RAB8A_CHICK
ID RAB8A_CHICK Reviewed; 207 AA.
AC Q5F470;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ras-related protein Rab-8A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61006};
DE Flags: Precursor;
GN Name=RAB8A; ORFNames=RCJMB04_2k8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different sets of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab is involved in
CC polarized vesicular trafficking and neurotransmitter release.
CC {ECO:0000250|UniProtKB:P61006}.
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:0000250|UniProtKB:P61006};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P61006};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. {ECO:0000250|UniProtKB:P61006}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AJ851430; CAH65064.1; -; mRNA.
DR RefSeq; NP_001026675.1; NM_001031504.1.
DR AlphaFoldDB; Q5F470; -.
DR SMR; Q5F470; -.
DR STRING; 9031.ENSGALP00000041790; -.
DR PaxDb; Q5F470; -.
DR PRIDE; Q5F470; -.
DR Ensembl; ENSGALT00000044909; ENSGALP00000041790; ENSGALG00000028851.
DR GeneID; 428352; -.
DR KEGG; gga:428352; -.
DR CTD; 4218; -.
DR VEuPathDB; HostDB:geneid_428352; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000157246; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q5F470; -.
DR OMA; KIGQTDQ; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; Q5F470; -.
DR TreeFam; TF314097; -.
DR Reactome; R-GGA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-GGA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-GGA-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-GGA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:Q5F470; -.
DR Proteomes; UP000000539; Chromosome 28.
DR Bgee; ENSGALG00000028851; Expressed in spermatocyte and 13 other tissues.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IBA:GO_Central.
DR GO; GO:0098969; P:neurotransmitter receptor transport to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Proto-oncogene;
KW Reference proteome; Transport.
FT CHAIN 1..204
FT /note="Ras-related protein Rab-8A"
FT /id="PRO_0000260749"
FT PROPEP 205..207
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370798"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 204
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 23522 MW; CC300BE2212F7C72 CRC64;
MAKTYDYLFK LLLIGDSGVG KTCALFRFSE DAFNATFIST IGIDFKIRTI ELDGKRIKLQ
IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFENIR NWVRNIEEHA SPDVEKMILG
NKCDANDKRQ VSREQGEKLA ASFGIKFMET SAKANINIEN AFFTLARDIK AKMDKKLEGN
SPQGSNQGVK ITPDQQKKSS FFRCVLL
