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SEM2A_CAEEL
ID   SEM2A_CAEEL             Reviewed;         658 AA.
AC   Q95XP4; Q86LT8; Q9NI38; W6RTP3; W6SBL1;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Semaphorin-2A;
DE            Short=Sema-2a;
DE   AltName: Full=Protein male abnormal 20;
DE   Flags: Precursor;
GN   Name=mab-20 {ECO:0000312|WormBase:Y71G12B.20a};
GN   ORFNames=Y71G12B.20 {ECO:0000312|WormBase:Y71G12B.20a};
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] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=10648234; DOI=10.1242/dev.127.4.755;
RA   Roy P.J., Zheng H., Warren C.E., Culotti J.G.;
RT   "mab-20 encodes Semaphorin-2a and is required to prevent ectopic cell
RT   contacts during epidermal morphogenesis in Caenorhabditis elegans.";
RL   Development 127:755-767(2000).
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).
RN   [3]
RP   FUNCTION.
RX   PubMed=12403719; DOI=10.1242/dev.00122;
RA   Chin-Sang I.D., Moseley S.L., Ding M., Harrington R.J., George S.E.,
RA   Chisholm A.D.;
RT   "The divergent C. elegans ephrin EFN-4 functions in embryonic morphogenesis
RT   in a pathway independent of the VAB-1 Eph receptor.";
RL   Development 129:5499-5510(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=12679110; DOI=10.1016/s0012-1606(02)00129-x;
RA   Hahn A.C., Emmons S.W.;
RT   "The roles of an ephrin and a semaphorin in patterning cell-cell contacts
RT   in C. elegans sensory organ development.";
RL   Dev. Biol. 256:379-388(2003).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=12754521; DOI=10.1038/nbt829;
RA   Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA   Kasai K., Takahashi N., Isobe T.;
RT   "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT   identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH PLX-2.
RX   PubMed=15030761; DOI=10.1016/s1534-5807(04)00057-7;
RA   Ikegami R., Zheng H., Ong S.-H., Culotti J.G.;
RT   "Integration of semaphorin-2A/MAB-20, ephrin-4, and UNC-129 TGF-beta
RT   signaling pathways regulates sorting of distinct sensory rays in C.
RT   elegans.";
RL   Dev. Cell 6:383-395(2004).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65 AND ASN-275, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
RN   [8]
RP   FUNCTION.
RX   PubMed=25358863; DOI=10.1038/ncomms6325;
RA   Nakamura F., Kumeta K., Hida T., Isono T., Nakayama Y.,
RA   Kuramata-Matsuoka E., Yamashita N., Uchida Y., Ogura K., Gengyo-Ando K.,
RA   Mitani S., Ogino T., Goshima Y.;
RT   "Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to
RT   mediate Sema3A signalling.";
RL   Nat. Commun. 5:5325-5325(2014).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF ARG-247.
RX   PubMed=28846083; DOI=10.1038/nn.4630;
RA   Rapti G., Li C., Shan A., Lu Y., Shaham S.;
RT   "Glia initiate brain assembly through noncanonical Chimaerin-Furin axon
RT   guidance in C. elegans.";
RL   Nat. Neurosci. 20:1350-1360(2017).
CC   -!- FUNCTION: Regulates the formation or stabilization of cell-cell
CC       contacts at several stages of epithelial morphogenesis
CC       (PubMed:10648234, PubMed:12403719, PubMed:17761667). In early embryonic
CC       development, required for proper ventral closure of the epidermis
CC       (PubMed:12403719). During male tail morphogenesis, regulates precursor
CC       cell sorting and allows the formation of distinct sensory rays
CC       (PubMed:12679110). Seems to control cell-cell contact formation through
CC       2 parallel pathways, one involving efn-4 and one involving plx-2 and
CC       unc-129 (PubMed:15030761). Involved in follower axon guidance
CC       (PubMed:25358863, PubMed:28846083). In particular, it is required for
CC       the guidance of axons from neurons, including SubL neurons and AIY
CC       interneurons, into the nerve ring (PubMed:28846083). Probably by
CC       binding receptor plx-2, regulates fln-1-mediated remodeling of the
CC       actin cytoskeleton and thus axon guidance and/or fasciculation of DD/VD
CC       neurons (PubMed:25358863). {ECO:0000269|PubMed:10648234,
CC       ECO:0000269|PubMed:12403719, ECO:0000269|PubMed:12679110,
CC       ECO:0000269|PubMed:15030761, ECO:0000269|PubMed:17761667,
CC       ECO:0000269|PubMed:25358863, ECO:0000269|PubMed:28846083}.
CC   -!- FUNCTION: [Isoform a]: Required for the guidance of axons from neurons,
CC       including AIY interneurons, into the nerve ring.
CC       {ECO:0000269|PubMed:28846083}.
