPECIFICITY. RC TISSUE=Foreskin; RX PubMed=9586637; DOI=10.1016/S1074-7613(00)80552-X; RA Comeau M.R., Johnson R., DuBose R.F., Petersen M., Gearing P., RA VandenBos T., Park L., Farrah T., Buller R.M., Cohen J.I., RA Strockbine L.D., Rauch C., Spriggs M.K.; RT "A poxvirus-encoded semaphorin induces cytokine production from RT monocytes and binds to a novel cellular semaphorin receptor, VESPR."; RL Immunity 8:473-482(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 358-1568. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1198-1305. RG Structural genomics consortium (SGC); RT "Crystal structure of the ubiquitin like domain of PLXNC1."; RL Submitted (DEC-2009) to the PDB data bank. RN [4] RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 35-507 IN COMPLEXES WITH RP SEMA7A AND SMALLPOX VIRUS A39R, FUNCTION, SUBUNIT, DISULFIDE BONDS, RP AND GLYCOSYLATION AT ASN-86; ASN-141; ASN-149; ASN-241; ASN-252; RP ASN-386 AND ASN-407. RX PubMed=20727575; DOI=10.1016/j.cell.2010.07.040; RA Liu H., Juo Z.S., Shim A.H., Focia P.J., Chen X., Garcia K.C., He X.; RT "Structural basis of semaphorin-plexin recognition and viral mimicry RT from Sema7A and A39R complexes with PlexinC1."; RL Cell 142:749-761(2010). CC -!- FUNCTION: Receptor for SEMA7A, for smallpox semaphorin A39R, CC vaccinia virus semaphorin A39R and for herpesvirus Sema protein. CC Binding of semaphorins triggers cellular responses leading to the CC rearrangement of the cytoskeleton and to secretion of IL6 and IL8 CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:20727575}. CC -!- SUBUNIT: Monomer. Homodimer. Interacts with SEMA7A. CC {ECO:0000269|PubMed:20727575, ECO:0000269|PubMed:9586637}. CC -!- INTERACTION: CC Q8JL80:EVM139 (xeno); NbExp=3; IntAct=EBI-2927384, EBI-2927425; CC O75326:SEMA7A; NbExp=4; IntAct=EBI-2927384, EBI-1753538; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Detected in heart, brain, lung, spleen and CC placenta. {ECO:0000269|PubMed:9586637}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20727575, CC ECO:0000269|PubMed:9586637}. CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Sema domain. {ECO:0000255|PROSITE- CC ProRule:PRU00352}. 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; AF030339; AAC18823.1; -; mRNA. DR EMBL; AB208934; BAD92171.1; -; mRNA. DR CCDS; CCDS9049.1; -. DR PIR; T09074; T09074. DR RefSeq; NP_005752.1; NM_005761.2. DR UniGene; Hs.584845; -. DR PDB; 3KUZ; X-ray; 2.30 A; A/B=1198-1305. DR PDB; 3NVN; X-ray; 2.26 A; B=35-507. DR PDB; 3NVQ; X-ray; 2.40 A; B/F=35-507. DR PDBsum; 3KUZ; -. DR PDBsum; 3NVN; -. DR PDBsum; 3NVQ; -. DR ProteinModelPortal; O60486; -. DR SMR; O60486; 37-507, 1198-1305. DR IntAct; O60486; 3. DR STRING; 9606.ENSP00000258526; -. DR iPTMnet; O60486; -. DR PhosphoSite; O60486; -. DR UniCarbKB; O60486; -. DR BioMuta; PLXNC1; -. DR EPD; O60486; -. DR MaxQB; O60486; -. DR PaxDb; O60486; -. DR PRIDE; O60486; -. DR DNASU; 10154; -. DR Ensembl; ENST00000258526; ENSP00000258526; ENSG00000136040. DR