SEM1A_CAEEL
ID SEM1A_CAEEL Reviewed; 712 AA.
AC Q17330; Q9XWF8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Semaphorin-1A;
DE AltName: Full=CeSema;
DE Flags: Precursor;
GN Name=smp-1; Synonyms=sema-1a; ORFNames=Y54E5B.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=11959817; DOI=10.1242/dev.129.9.2065;
RA Ginzburg V.E., Roy P.J., Culotti J.G.;
RT "Semaphorin 1a and semaphorin 1b are required for correct epidermal cell
RT positioning and adhesion during morphogenesis in C. elegans.";
RL Development 129:2065-2078(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: May function in growth cone guidance. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; U15667; AAA51021.1; -; mRNA.
DR EMBL; AL032653; CAA21714.1; -; Genomic_DNA.
DR PIR; T27165; T27165.
DR RefSeq; NP_493582.3; NM_061181.5.
DR AlphaFoldDB; Q17330; -.
DR SMR; Q17330; -.
DR BioGRID; 38734; 1.
DR STRING; 6239.Y54E5B.1a; -.
DR EPD; Q17330; -.
DR PaxDb; Q17330; -.
DR PeptideAtlas; Q17330; -.
DR EnsemblMetazoa; Y54E5B.1a.1; Y54E5B.1a.1; WBGene00004889.
DR GeneID; 173351; -.
DR KEGG; cel:CELE_Y54E5B.1; -.
DR UCSC; Y54E5B.1b.1; c. elegans.
DR CTD; 173351; -.
DR WormBase; Y54E5B.1a; CE19225; WBGene00004889; smp-1.
DR eggNOG; KOG3611; Eukaryota.
DR HOGENOM; CLU_009051_7_2_1; -.
DR InParanoid; Q17330; -.
DR OMA; FGQSEQC; -.
DR OrthoDB; 493443at2759; -.
DR PhylomeDB; Q17330; -.
DR Reactome; R-CEL-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-CEL-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-CEL-399956; CRMPs in Sema3A signaling.
DR Reactome; R-CEL-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-CEL-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-CEL-416700; Other semaphorin interactions.
DR PRO; PR:Q17330; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004889; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q17330; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0030215; F:semaphorin receptor binding; IPI:WormBase.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR GO; GO:0090597; P:nematode male tail mating organ morphogenesis; IMP:WormBase.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR CDD; cd11237; Sema_1A; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR042068; SEM1A_sema_dom.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Membrane; Neurogenesis; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..712
FT /note="Semaphorin-1A"
FT /id="PRO_0000032300"
FT TOPO_DOM 17..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..712
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..494
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 127..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 262..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 286..333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 497..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 506..523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 108
FT /note="D -> DD (in Ref. 1; AAA51021)"
FT /evidence="ECO:0000305"
FT CONFLICT 250..252
FT /note="EEP -> RSRSF (in Ref. 1; AAA51021)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="C -> Y (in Ref. 1; AAA51021)"
FT /evidence="ECO:0000305"
FT CONFLICT 307..308
FT /note="ID -> RH (in Ref. 1; AAA51021)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="H -> Q (in Ref. 1; AAA51021)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="A -> D (in Ref. 1; AAA51021)"
FT /evidence="ECO:0000305"
FT CONFLICT 523..712
FT /note="CVHGGSWTGDQFIQNMVFGQSEQCPEGIIVREVFDDNESEAQPEAVSRSGYP
FT KEHSTITVVLVAAVASLISLIIGAFIGIRVNRWAATSEPHRSASSTSGSDYDSFGRARL
FT TRHDSLTTATKVDHGFVPQSKQSVDATSLVMSINATHHPMSMSQHGSGINTPSRDKNAI
FT VTSINQNTLPRDYKVKKVYL -> QVIVMSSLTPTSLMWTRKMEIPLKKDKKRWKTRKM
FT EI (in Ref. 1; AAA51021)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 712 AA; 78081 MW; 04CBD96EB0EA01BE CRC64;
MRRILTLLLL FNVVRSSEAI TGGVVNLRPK QIINSVGIGD RFGGIGTSSD ESDHFKLLAA
DGDSLLVGAR NAVYNLSLST LSVNHKIDWK PPAEHIEECI MKGKSKTDCQ NYIRVLARKS
AGVSLVCGTH AFSPKCREYT VTEFGIRNTR QFDGQGISPY DPKHNSSALY VPGTNQLFVA
TVTDFVGNDA LIYRKTIDET PSSKSAANIR TQSYDARVLN APNFVATFAY KEHVYFWFRE
IASEAIDNNE EPQIYARVAR VCKNDKGGAR PANERWTSYL KARLNCSLPS GSSPFYFNEL
KAVSDPIDAG NNNHVVYTVF STPDSDVRMS AVCKFSMKKI REEFDNGTFK HQNNAQSMWM
AFNRNEVPKP RPGSCSPDST KLPENTVSFI LHHPLLHRPI PSVAAPLLVE GADRADLTQI
TVLPRVRAVG GHNYDILFIG TSDGKVLKVV EVDGNATVIQ SATVFQRGVP IVNLLTTKES
VVIVSADEIA SLPVHNCAQQ TSCSKCVQLQ DPHCAWDSSI ARCVHGGSWT GDQFIQNMVF
GQSEQCPEGI IVREVFDDNE SEAQPEAVSR SGYPKEHSTI TVVLVAAVAS LISLIIGAFI
GIRVNRWAAT SEPHRSASST SGSDYDSFGR ARLTRHDSLT TATKVDHGFV PQSKQSVDAT
SLVMSINATH HPMSMSQHGS GINTPSRDKN AIVTSINQNT LPRDYKVKKV YL
