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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
 
 
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