GeneID; 10154; -. DR KEGG; hsa:10154; -. DR UCSC; uc001tdc.3; human. DR CTD; 10154; -. DR GeneCards; PLXNC1; -. DR H-InvDB; HIX0171620; -. DR HGNC; HGNC:9106; PLXNC1. DR HPA; CAB026155; -. DR MIM; 604259; gene. DR neXtProt; NX_O60486; -. DR PharmGKB; PA33432; -. DR eggNOG; ENOG410IN3C; Eukaryota. DR eggNOG; ENOG41107MM; LUCA. DR GeneTree; ENSGT00760000119048; -. DR HOGENOM; HOG000115583; -. DR HOVERGEN; HBG082153; -. DR InParanoid; O60486; -. DR KO; K06572; -. DR OMA; VANCNKH; -. DR OrthoDB; EOG75MVV8; -. DR PhylomeDB; O60486; -. DR TreeFam; TF312962; -. DR Reactome; R-HSA-416700; Other semaphorin interactions. DR ChiTaRS; PLXNC1; human. DR EvolutionaryTrace; O60486; -. DR GenomeRNAi; 10154; -. DR NextBio; 38436; -. DR PRO; PR:O60486; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; O60486; -. DR CleanEx; HS_PLXNC1; -. DR ExpressionAtlas; O60486; baseline and differential. DR Genevisible; O60486; HS. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central. DR GO; GO:0005102; F:receptor binding; TAS:ProtInc. DR GO; GO:0017154; F:semaphorin receptor activity; IBA:GO_Central. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0021785; P:branchiomotor neuron axon guidance; IBA:GO_Central. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IBA:GO_Central. DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central. DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central. DR Gene3D; 2.130.10.10; -; 1. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR002909; IPT. DR InterPro; IPR031148; Plexin. DR InterPro; IPR016201; Plexin-like_fold. DR InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom. DR InterPro; IPR002165; Plexin_repeat. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR001627; Semap_dom. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR PANTHER; PTHR22625; PTHR22625; 2. DR Pfam; PF08337; Plexin_cytopl; 1. DR Pfam; PF01437; PSI; 1. DR Pfam; PF01403; Sema; 1. DR Pfam; PF01833; TIG; 2. DR SMART; SM00429; IPT; 2. DR SMART; SM00423; PSI; 2. DR SUPFAM; SSF101912; SSF101912; 1. DR SUPFAM; SSF103575; SSF103575; 1. DR SUPFAM; SSF48350; SSF48350; 2. DR PROSITE; PS51004; SEMA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Membrane; Phosphoprotein; Polymorphism; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 34 {ECO:0000255}. FT CHAIN 35 1568 Plexin-C1. FT /FTId=PRO_0000232749. FT TOPO_DOM 35 944 Extracellular. {ECO:0000255}. FT TRANSMEM 945 965 Helical. {ECO:0000255}. FT TOPO_DOM 966 1568 Cytoplasmic. {ECO:0000255}. FT DOMAIN 35 452 Sema. {ECO:0000255|PROSITE- FT ProRule:PRU00352}. FT MOD_RES 978 978 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9QZC2}. FT CARBOHYD 86 86 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:20727575}. FT CARBOHYD 141 141 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:20727575}. FT CARBOHYD 149 149 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:20727575}. FT CARBOHYD 241 241 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:20727575}. FT CARBOHYD 