RAB1A_CANLF
ID RAB1A_CANLF Reviewed; 205 AA.
AC P62822; P05711;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ras-related protein Rab-1A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62820};
GN Name=RAB1A; Synonyms=RAB1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=2123294; DOI=10.1128/mcb.10.12.6578-6585.1990;
RA Chavrier P., Vingron M., Sander C., Simons K., Zerial M.;
RT "Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell
RT line.";
RL Mol. Cell. Biol. 10:6578-6585(1990).
RN [2]
RP ISOPRENYLATION AT CYS-204 AND CYS-205.
RX PubMed=1648736; DOI=10.1073/pnas.88.14.6264;
RA Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R., Sinensky M.,
RA Balch W.E., Buss J.E., Der C.J.;
RT "Isoprenoid modification of rab proteins terminating in CC or CXC motifs.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991).
RN [3]
RP FUNCTION, MUTAGENESIS OF ASN-124, AND SUBCELLULAR LOCATION.
RX PubMed=1429835; DOI=10.1083/jcb.119.4.749;
RA Tisdale E.J., Bourne J.R., Khosravi-Far R., Der C.J., Balch W.E.;
RT "GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular
RT transport from the endoplasmic reticulum to the Golgi complex.";
RL J. Cell Biol. 119:749-761(1992).
RN [4]
RP INTERACTION WITH YIPF5.
RX PubMed=15611160; DOI=10.1534/genetics.104.032888;
RA Chen C.Z., Calero M., DeRegis C.J., Heidtman M., Barlowe C., Collins R.N.;
RT "Genetic analysis of yeast Yip1p function reveals a requirement for Golgi-
RT localized rab proteins and rab-Guanine nucleotide dissociation inhibitor.";
RL Genetics 168:1827-1841(2004).
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 (PubMed:1429835). Rabs cycle between an inactive
CC GDP-bound form and an active GTP-bound form that is able to recruit to
CC membranes different sets of downstream effectors directly responsible
CC for vesicle formation, movement, tethering and fusion (PubMed:1429835).
CC RAB1A regulates vesicular protein transport from the endoplasmic
CC reticulum (ER) to the Golgi compartment and on to the cell surface, and
CC plays a role in IL-8 and growth hormone secretion (PubMed:1429835).
CC Required to modulate the compacted morphology of the Golgi. Regulates
CC the level of CASR present at the cell membrane. Plays a role in cell
CC adhesion and cell migration, via its role in protein trafficking. Plays
CC a role in autophagosome assembly and cellular defense reactions against
CC pathogenic bacteria (By similarity). Plays a role in microtubule-
CC dependent protein transport by early endosomes and in anterograde
CC melanosome transport (By similarity). {ECO:0000250|UniProtKB:P62820,
CC ECO:0000250|UniProtKB:P62821, ECO:0000269|PubMed:1429835}.
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:P62820};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P62820};
CC -!- SUBUNIT: May interact with YIPF5 (PubMed:15611160). Interacts with
CC C9orf72; the interaction mediates recruitment of RAB1A to the ATG1/ULK1
CC kinase complex (By similarity). Interacts with GDI1; this promotes
CC dissociation from membranes (By similarity).
CC {ECO:0000250|UniProtKB:P62820, ECO:0000269|PubMed:15611160}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P62820}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P62820}. Early endosome
CC {ECO:0000250|UniProtKB:P62820}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:1429835}. Membrane {ECO:0000269|PubMed:1429835}.
CC Melanosome {ECO:0000250|UniProtKB:P62821}. Note=Alternates between
CC membrane-associated and cytosolic forms. {ECO:0000269|PubMed:1429835}.
CC -!- PTM: Phosphorylated by CDK1 kinase during mitosis.
CC {ECO:0000250|UniProtKB:P62820}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X56384; CAB56775.1; -; mRNA.
DR RefSeq; NP_001003153.1; NM_001003153.1.
DR AlphaFoldDB; P62822; -.
DR SMR; P62822; -.
DR IntAct; P62822; 2.
DR STRING; 9615.ENSCAFP00000040655; -.
DR PaxDb; P62822; -.
DR PRIDE; P62822; -.
DR Ensembl; ENSCAFT00030030532; ENSCAFP00030026622; ENSCAFG00030016473.
DR Ensembl; ENSCAFT00040010139; ENSCAFP00040008794; ENSCAFG00040005347.
DR GeneID; 403774; -.
DR KEGG; cfa:403774; -.
DR CTD; 5861; -.
DR eggNOG; KOG0084; Eukaryota.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P62822; -.
DR OrthoDB; 1149105at2759; -.
DR Reactome; R-CFA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-CFA-204005; COPII-mediated vesicle transport.
DR Reactome; R-CFA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-CFA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-CFA-8873719; RAB geranylgeranylation.
DR Reactome; R-CFA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000003187; Expressed in lymph node and 46 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0030252; P:growth hormone secretion; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0032402; P:melanosome transport; IEA:Ensembl.
DR GO; GO:1903020; P:positive regulation of glycoprotein metabolic process; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:UniProtKB.
DR GO; GO:0019068; P:virion assembly; IEA:Ensembl.
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 1: Evidence at protein level;
KW Acetylation; Autophagy; Cytoplasm; Endoplasmic reticulum; Endosome;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT CHAIN 2..205
FT /note="Ras-related protein Rab-1A"
FT /id="PRO_0000121055"
FT REGION 178..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 187..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1648736"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1648736"
FT MUTAGEN 124
FT /note="N->I: Dominant negative mutant that impairs
FT vesicular protein transport."
FT /evidence="ECO:0000269|PubMed:1429835"
SQ SEQUENCE 205 AA; 22678 MW; B2A8F4E3B0FB17D6 CRC64;
MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI
KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN NVKQWLQEID RYASENVNKL
LVGNKCDLTT KKVVDYTTAK EFADSLGIPF LETSAKNATN VEQSFMTMAA EIKKRMGPGA
TAGGAEKSNV KIQSTPVKQS GGGCC