CC   -!- SUBUNIT: Interacts with plx-2. {ECO:0000269|PubMed:15030761}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a {ECO:0000312|WormBase:Y71G12B.20a};
CC         IsoId=Q95XP4-1; Sequence=Displayed;
CC       Name=c {ECO:0000312|WormBase:Y71G12B.20c};
CC         IsoId=Q95XP4-3; Sequence=VSP_060648;
CC       Name=d {ECO:0000312|WormBase:Y71G12B.20d};
CC         IsoId=Q95XP4-4; Sequence=VSP_060647;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:10648234}.
CC   -!- DISRUPTION PHENOTYPE: Worms have defects both in early embryonic
CC       morphogenesis and in postembryonic male tail morphogenesis.
CC       {ECO:0000269|PubMed:10648234}.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR   EMBL; AF216968; AAF60253.2; -; mRNA.
DR   EMBL; BX284601; CCD67974.1; -; Genomic_DNA.
DR   EMBL; BX284601; CDM63583.1; -; Genomic_DNA.
DR   EMBL; BX284601; CDM63584.1; -; Genomic_DNA.
DR   RefSeq; NP_001293443.1; NM_001306514.1. [Q95XP4-3]
DR   RefSeq; NP_001293444.1; NM_001306515.1. [Q95XP4-4]
DR   RefSeq; NP_490875.1; NM_058474.4. [Q95XP4-1]
DR   AlphaFoldDB; Q95XP4; -.
DR   SMR; Q95XP4; -.
DR   BioGRID; 37220; 4.
DR   IntAct; Q95XP4; 1.
DR   STRING; 6239.Y71G12B.20a; -.
DR   iPTMnet; Q95XP4; -.
DR   EPD; Q95XP4; -.
DR   PaxDb; Q95XP4; -.
DR   PeptideAtlas; Q95XP4; -.
DR   EnsemblMetazoa; Y71G12B.20a.1; Y71G12B.20a.1; WBGene00003111. [Q95XP4-1]
DR   EnsemblMetazoa; Y71G12B.20c.1; Y71G12B.20c.1; WBGene00003111. [Q95XP4-3]
DR   EnsemblMetazoa; Y71G12B.20d.1; Y71G12B.20d.1; WBGene00003111. [Q95XP4-4]
DR   GeneID; 171727; -.
DR   KEGG; cel:CELE_Y71G12B.20; -.
DR   UCSC; Y71G12B.20a; c. elegans. [Q95XP4-1]
DR   CTD; 171727; -.
DR   WormBase; Y71G12B.20a; CE22926; WBGene00003111; mab-20. [Q95XP4-1]
DR   WormBase; Y71G12B.20c; CE49604; WBGene00003111; mab-20. [Q95XP4-3]
DR   WormBase; Y71G12B.20d; CE49534; WBGene00003111; mab-20. [Q95XP4-4]
DR   eggNOG; KOG3611; Eukaryota.
DR   HOGENOM; CLU_009051_10_0_1; -.
DR   InParanoid; Q95XP4; -.
DR   OMA; HENCARP; -.
DR   OrthoDB; 297290at2759; -.
DR   PhylomeDB; Q95XP4; -.
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:Q95XP4; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00003111; Expressed in embryo and 3 other tissues.
DR   ExpressionAtlas; Q95XP4; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:WormBase.
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; IPI:WormBase.
DR   GO; GO:0007411; P:axon guidance; IMP:WormBase.
DR   GO; GO:0007413; P:axonal fasciculation; IMP:WormBase.
DR   GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:WormBase.
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:UniProtKB.
DR   GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR   GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:WormBase.
DR   GO; GO:1902667; P:regulation of axon guidance; IMP:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; IMP:WormBase.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
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; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
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; PF01403; Sema; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF101912; SSF101912; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..658
FT                   /note="Semaphorin-2A"
FT                   /id="PRO_0000248547"
FT   DOMAIN          20..476
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          478..527
FT                   /note="PSI"
FT   DOMAIN          556..592
FT                   /note="Ig-like"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        653
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        87..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        252..360
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        276..320
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        479..494
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        488..503
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   VAR_SEQ         1..177
FT                   /note="Missing (in isoform d)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060647"
FT   VAR_SEQ         1..120
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060648"
FT   MUTAGEN         247
FT                   /note="R->H: In ns789; impairs nerve ring assembly due to
FT                   non-commissural interneurons AIY failing to extend dorsally
FT                   and enter the nerve ring. This phenotype is enhanced in a
FT                   chin-1 ns399 mutant background."
FT                   /evidence="ECO:0000269|PubMed:28846083"
FT   CONFLICT        87
FT                   /note="C -> Y (in Ref. 1; AAF60253)"
FT                   /evidence="ECO:0000305"
SQ   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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