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Semaphorin-2A (Sema-2a) (Protein male abnormal 20)

 SEM2A_CAEEL             Reviewed;         658 AA.
Q95XP4; Q86LT8; Q9NI38;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 119.
RecName: Full=Semaphorin-2A;
Short=Sema-2a;
AltName: Full=Protein male abnormal 20;
Flags: Precursor;
Name=mab-20; ORFNames=Y71G12B.20;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY,
AND DISRUPTION PHENOTYPE.
PubMed=10648234;
Roy P.J., Zheng H., Warren C.E., Culotti J.G.;
"mab-20 encodes Semaphorin-2a and is required to prevent ectopic cell
contacts during epidermal morphogenesis in Caenorhabditis elegans.";
Development 127:755-767(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION.
PubMed=12403719; DOI=10.1242/dev.00122;
Chin-Sang I.D., Moseley S.L., Ding M., Harrington R.J., George S.E.,
Chisholm A.D.;
"The divergent C. elegans ephrin EFN-4 functions in embryonic
morphogenesis in a pathway independent of the VAB-1 Eph receptor.";
Development 129:5499-5510(2002).
[4]
FUNCTION.
PubMed=12679110; DOI=10.1016/S0012-1606(02)00129-X;
Hahn A.C., Emmons S.W.;
"The roles of an ephrin and a semaphorin in patterning cell-cell
contacts in C. elegans sensory organ development.";
Dev. Biol. 256:379-388(2003).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Bristol N2;
PubMed=12754521; DOI=10.1038/nbt829;
Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
Kasai K., Takahashi N., Isobe T.;
"Lectin affinity capture, isotope-coded tagging and mass spectrometry
to identify N-linked glycoproteins.";
Nat. Biotechnol. 21:667-672(2003).
[6]
FUNCTION, AND INTERACTION WITH PLX-2.
PubMed=15030761; DOI=10.1016/S1534-5807(04)00057-7;
Ikegami R., Zheng H., Ong S.-H., Culotti J.G.;
"Integration of semaphorin-2A/MAB-20, ephrin-4, and UNC-129 TGF-beta
signaling pathways regulates sorting of distinct sensory rays in C.
elegans.";
Dev. Cell 6:383-395(2004).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65 AND ASN-275, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Bristol N2;
PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
Taoka M., Takahashi N., Isobe T.;
"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
elegans and suggests an atypical translocation mechanism for integral
membrane proteins.";
Mol. Cell. Proteomics 6:2100-2109(2007).
-!- FUNCTION: Regulates the formation or stabilization of cell-cell
contacts at several stages of epithelial morphogenesis. In early
embryonic development, required for proper ventral closure of the
epidermis. During male tail morphogenesis, regulates precursor
cell sorting and allows the formation of distinct sensory rays.
Seems to control cell-cell contact formation through 2 parallel
pathways, one involving efn-4 and one involving plx-2 and unc-129.
May also be involved in axon guidance.
{ECO:0000269|PubMed:10648234, ECO:0000269|PubMed:12403719,
ECO:0000269|PubMed:12679110, ECO:0000269|PubMed:15030761}.
-!- SUBUNIT: Interacts with plx-2. {ECO:0000269|PubMed:15030761}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a;
IsoId=Q95XP4-1; Sequence=Displayed;
Name=b;
IsoId=Q95XP4-2; Sequence=VSP_020310, VSP_020311;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:10648234}.
-!- DISRUPTION PHENOTYPE: Worms have defects both in early embryonic
morphogenesis and in postembryonic male tail morphogenesis.
{ECO:0000269|PubMed:10648234}.
-!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF216968; AAF60253.2; -; mRNA.
EMBL; FO080942; CCD67974.1; -; Genomic_DNA.
EMBL; FO080942; CCD67975.1; -; Genomic_DNA.
RefSeq; NP_001021820.1; NM_001026649.3. [Q95XP4-2]
RefSeq; NP_490875.1; NM_058474.4. [Q95XP4-1]
UniGene; Cel.39551; -.
UniGene; Cel.7500; -.
ProteinModelPortal; Q95XP4; -.
IntAct; Q95XP4; 1.
STRING; 6239.Y71G12B.20a; -.
iPTMnet; Q95XP4; -.
EPD; Q95XP4; -.
PaxDb; Q95XP4; -.
PeptideAtlas; Q95XP4; -.
EnsemblMetazoa; Y71G12B.20a; Y71G12B.20a; WBGene00003111. [Q95XP4-1]
GeneID; 171727; -.