252 252 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:20727575}. FT CARBOHYD 386 386 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:20727575}. FT CARBOHYD 407 407 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:20727575}. FT CARBOHYD 548 548 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 582 582 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 653 653 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 692 692 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 771 771 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 796 796 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 821 821 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 871 871 N-linked (GlcNAc...). FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 890 890 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 64 87 {ECO:0000255|PROSITE-ProRule:PRU00352, FT ECO:0000269|PubMed:20727575}. FT DISULFID 156 194 {ECO:0000255|PROSITE-ProRule:PRU00352, FT ECO:0000269|PubMed:20727575}. FT DISULFID 226 354 {ECO:0000255|PROSITE-ProRule:PRU00352, FT ECO:0000269|PubMed:20727575}. FT DISULFID 283 329 {ECO:0000255|PROSITE-ProRule:PRU00352, FT ECO:0000269|PubMed:20727575}. FT DISULFID 455 472 {ECO:0000255|PROSITE-ProRule:PRU00352, FT ECO:0000269|PubMed:20727575}. FT DISULFID 461 506 {ECO:0000255|PROSITE-ProRule:PRU00352, FT ECO:0000269|PubMed:20727575}. FT DISULFID 464 481 {ECO:0000255|PROSITE-ProRule:PRU00352, FT ECO:0000269|PubMed:20727575}. FT DISULFID 475 487 {ECO:0000255|PROSITE-ProRule:PRU00352, FT ECO:0000269|PubMed:20727575}. FT VARIANT 1499 1499 E -> K (in dbSNP:rs11107500). FT /FTId=VAR_050602. FT CONFLICT 671 671 K -> R (in Ref. 2; BAD92171). FT {ECO:0000305}. FT STRAND 39 41 {ECO:0000244|PDB:3NVN}. FT STRAND 48 51 {ECO:0000244|PDB:3NVN}. FT STRAND 53 55 {ECO:0000244|PDB:3NVN}. FT STRAND 57 60 {ECO:0000244|PDB:3NVN}. FT STRAND 62 68 {ECO:0000244|PDB:3NVN}. FT STRAND 75 85 {ECO:0000244|PDB:3NVN}. FT STRAND 98 100 {ECO:0000244|PDB:3NVN}. FT STRAND 105 113 {ECO:0000244|PDB:3NVN}. FT STRAND 117 119 {ECO:0000244|PDB:3NVQ}. FT STRAND 122 128 {ECO:0000244|PDB:3NVN}. FT HELIX 129 132 {ECO:0000244|PDB:3NVN}. FT STRAND 134 140 {ECO:0000244|PDB:3NVN}. FT STRAND 149 154 {ECO:0000244|PDB:3NVN}. FT STRAND 162 169 {ECO:0000244|PDB:3NVN}. FT TURN 170 173 {ECO:0000244|PDB:3NVN}. FT STRAND 174 181 {ECO:0000244|PDB:3NVN}. FT TURN 190 192 {ECO:0000244|PDB:3NVN}. FT HELIX 198 200 {ECO:0000244|PDB:3NVN}. FT STRAND 203 212 {ECO:0000244|PDB:3NVN}. FT HELIX 213 215 {ECO:0000244|PDB:3NVN}. FT STRAND 221 225 {ECO:0000244|PDB:3NVN}. FT STRAND 232 234 {ECO:0000244|PDB:3NVN}. FT STRAND 238 240 {ECO:0000244|PDB:3NVQ}. FT STRAND 241 252 {ECO:0000244|PDB:3NVN}. FT TURN 253 256 {ECO:0000244|PDB:3NVN}. FT STRAND 263 272 {ECO:0000244|PDB:3NVN}. FT STRAND 275 281 {ECO:0000244|PDB:3NVN}. FT STRAND 293 299 {ECO:0000244|PDB:3NVN}. FT TURN 301 303 {ECO:0000244|PDB:3NVN}. FT STRAND 305 311 {ECO:0000244|PDB:3NVN}. FT STRAND 316 318 {ECO:0000244|PDB:3NVN}. FT STRAND 325 