ID T1D9F1_CROHD Unreviewed; 217 AA.
AC T1D9F1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ras-related protein Rab-11A {ECO:0000256|ARBA:ARBA00040050};
DE EC=3.6.5.2 {ECO:0000256|ARBA:ARBA00011984};
OS Crotalus horridus (Timber rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=35024 {ECO:0000313|EMBL:JAA95969.1};
RN [1] {ECO:0000313|EMBL:JAA95969.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:JAA95969.1};
RX PubMed=23758969; DOI=10.1186/1471-2164-14-394;
RA Rokyta D.R., Wray K.P., Margres M.J.;
RT "The genesis of an exceptionally lethal venom in the timber rattlesnake
RT (Crotalus horridus) revealed through comparative venom-gland
RT transcriptomics.";
RL BMC Genomics 14:394-394(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000249};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00000249};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Cleavage furrow
CC {ECO:0000256|ARBA:ARBA00004626}. Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004156}. Cytoplasmic vesicle, phagosome
CC {ECO:0000256|ARBA:ARBA00004262}. Golgi apparatus, trans-Golgi network
CC {ECO:0000256|ARBA:ARBA00004601}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}. Recycling endosome membrane
CC {ECO:0000256|ARBA:ARBA00004139}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004139}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000256|ARBA:ARBA00006270}.
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DR EMBL; GAAZ01001974; JAA95969.1; -; mRNA.
DR AlphaFoldDB; T1D9F1; -.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd01868; Rab11_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR47979; DRAB11-RELATED; 1.
DR PANTHER; PTHR47979:SF110; RAS-RELATED PROTEIN RAB-11A; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
DR PROSITE; PS51420; RHO; 1.
PE 2: Evidence at transcript level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT REGION 184..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 217 AA; 24469 MW; 909F1E43DAAC549F CRC64;
MGGSRDDEYD YLFKVVLIGD SGVGKSNLLS RFTRNEFNLE SKSTIGVEFA TRSIQVDGKT
IKAQIWDTAG QERYRAITSA YYRGAVGALL VYDIAKHLTY ENVERWLKEL RDHADSNIVI
MLVGNKSDLR HLRAVPTDEA RAFAEKNGLS FIETSALDST NVEAAFQTIL TEIYRIVSQK
QMSDRRENDM SPSNNVVPIH VPPTTENKPK MQCCQNI
//
