ID A0A8S1FE52_9PELO Unreviewed; 916 AA.
AC A0A8S1FE52;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 10-JUN-2026, entry version 14.
DE RecName: Full=Rho GTPase-activating protein syd-1 {ECO:0000256|ARBA:ARBA00067645};
DE AltName: Full=Synapse defective protein 1 {ECO:0000256|ARBA:ARBA00081459};
GN ORFNames=CBOVIS_LOCUS12723 {ECO:0000313|EMBL:CAB3411317.1};
OS Caenorhabditis bovis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=2654633 {ECO:0000313|EMBL:CAB3411317.1, ECO:0000313|Proteomes:UP000494206};
RN [1] {ECO:0000313|EMBL:CAB3411317.1, ECO:0000313|Proteomes:UP000494206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00053220}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAB3411317.1}.
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DR EMBL; CADEPM010000013; CAB3411317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8S1FE52; -.
DR OrthoDB; 120383at2759; -.
DR Proteomes; UP000494206; Unassembled WGS sequence.
DR GO; GO:0097060; C:synaptic membrane; IEA:TreeGrafter.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0030030; P:cell projection organization; IEA:TreeGrafter.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IEA:TreeGrafter.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06718; PDZ_Par6-like; 1.
DR FunFam; 1.10.555.10:FF:000031; rho GTPase-activating protein 100F isoform X6; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR052118; Rho-GAP_regulator.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR057459; SYDE1/2_C2.
DR PANTHER; PTHR46150; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR PANTHER; PTHR46150:SF3; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR Pfam; PF25336; C2_SYDE; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468, ECO:0000256|PROSITE-
KW ProRule:PRU00172}; Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Reference proteome {ECO:0000313|Proteomes:UP000494206}.
FT DOMAIN 57..128
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 528..652
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 685..890
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 167..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..223
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..428
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 101340 MW; ED1CF85719B39510 CRC64;
MISSQPPPGG GGRLPDEVFR KITSVDQGTS TLTQAGIQGL SARILDKDVR GDVVIQFVEI
IKKPGQSLGL YLREGNGKDR FDGVFVSRFG ETSHLAKYGD VIRPGDEILT INNVEVSNMG
IDDVVLILSI PRRLLLRIRF SKSTRHELPI SNRAVERPVV VFHKVEERRE SESNSNAPIL
SQPTSTANTW LGKKSRQQME EMRSGTLRSS STQQQQQVSP RSQYAPRLLN GHAHPINSSE
PTTGGTYQRF ASEPSDSITR TARVPPPRLQ SATVRRTESF NSAPGASTTA TMYTLPRSST
AVPPPDMMNA SRVPLTAREP LMRNDYDPMM GGRMATNAAD ALLSRSWCSP ILPRSLRPTA
DHKSNSLPRR RLMSGTGDRF VGARKVKWRN DVVATELCGE ESDGAISAPE YSSPSFSRLS
QQQQFRLSNG SPGRTVNDIF SAAEYRNWAG PYDPRANYSG RATRWSHTYG EQRAPRTSSL
PGRTILAQSL VGSPVLPRHP QPIVQERPSA VFDRYHVSPL MNRRAPLRAA GPGINIDRLN
VSSLTGILFV QILEGRGLKI PEKQKGLTEE MYCVLEVDEQ HRARTGVSTI EQKFRWRETF
HIDVVNATVT NFFVYSWHPQ FRHKLCHKGS LKLLEAFVVD QLNGDRMFAL NLEPRGQLIV
RIGFHDMASV FRRTVNPRLD GVFGVPLSRL IHRERRDTPI VLTRLIQEIE KRGVDNNGLY
VLCGSVEKKR MLRDELEANP LGTELGADSI PDTNVIACLV KDFLRELPEP LISPQIHAML
LDAASVALPN DVQANRALVL RIIDCLTLAC KNCLLLVLDH LVTVLSSSPH NGLSPSRLST
IFAPLLFCCL DSMSPYPSSP TSKSTTVRCL DVAQASASLQ MILSIWPTRV SSESGSDSPA
TASQKGASVY VSESQC
//