332 {ECO:0000244|PDB:3NVN}. FT HELIX 333 339 {ECO:0000244|PDB:3NVN}. FT STRAND 345 347 {ECO:0000244|PDB:3NVN}. FT STRAND 350 352 {ECO:0000244|PDB:3NVQ}. FT STRAND 354 357 {ECO:0000244|PDB:3NVN}. FT STRAND 361 363 {ECO:0000244|PDB:3NVN}. FT TURN 367 369 {ECO:0000244|PDB:3NVQ}. FT STRAND 371 394 {ECO:0000244|PDB:3NVN}. FT STRAND 397 403 {ECO:0000244|PDB:3NVN}. FT STRAND 414 418 {ECO:0000244|PDB:3NVN}. FT STRAND 438 443 {ECO:0000244|PDB:3NVN}. FT STRAND 446 452 {ECO:0000244|PDB:3NVN}. FT HELIX 455 457 {ECO:0000244|PDB:3NVQ}. FT HELIX 461 465 {ECO:0000244|PDB:3NVN}. FT STRAND 472 475 {ECO:0000244|PDB:3NVN}. FT TURN 476 479 {ECO:0000244|PDB:3NVN}. FT STRAND 480 483 {ECO:0000244|PDB:3NVN}. FT HELIX 484 486 {ECO:0000244|PDB:3NVN}. FT STRAND 491 493 {ECO:0000244|PDB:3NVQ}. FT TURN 499 501 {ECO:0000244|PDB:3NVN}. FT HELIX 503 505 {ECO:0000244|PDB:3NVN}. FT STRAND 1198 1205 {ECO:0000244|PDB:3KUZ}. FT STRAND 1219 1225 {ECO:0000244|PDB:3KUZ}. FT HELIX 1230 1245 {ECO:0000244|PDB:3KUZ}. FT HELIX 1253 1255 {ECO:0000244|PDB:3KUZ}. FT STRAND 1256 1262 {ECO:0000244|PDB:3KUZ}. FT STRAND 1265 1269 {ECO:0000244|PDB:3KUZ}. FT HELIX 1290 1292 {ECO:0000244|PDB:3KUZ}. FT STRAND 1299 1304 {ECO:0000244|PDB:3KUZ}. SQ SEQUENCE 1568 AA; 175742 MW; EA0CE5519BEF925D CRC64; MEVSRRKAPP RPPRPAAPLP LLAYLLALAA PGRGADEPVW RSEQAIGAIA ASQEDGVFVA SGSCLDQLDY SLEHSLSRLY RDQAGNCTEP VSLAPPARPR PGSSFSKLLL PYREGAAGLG GLLLTGWTFD RGACEVRPLG NLSRNSLRNG TEVVSCHPQG STAGVVYRAG RNNRWYLAVA ATYVLPEPET ASRCNPAASD HDTAIALKDT EGRSLATQEL GRLKLCEGAG SLHFVDAFLW NGSIYFPYYP YNYTSGAATG WPSMARIAQS TEVLFQGQAS LDCGHGHPDG RRLLLSSSLV EALDVWAGVF SAAAGEGQER RSPTTTALCL FRMSEIQARA KRVSWDFKTA ESHCKEGDQP ERVQPIASST LIHSDLTSVY GTVVMNRTVL FLGTGDGQLL KVILGENLTS NCPEVIYEIK EETPVFYKLV PDPVKNIYIY LTAGKEVRRI RVANCNKHKS CSECLTATDP HCGWCHSLQR CTFQGDCVHS ENLENWLDIS SGAKKCPKIQ IIRSSKEKTT VTMVGSFSPR HSKCMVKNVD SSRELCQNKS QPNRTCTCSI PTRATYKDVS VVNVMFSFGS WNLSDRFNFT NCSSLKECPA CVETGCAWCK SARRCIHPFT ACDPSDYERN QEQCPVAVEK TSGGGRPKEN KGNRTNQALQ VFYIKSIEPQ KVSTLGKSNV IVTGANFTRA SNITMILKGT STCDKDVIQV SHVLNDTHMK FSLPSSRKEM KDVCIQFDGG NCSSVGSLSY IALPHCSLIF PATTWISGGQ NITMMGRNFD VIDNLIISHE LKGNINVSEY CVATYCGFLA PSLKSSKVRT NVTVKLRVQD TYLDCGTLQY REDPRFTGYR VESEVDTELE VKIQKENDNF NISKKDIEIT LFHGENGQLN CSFENITRNQ DLTTILCKIK GIKTASTIAN SSKKVRVKLG NLELYVEQES VPSTWYFLIV LPVLLVIVIF AAVGVTRHKS KELSRKQSQQ LELLESELRK EIRDGFAELQ MDKLDVVDSF GTVPFLDYKH FALRTFFPES GGFTHIFTED MHNRDANDKN ESLTALDALI CNKSFLVTVI HTLEKQKNFS VKDRCLFASF LTIALQTKLV YLTSILEVLT RDLMEQCSNM QPKLMLRRTE SVVEKLLTNW MSVCLSGFLR ETVGEPFYLL VTTLNQKINK GPVDVITCKA LYTLNEDWLL WQVPEFSTVA LNVVFEKIPE NESADVCRNI SVNVLDCDTI GQAKEKIFQA FLSKNGSPYG LQLNEIGLEL QMGTRQKELL DIDSSSVILE DGITKLNTIG HYEISNGSTI KVFKKIANFT SDVEYSDDHC HLILPDSEAF QDVQGKRHRG KHKFKVKEMY LTKLLSTKVA IHSVLEKLFR SIWSLPNSRA PFAIKYFFDF LDAQAENKKI TDPDVVHIWK TNSLPLRFWV NILKNPQFVF DIKKTPHIDG CLSVIAQAFM DAFSLTEQQL GKEAPTNKLL YAKDIPTYKE EVKSYYKAIR DLPPLSSSEM EEFLTQESKK HENEFNEEVA LTEIYKYIVK YFDEILNKLE RERGLEEAQK QLLHVKVLFD EKKKCKWM //