KEGG; cel:CELE_Y71G12B.20; -.
UCSC; Y71G12B.20a; c. elegans. [Q95XP4-1]
CTD; 171727; -.
WormBase; Y71G12B.20a; CE22926; WBGene00003111; mab-20. [Q95XP4-1]
WormBase; Y71G12B.20b; CE33246; WBGene00003111; mab-20. [Q95XP4-2]
eggNOG; KOG3611; Eukaryota.
eggNOG; ENOG410XQZC; LUCA.
GeneTree; ENSGT00760000119134; -.
HOGENOM; HOG000154283; -.
InParanoid; Q95XP4; -.
OMA; WAYNIND; -.
OrthoDB; EOG091G0QST; -.
PhylomeDB; Q95XP4; -.
Reactome; R-CEL-416700; Other semaphorin interactions.
PRO; PR:Q95XP4; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00003111; -.
ExpressionAtlas; Q95XP4; baseline.
GO; GO:0009986; C:cell surface; IDA:WormBase.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0030215; F:semaphorin receptor binding; IPI:WormBase.
GO; GO:0007411; P:axon guidance; IMP:WormBase.
GO; GO:0007413; P:axonal fasciculation; IMP:WormBase.
GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:WormBase.
GO; GO:0090597; P:nematode male tail mating organ morphogenesis; IMP:WormBase.
GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:WormBase.
GO; GO:1902667; P:regulation of axon guidance; IMP:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IMP:WormBase.
GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
GO; GO:0071526; P:semaphorin-plexin signaling pathway; IC:WormBase.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR001627; Semap_dom.
InterPro; IPR036352; Semap_dom_sf.
InterPro; IPR027231; Semaphorin.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
PANTHER; PTHR11036; PTHR11036; 1.
Pfam; PF01403; Sema; 1.
SMART; SM00630; Sema; 1.
SUPFAM; SSF101912; SSF101912; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS51004; SEMA; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Developmental protein;
Disulfide bond; Glycoprotein; Immunoglobulin domain;
Reference proteome; Secreted; Signal.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 658 Semaphorin-2A.
/FTId=PRO_0000248547.
DOMAIN 20 476 Sema. {ECO:0000255|PROSITE-
ProRule:PRU00352}.
DOMAIN 478 527 PSI.
DOMAIN 556 592 Ig-like.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754521,
ECO:0000269|PubMed:17761667}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 653 653 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 87 97 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 252 360 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 276 320 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 479 494 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 488 503 {ECO:0000255|PROSITE-ProRule:PRU00352}.
VAR_SEQ 166 174 DATSVYSGI -> GKQVRSIDK (in isoform b).
{ECO:0000305}.
/FTId=VSP_020310.
VAR_SEQ 175 658 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_020311.
CONFLICT 87 87 C -> Y (in Ref. 1; AAF60253).
{ECO:0000305}.
SEQUENCE 658 AA; 73328 MW; F2AE83F7667D4F6E CRC64;
MRNFLVFSVI FIAYNSCEAA NIQADNTFAD PNIGEFRELL IDPKAGALFV GSEGAIFRLW
AYNINDTGEN VFAKKQLVLS ESEESECRST ASDERLCRPS TRFLAFTNNL DSIYVCSSVG
MRPEIRVLDS LSLRDQQEPR TEIGICVVDP TFNFTAVVVD SGNPEDATSV YSGIRTGMGG
ENHLIYRPPL TKNGKQLHAS IRTIYSDNKW LNEPQFVGSF DVGQHVFFFF REIAHDNSFG
ERIVHSRVAR VCKKDIGGRN VLRQVWTSFV KARLNCSVSA NFPFYFDHIQ SVKRVDKHGE
TYFYATFSTS ETAFTSSAIC MFQLSSINHL LDTGLLMEET ANGQFSVTAD EIPAHRPGTC
SQNSHSISDT DLHFAKTHLL VSDSISGGTP ILPLRDHVFT HIVVDQLPNQ NVIFAFDSAN
RRVWKISHWK EGNEWKSNLI EEKSLKIAAS RINDVALLPA EFFFVTSGAG VSQFSVARCS
EQPSCALCSL DPYCSWNAVN SKCSLKTKTN EKSVGWISSS WAGRISPECS AVEKLTVKDV
YLGDGLRLVG AKNGVWQKDG RSVESGQRHV VTRNGELVVL DAQLEDAGTY ECLRDNIILV
RARIVVHENC ARPTSVAEYR SCQREWCKKA DAYKAALNIW SDSNKKNVQC KANTSSAH


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