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 25-JAN-2012, entry version 81. 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], MASS SPECTROMETRY, GLYCOSYLATION, RP INTERACTION WITH VACCINIA VIRUS PROTEIN A39R AND HERPESVIRUS SEMA, AND RP TISSUE SPECIFICITY. RC TISSUE=Foreskin; RX MEDLINE=98246049; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1466, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [4] 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 [5] 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). CC -!- SUBUNIT: Monomer. Homodimer. Interacts with SEMA7A. 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; Single-pass type I membrane CC protein (Potential). CC -!- TISSUE SPECIFICITY: Detected in heart, brain, lung, spleen and CC placenta. CC -!- PTM: N-glycosylated. CC -!- SIMILARITY: Belongs to the plexin family. CC -!- SIMILARITY: Contains 1 Sema domain. 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 IPI; IPI00024766; -. 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, 585-623, 968-1562. DR IntAct; O60486; 2. DR STRING; O60486; -. DR PhosphoSite; O60486; -. DR PRIDE; O60486; -. DR Ensembl; ENST00000258526; ENSP00000258526; ENSG00000136040. DR GeneID; 10154; -. DR KEGG; hsa:10154; -. DR UCSC; uc001tdc.1; human. DR CTD; 10154; -. DR GeneCards; GC12P094542; -. DR H-InvDB; HIX0010887; -. DR HGNC; HGNC:9106; PLXNC1. DR HPA; CAB026155; -. DR MIM; 604259; gene. DR neXtProt; NX_O60486; -. DR PharmGKB; PA33432; -. DR eggNOG; prNOG11301; -. DR GeneTree; ENSGT00560000076899; -. DR HOGENOM; HBG714508; -. DR HOVERGEN; HBG082153; -. DR InParanoid; O60486; -. DR OMA; ADVCRNI; -. DR OrthoDB; EOG4VQ9NM; -. DR PhylomeDB; O60486; -. DR Reactome; REACT_111045; Developmental Biology. DR NextBio; 38436; -. DR ArrayExpress; O60486; -. DR Bgee; O60486; -. DR CleanEx; HS_PLXNC1; -. DR Genevestigator; O60486; -. DR GermOnline; ENSG00000136040; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0005102; F:receptor binding; TAS:ProtInc. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR002909; IPT_TIG_rcpt. DR InterPro; IPR003659; Plexin-like. 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; Semaphorin/CD100_Ag. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3. DR Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1. DR KO; K06572; -. DR Pfam; PF08337; Plexin_cytopl; 1. DR Pfam; PF01437; PSI; 1. DR Pfam; PF01833; TIG; 2. DR SMART; SM00429; IPT; 2. DR SMART; SM00423; PSI; 2. DR SUPFAM; SSF81296; Ig_E-set; 1. DR SUPFAM; SSF103575; Plexin-like_fold; 1. DR SUPFAM; SSF48350; Rho_GAP; 1. DR SUPFAM; SSF101912; Sema; 1. 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 Potential. FT CHAIN 35 1568 Plexin-C1. FT /FTId=PRO_0000232749. FT TOPO_DOM 35 944 Extracellular (Potential). FT TRANSMEM 945 965 Helical; (Potential). FT TOPO_DOM 966 1568 Cytoplasmic (Potential). FT DOMAIN 35 452 Sema. FT MOD_RES 978 978 Phosphoserine (By similarity). FT MOD_RES 1466 1466 Phosphothreonine. FT CARBOHYD 86 86 N-linked (GlcNAc...). FT CARBOHYD 141 141 N-linked (GlcNAc...). FT CARBOHYD 149 149 N-linked (GlcNAc...). FT CARBOHYD 241 241 N-linked (GlcNAc...). FT CARBOHYD 252 252 N-linked (GlcNAc...). FT CARBOHYD 386 386 N-linked (GlcNAc...). FT CARBOHYD 407 407 N-linked (GlcNAc...). FT CARBOHYD 548 548 N-linked (GlcNAc...) (Potential). FT CARBOHYD 582 582 N-linked (GlcNAc...) (Potential). FT CARBOHYD 653 653 N-linked (GlcNAc...) (Potential). FT CARBOHYD 692 692 N-linked (GlcNAc...) (Potential). FT CARBOHYD 771 771 N-linked (GlcNAc...) (Potential). FT CARBOHYD 796 796 N-linked (GlcNAc...) (Potential). FT CARBOHYD 821 821 N-linked (GlcNAc...) (Potential). FT CARBOHYD 890 890 N-linked (GlcNAc...) (Potential). FT DISULFID 64 87 FT DISULFID 156 194 FT DISULFID 226 354 FT DISULFID 283 329 FT DISULFID 455 472 FT DISULFID 461 506 FT DISULFID 464 481 FT DISULFID 475 487 FT VARIANT 1499 1499 E -> K (in dbSNP:rs11107500). FT /FTId=VAR_050602. FT CONFLICT 671 671 K -> R (in Ref. 2; BAD92171). FT STRAND 39 41 FT STRAND 58 60 FT STRAND 64 68 FT STRAND 75 82 FT STRAND 123 125 FT STRAND 135 137 FT STRAND 165 169 FT STRAND 174 181 FT TURN 190 192 FT HELIX 198 200 FT STRAND 203 209 FT STRAND 223 225 FT STRAND 232 234 FT STRAND 244 251 FT STRAND 263 267 FT STRAND 269 272 FT STRAND 279 281 FT STRAND 293 299 FT TURN 301 303 FT STRAND 305 307 FT STRAND 309 311 FT STRAND 325 328 FT HELIX 333 339 FT STRAND 345 347 FT STRAND 361 363 FT STRAND 371 375 FT STRAND 382 392 FT STRAND 399 403 FT STRAND 414 417 FT STRAND 438 442 FT STRAND 446 452 FT HELIX 461 465 FT TURN 476 479 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 //