SYD1_CAEEL
ID SYD1_CAEEL Reviewed; 987 AA.
AC Q86NH1; Q86NH0; Q8ISS1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Rho GTPase-activating protein syd-1;
DE AltName: Full=Axon identity specification protein syd-1;
DE AltName: Full=Synapse defective protein 1;
GN Name=syd-1 {ECO:0000312|WormBase:F35D2.5b}; ORFNames=F35D2.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAN38752.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12379863; DOI=10.1038/nn959;
RA Hallam S.J., Goncharov A., McEwen J., Baran R., Jin Y.;
RT "SYD-1, a presynaptic protein with PDZ, C2 and rhoGAP-like domains,
RT specifies axon identity in C. elegans.";
RL Nat. Neurosci. 5:1137-1146(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17115037; DOI=10.1038/nn1808;
RA Dai Y., Taru H., Deken S.L., Grill B., Ackley B., Nonet M.L., Jin Y.;
RT "SYD-2 Liprin-alpha organizes presynaptic active zone formation through
RT ELKS.";
RL Nat. Neurosci. 9:1479-1487(2006).
RN [4] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17115039; DOI=10.1038/nn1806;
RA Patel M.R., Lehrman E.K., Poon V.Y., Crump J.G., Zhen M., Bargmann C.I.,
RA Shen K.;
RT "Hierarchical assembly of presynaptic components in defined C. elegans
RT synapses.";
RL Nat. Neurosci. 9:1488-1498(2006).
CC -!- FUNCTION: Probable GTPase activator for the Rho-type GTPases by
CC converting them to an inactive GDP-bound state. Regulates the
CC localization and assembly of presynaptic components during presynaptic
CC development and is required for specifying the identity of axons during
CC initial polarity acquisition. In these roles it is thought to act cell
CC autonomously downstream of syg-1 and syg-2 and upstream of syd-2,
CC possibly as a positive regulator of the latter. Required for the
CC control of movement, egg-laying and the correct localization of elks-1.
CC {ECO:0000269|PubMed:12379863, ECO:0000269|PubMed:17115037,
CC ECO:0000269|PubMed:17115039}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:12379863}.
CC Note=Presynaptic terminals. {ECO:0000269|PubMed:12379863}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000269|PubMed:9851916};
CC IsoId=Q86NH1-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:12379863, ECO:0000269|PubMed:9851916};
CC IsoId=Q86NH1-2; Sequence=VSP_052592, VSP_052593, VSP_052594;
CC Name=c {ECO:0000269|PubMed:9851916};
CC IsoId=Q86NH1-3; Sequence=VSP_052591;
CC -!- TISSUE SPECIFICITY: Expressed in the nerve ring of embryos. In L1
CC larvae, expression is seen in the ventral processes of ventral cord
CC motor neurons. In adults, expression is seen along the dorsal and
CC ventral nerve cords, the HSNL motor neuron and more specifically
CC localizes to the axonal processes. {ECO:0000269|PubMed:12379863,
CC ECO:0000269|PubMed:17115037, ECO:0000269|PubMed:17115039}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit an irregular shape and fail to show
CC axonic polarization. Uncoordinated movement and retention of eggs, an
CC egg-laying defect are apparent. {ECO:0000269|PubMed:17115037}.
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DR EMBL; AF546880; AAN38752.1; -; mRNA.
DR EMBL; FO081290; CCD70505.1; -; Genomic_DNA.
DR EMBL; FO081290; CCD70506.1; -; Genomic_DNA.
DR EMBL; FO081290; CCD70507.1; -; Genomic_DNA.
DR RefSeq; NP_001022146.1; NM_001026975.3. [Q86NH1-1]
DR RefSeq; NP_001022148.1; NM_001026977.2.
DR RefSeq; NP_495592.2; NM_063191.4.
DR AlphaFoldDB; Q86NH1; -.
DR SMR; Q86NH1; -.
DR BioGRID; 39564; 12.
DR IntAct; Q86NH1; 9.
DR STRING; 6239.F35D2.5a; -.
DR EPD; Q86NH1; -.
DR PaxDb; Q86NH1; -.
DR EnsemblMetazoa; F35D2.5a.1; F35D2.5a.1; WBGene00006363. [Q86NH1-1]
DR EnsemblMetazoa; F35D2.5c.1; F35D2.5c.1; WBGene00006363. [Q86NH1-3]
DR EnsemblMetazoa; F35D2.5c.2; F35D2.5c.2; WBGene00006363. [Q86NH1-3]
DR GeneID; 174230; -.
DR KEGG; cel:CELE_F35D2.5; -.
DR UCSC; F35D2.5b; c. elegans. [Q86NH1-1]
DR CTD; 174230; -.
