SEM2A_CAEBR
ID SEM2A_CAEBR Reviewed; 656 AA.
AC Q60PR7; A8Y1M0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Semaphorin-2A;
DE Short=Sema-2a;
DE AltName: Full=Male abnormal protein 20;
DE Flags: Precursor;
GN Name=mab-20; ORFNames=CBG22137;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Regulates the formation or stabilization of cell-cell
CC contacts at several stages of epithelial morphogenesis. In early
CC embryonic development, required for proper ventral closure of the
CC epidermis. During male tail morphogenesis, regulates precursor cell
CC sorting and allows the formation of distinct sensory rays. Seems to
CC control cell-cell contact formation through 2 parallel pathways, one
CC involving efn-4 and one involving plx-2 and unc-129. Involved in axon
CC guidance. Probably by binding receptor plx-2, regulates fln-1-mediated
CC remodeling of the actin cytoskeleton and thus axon guidance and/or
CC fasciculation of DD/VD neurons. {ECO:0000250|UniProtKB:Q95XP4}.
CC -!- SUBUNIT: Interacts with plx-2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; HE601428; CAP38790.3; -; Genomic_DNA.
DR RefSeq; XP_002638911.1; XM_002638865.1.
DR AlphaFoldDB; Q60PR7; -.
DR SMR; Q60PR7; -.
DR STRING; 6238.CBG22137; -.
DR EnsemblMetazoa; CBG22137.1; CBG22137.1; WBGene00040760.
DR GeneID; 8580907; -.
DR KEGG; cbr:CBG_22137; -.
DR CTD; 8580907; -.
DR WormBase; CBG22137; CBP12026; WBGene00040760; Cbr-mab-20.
DR eggNOG; KOG3611; Eukaryota.
DR HOGENOM; CLU_009051_10_0_1; -.
DR InParanoid; Q60PR7; -.
DR OMA; HENCARP; -.
DR OrthoDB; 297290at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
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:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
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; PF07679; I-set; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 3: Inferred from homology;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..656
FT /note="Semaphorin-2A"
FT /id="PRO_0000248546"
FT DOMAIN 21..472
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 474..523
FT /note="PSI"
FT DOMAIN 518..604
FT /note="Ig-like"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..93
FT /evidence="ECO:0000250"
FT DISULFID 248..356
FT /evidence="ECO:0000250"
FT DISULFID 272..316
FT /evidence="ECO:0000250"
FT DISULFID 475..490
FT /evidence="ECO:0000250"
FT DISULFID 484..499
FT /evidence="ECO:0000250"
SQ SEQUENCE 656 AA; 73227 MW; C424E1EB68820C6F CRC64;
MKAWILLLVL TRCSWGLISA DNTFSDRTIG EFRELLINTK DGALFAGSEG AIFRLWAYNI
NDTGENVFSK KQLILSETEE SECCSTASDE KLCRPSTRFL AFTNNKDSIY VCSSVGMRPE
IRVLDSISLQ DQQEPRTEIG ICVVDPTFNS TAVVVDNGNP EDASSVYSGI RTGMGGENHL
IYRPPLTKNG KQLHASIRTI YSDNKWLNEP QFVGSFDVGQ HVLFFFREIA HDNSFGERII
HSRVARVCKK DIGGRNVLRQ VWTSFVKARL NCSVSANFPF YFDHIQSVKR VDKHGETFFY
ATFSTSETAF TSSAICMFQL SSINHLLDTG LLMEETANGQ FAVTADEIPA HRPGTCSSNS
HSISDTDLHF AKTHLLVSDS ISGGTPILPL RDHVYTQILV DQLNNQNVIF AFDSSQQKMW
KISHWKEGNE WKWNLIETQT LKTSGFRIND VALLPGEFFF ATSKAGVHQF SVARCQELPS
CALCSMDPYC SWNAVNSKCA LKTKTNEKSV GWISSSWAGR ISPECSAVEK LQVKDVYLGD
GFKIQGARGG TWQKDGRDLE ESQRHVATSQ GELVILNVDV EDAGTYECTR NGVILMRARV
VVHENCARPT SVAEYRSCQR EWCKKADAYK AALNIWSDSN KKNVQCKANG PSINGL
