SYD1_CAEBR
ID SYD1_CAEBR Reviewed; 962 AA.
AC Q61CA4; A8XGV5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Rho GTPase-activating protein syd-1;
DE AltName: Full=Synapse defective protein 1;
GN Name=syd-1 {ECO:0000250|UniProtKB:Q86NH1}; ORFNames=CBG13003;
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: 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:Q86NH1}.
CC Note=Presynaptic terminals. {ECO:0000250|UniProtKB:Q86NH1}.
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DR EMBL; HE600938; CAP31879.3; -; Genomic_DNA.
DR AlphaFoldDB; Q61CA4; -.
DR SMR; Q61CA4; -.
DR STRING; 6238.CBG13003; -.
DR WormBase; CBG13003a; CBP46422; WBGene00033849; Cbr-syd-1.
DR eggNOG; KOG1452; Eukaryota.
DR eggNOG; KOG3528; Eukaryota.
DR HOGENOM; CLU_003464_0_0_1; -.
DR InParanoid; Q61CA4; -.
DR OMA; GLTEEMY; -.
DR OrthoDB; 1181644at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0097060; C:synaptic membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 3: Inferred from homology;
KW Developmental protein; Differentiation; GTPase activation; Neurogenesis;
KW Reference proteome; Synapse.
FT CHAIN 1..962
FT /note="Rho GTPase-activating protein syd-1"
FT /id="PRO_0000309559"
FT DOMAIN 572..696
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 729..923
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 231..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 106449 MW; 72CA1657A6845AD8 CRC64;
MLPLQGFNMT YPRKGVMPYP STFLYREEPS VSTTECCCCW LCRLLCCCST VDSQTALRDR
MNASQPPPGG GGRLPDEVYR KIKAVDQGQS TLTQSGIQGL SARTLDENQR GDLVFQLVEI
IKKPGQSLGL YLREGNGKDR SDGVFVSRFG DNSELAKSFL MSIDDVVLIL SIPRRLLLRI
RFSKSMRHEV ITSRSSERPV VVFHKYDDRR DSETNAPILS QPTSTANTWL GKKSRQQMEE
MRNATTTSTM RAAHASTSSP RNHFAPRLVN GHSQPIGVPS ASSASTSDHH YQRFASEPSD
SVSRTARVPP PRLASATVRR TESFNSAPGV SSSAPMYTLP RSSTAVPPPD IIGSIPHSAR
DPLMRSDLPY DPLTGRLSSS VPTDPLLSRS LCSPILPRTL RQPNDSNKSN SLPRRRIMTG
GRNVKWRNDV VSTSDLCGEE SDGAISAPEY SSPPFSRLTQ QQQFRLSNGS PGRTVNDIFS
AAEYRNWAGP YDPRGMYGPY PPGQRTTRWS HTYGEQRAPR TSSLPGRTVL AQSLVGSPVL
PRHPPPIVQD RPSAVFDRYH VSPLMNRRAP LRAAGPGINV DRLSVSSLTG ILYVHILEGR
GLKIPEKQKG LTEEMYCVLE VDEQHRARTG VSTIEQKFKW RETFHIDVVN ATVSNFFVYS
WHPQFRHKLC HKGSLKLLEA FVVDQLNDDR VFALNLEPRG QLIVRIGFHD LQAVFRRTVN
PRLNGVFGVP LGRLVQRERR DTPIVLTRLI QEIEKRGVDL SGLYVLCGSV EKKKMLRAQL
ESNPLGTDLN AENIPDTNVI ACLIKDFLRE LPEPLISPQI HGMLLEAATV ALPNDVQANR
TLVLKIIDCL QLSAKNCLLL VLDHLSTILC SSPHNGLTPT RLSLIFAPLL FFCLDAISPY
TTSPTSKMAA VRSLDMNQAS SSLQMILSIW PSRVNSESGS DSPATSGQKG GGGVSYVSES
QC