DR WormBase; F35D2.5a; CE33391; WBGene00006363; syd-1. [Q86NH1-1]
DR WormBase; F35D2.5b; CE33069; WBGene00006363; syd-1. [Q86NH1-2]
DR WormBase; F35D2.5c; CE33392; WBGene00006363; syd-1. [Q86NH1-3]
DR eggNOG; KOG1452; Eukaryota.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR InParanoid; Q86NH1; -.
DR OMA; GLTEEMY; -.
DR OrthoDB; 1181644at2759; -.
DR PhylomeDB; Q86NH1; -.
DR Reactome; R-CEL-9013148; CDC42 GTPase cycle.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR SignaLink; Q86NH1; -.
DR PRO; PR:Q86NH1; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006363; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:GOC.
DR GO; GO:0042734; C:presynaptic membrane; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0097060; C:synaptic membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IMP:UniProtKB.
DR GO; GO:0048495; F:Roundabout binding; IPI:WormBase.
DR GO; GO:0005102; F:signaling receptor binding; IPI:WormBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0008088; P:axo-dendritic transport; IGI:WormBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030030; P:cell projection organization; IMP:UniProtKB.
DR GO; GO:0040011; P:locomotion; IGI:WormBase.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0008104; P:protein localization; IGI:WormBase.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; Differentiation;
KW GTPase activation; Neurogenesis; Reference proteome; Synapse.
FT CHAIN 1..987
FT /note="Rho GTPase-activating protein syd-1"
FT /id="PRO_0000309560"
FT DOMAIN 123..209
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 598..722
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 755..949
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 266..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..266
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052591"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:12379863,
FT ECO:0000303|PubMed:9851916"
FT /id="VSP_052592"
FT VAR_SEQ 77..78
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:12379863,
FT ECO:0000303|PubMed:9851916"
FT /id="VSP_052593"
FT VAR_SEQ 961
FT /note="N -> SELVEFFPFLLNYPTVSYSSPNPH (in isoform b)"
FT /evidence="ECO:0000303|PubMed:12379863,
FT ECO:0000303|PubMed:9851916"
FT /id="VSP_052594"
SQ SEQUENCE 987 AA; 109299 MW; 71352844D35C966E CRC64;
MLISTSLKFL TMLTSNGFGG TNPPKGMPYP PTYLYTEEPQ NECCCCWLCR LLCCCSPVDQ
TASRSRMNAS QPPPGGGGRL PDEVFRKITA VDQGQSTLTQ SGIQGLSART LSSEPRGDLV
FQLVEIIKKP GQSLGLYLRE GNGKDRSDGV FVSRFGDNSE LAKYGEVMRP GDEILTINNV
EVSMMSIDDV VLILSIPRRL LLRIRYSKSM RHEIISSRSR ESERPVVVFH KYDDRRDSET
NAPILSQPTS TANTWLGKKS RQQMEEMRNA TTSSTLRTHA STSSPRNHFA PRLVNGHSHS
IGVPSASTTS HDHQYQRFAS EPSDSVSRTA RVPPPRLASA TVRRTESFNS APGVSTSAPM
YTLPRSSTAV PPPDILGSIP YSARDPLMRS SADLPYDPMT GRLSSSVPTD PLLSRSLCSP
ILPRTLRQAN DSNKSNSLPR RRIMTGGRNV KWRNDVVSTS DLCGEESDGA ISAPEYSSPP
FSRLTQQQQF RLSNGSPGRT VNDIFSAAEY RNWAGPYDPR GMYGPFPPGQ RATRWSHTYG
EQRAPRTSSL PGRTVLAQSL VGSPVLPRHP PPIVQDRPSA VFDRYHVSPL MNRRAPLRAA
GPGINVDRLS VSSLTGILYV HIVEGRGLKI PEKQKGLTEE MYCVLEVDEQ HRARTGVSTI
EQKFKWRETF HIDVVNATVS NFFVYSWHPQ FRHKLCHKGS LKLLEAFVVD QLNDDRVFAL
NLEPRGQLIV RIGFHDLQAV FRRTVNPRLN GVFGISLSRL VQRERRDTPI VLTRLIQEIE
KRGVDYSGLY VLCGSVEKKK MLRAELESNP LGTELAAESI PDTNVIACLI KDFLRELPEP
LISPQIHGML LEAASVALPN DVQTNRHLVL KIIDCLQLSA KNCLLLVLDH LSTVLCSSPH
NGLTPTRLSL IFAPLLFFCL DTFSPYTISP TSKMAAVRTL DINQASSSLQ MILSIWPSRV
NSESGSDSPA TTCQKGGVIA YVSESQC
