ID Q3V5K0_CAEEL Unreviewed; 1945 AA.
AC Q3V5K0; G4SL42;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 2.
DT 27-MAR-2024, entry version 136.
DE SubName: Full=Sema domain-containing protein {ECO:0000313|EMBL:CCD72079.1};
GN Name=plx-1 {ECO:0000313|EMBL:CCD72079.1,
GN ECO:0000313|WormBase:Y55F3AL.1a};
GN ORFNames=CELE_Y55F3AL.1 {ECO:0000313|EMBL:CCD72079.1}, Y55F3AL.1
GN {ECO:0000313|WormBase:Y55F3AL.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD72079.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD72079.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD72079.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC -!- SIMILARITY: Belongs to the plexin family.
CC {ECO:0000256|ARBA:ARBA00010297}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00352}.
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DR EMBL; BX284604; CCD72079.1; -; Genomic_DNA.
DR RefSeq; NP_500018.3; NM_067617.4.
DR SMR; Q3V5K0; -.
DR EPD; Q3V5K0; -.
DR PeptideAtlas; Q3V5K0; -.
DR EnsemblMetazoa; Y55F3AL.1a.1; Y55F3AL.1a.1; WBGene00004047.
DR GeneID; 246019; -.
DR UCSC; Y55F3AL.1; c. elegans.
DR AGR; WB:WBGene00004047; -.
DR WormBase; Y55F3AL.1a; CE37069; WBGene00004047; plx-1.
DR OrthoDB; 1387371at2759; -.
DR PhylomeDB; Q3V5K0; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004047; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR ExpressionAtlas; Q3V5K0; baseline.
DR GO; GO:0032587; C:ruffle membrane; IDA:WormBase.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0017154; F:semaphorin receptor activity; ISS:WormBase.
DR GO; GO:0031267; F:small GTPase binding; ISS:WormBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0090597; P:nematode male tail mating organ morphogenesis; IMP:WormBase.
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:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR GO; GO:0097374; P:sensory neuron axon guidance; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:WormBase.
DR CDD; cd00603; IPT_PCSR; 2.
DR CDD; cd01180; IPT_plexin_repeat1; 1.
DR CDD; cd12790; RasGAP_plexin_A; 1.
DR CDD; cd11236; Sema_plexin_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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; IPR046800; Plexin_RBD.
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; PLEXIN; 1.
DR PANTHER; PTHR22625:SF69; PLEXIN A, ISOFORM A; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF20170; Plexin_RBD; 1.
DR Pfam; PF01437; PSI; 3.
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; 4.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF81296; E set domains; 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF101912; Sema domain; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Proteomics identification {ECO:0007829|EPD:Q3V5K0,
KW ECO:0007829|PeptideAtlas:Q3V5K0};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1945
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004230422"
FT TRANSMEM 1258..1280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..494
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
SQ SEQUENCE 1945 AA; 216917 MW; 896336D928374AD1 CRC64;
MPTFLQFFII FGVAAAAAGS KNVYSIDDNL VFKNPSHDGH EVFEKMAIDP STTRVFVGAV
NSLYDLTSAD LTVRRHVQTG PQDDSPLCRD ARNREECRHQ LSRTNSHTKA LSVYDKSSKL
IECSNLYQGR CRLRNLHNIS EVISEAIEPR VSNDTSSSVV IFVGSGPANL SSEPVLYVGA
TIGSGDHDRM SVSSLFLRPQ KAFEVVFPGL YGGTHVSLDY RSRGYYKYQI DYINGFESGD
YAYFVTRQRV NIADDSSIQS RLVRVCTGDK NFHSYTEVPL ECTQNGVEFN LVQDVYVTRA
GYELAKSLDI SVSDPVLYGV FWEGDKNSYR SQEPTGKSAI CMFTMREIET SFKQNIMKCY
KGTSGLKKNL PWFSSNDDCR FTTLPWEGIK CGKDVNSKIG GDTPISTSAT YVMEDSSNLL
TAIAINTTRS STVAFVGTQG GQLHKILIES KRSAEKYATE MLTDNEPILS DMEFGGDGKH
VYILTPSKVI KMPTSRCEAL STQCDTCLSS RDPYCGWCVS NNHCTQEESC EREVPHTSRG
WLDFQNSKCP RIRSVKPDQI QINTADYLNV TIENLQAPKG RRMQCLFQFS TGDAVVSDPM
PFDGSLKCAT PPMNRLPRIP TNEYHLPAKL IVVSDGSKLP LATTNFSFYD CNRYTSCSTC
SASQFPCDWC LESNECVAGK LTEDKCRKQH IVNGLNRDGS SIRKGPSKCP HIVAPVSKMS
VATGERRNIS VKVENVDATF MGDFKCEFKY GTVTHEKIAM RTSDDTITCD EMLFEPYGTS
LLGSGSTPYG FNVIWSATGF AVGKKSINRV LDNVASLAID VYSCENLATN CGRCLTLDAD
KYDCGWCSLD SKCARPHQCS NRQIPENWLN ASQLCPNPVI EDFKPKKGSI FGGTRVTING
INLGRHVSDV EKAVQIANVP CEVVEYVPSQ KIVCVTGKSP IKGSNERGVV AVTLRHDSLK
FFAHSTEHFS YVQPVVSSMK PVKGPRSGGT DVTLTGVDLD TGAEVTVRFG QIGCKILERA
SGWLRCRMGA SGEGGQFPLH IAFDGQLQNL PIPIYFEFTS DPSVQSISPN KTIPSGGITV
DVYGQGFTLL QRPRMVFTGL GDEKSYGPAC SIEDDQMMKC ATPTAPGKDS DRGSQERITE
YAFDFDGAEL YRSRIKVMPS PTFETLSEPR FVRPGEDFLT LNGNHLNLAA SERDIDVKVG
GEPCPLTALA NKVLTCQPPV KKPRGAGKLN PEIVVTVGNA SFSIGEVSYD SPGLSSSLFF
IIMFFIIFMI ALIICLIVLY RRKSNTHQRQ MKYLKTQMDT IEMKVATECK EAFAELQTSL
NQYTADLPLG TPTAPFLEYK DYCARVLFPN AGKNHAVLKN LEVDTHKAEA IEAGLREFHK
LLMNKTFLLT MVRTMEANKY FVGKDRVYVG SLLMVVLQEK MGYCTEMLKQ LLRELIEKTV
EKKFQPKILF RRSESIAERM LAAWFTFLLH DHLKTYDAGK KLYELFWGIK QQMEKGPQDA
LTLEARYSLS EEKLLRATFE YKELMVFVSA SDSVYSSTQD IPVRVLDCDT ITQVKEKCLD
AKYRGYRFAD RPAPGDMELE WKTGMNGKMA LQDIDSSSRV EGGNWKRLNT LAHYNVPNNA
ILTLTSKSNS LYNLSILSDR SEKSSVSMKT PGVGSPKPWG APPSVIADHA SSSADTDNGF
KLYHLVKPTE HGPTDSQEKM VTEIYLTRLL MMKGTLAKFI TSLLESIFSS STVPPCIKYM
FDFMDEQARE HGINDPEVVH AWKSNALPLR FWVNLIKNPH FLFDIQKPTK IEGCLSVVAQ
TLMDACSTQD HQLTKDSPSS KLLFAKDMYQ YRDLVDSYYT EISMTPRIDD ATMGANLSAE
SRQHNGEFHV FSALNELYKY LDQYKESIID ALESNEHAQA SRLPGRLQDL LALMESDYYR
ATDYESSTLG LGYNSNSRLM PRDRL
//
