RAB1A_RAT
ID RAB1A_RAT Reviewed; 205 AA.
AC Q6NYB7; P05711;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ras-related protein Rab-1A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62820};
GN Name=Rab1A; Synonyms=Rab1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3317403; DOI=10.1073/pnas.84.23.8210;
RA Touchot N., Chardin P., Tavitian A.;
RT "Four additional members of the ras gene superfamily isolated by an
RT oligonucleotide strategy: molecular cloning of YPT-related cDNAs from a rat
RT brain library.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8210-8214(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21303926; DOI=10.1242/jcs.079020;
RA Mukhopadhyay A., Nieves E., Che F.Y., Wang J., Jin L., Murray J.W.,
RA Gordon K., Angeletti R.H., Wolkoff A.W.;
RT "Proteomic analysis of endocytic vesicles: Rab1a regulates motility of
RT early endocytic vesicles.";
RL J. Cell Sci. 124:765-775(2011).
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:21303926). 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
CC (PubMed:21303926). RAB1A regulates vesicular protein transport from the
CC endoplasmic reticulum (ER) to the Golgi compartment and on to the cell
CC surface, and plays a role in IL-8 and growth hormone secretion
CC (PubMed:21303926). Required to modulate the compacted morphology of the
CC Golgi. Regulates the level of CASR present at the cell membrane (By
CC similarity). Plays a role in cell adhesion and cell migration, via its
CC role in protein trafficking (By similarity). Plays a role in
CC 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:21303926}.
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. Interacts with C9orf72; the
CC interaction mediates recruitment of RAB1A to the ATG1/ULK1 kinase
CC complex. Interacts with GDI1; this promotes dissociation from
CC membranes. {ECO:0000250|UniProtKB:P62820,
CC ECO:0000250|UniProtKB:P62822}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P62820}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P62820}. Early endosome
CC {ECO:0000269|PubMed:21303926}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P62820}. Membrane
CC {ECO:0000250|UniProtKB:P62820}. Melanosome
CC {ECO:0000250|UniProtKB:P62821}. Note=Alternates between membrane-
CC associated and cytosolic forms. {ECO:0000250|UniProtKB:P62820}.
CC -!- TISSUE SPECIFICITY: Expressed in flagella of epididymal sperm.
CC {ECO:0000269|PubMed:19423663}.
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; J02998; AAA42006.1; -; mRNA.
DR EMBL; BC066662; AAH66662.1; -; mRNA.
DR PIR; A39963; TVRTYP.
DR RefSeq; NP_112352.2; NM_031090.2.
DR AlphaFoldDB; Q6NYB7; -.
DR SMR; Q6NYB7; -.
DR BioGRID; 249626; 4.
DR CORUM; Q6NYB7; -.
DR IntAct; Q6NYB7; 2.
DR MINT; Q6NYB7; -.
DR iPTMnet; Q6NYB7; -.
DR PhosphoSitePlus; Q6NYB7; -.
DR jPOST; Q6NYB7; -.
DR PRIDE; Q6NYB7; -.
DR Ensembl; ENSRNOT00000103721; ENSRNOP00000080734; ENSRNOG00000004992.
DR GeneID; 81754; -.
DR KEGG; rno:81754; -.
DR UCSC; RGD:619736; rat.
DR CTD; 5861; -.
DR RGD; 619736; Rab1.
DR GeneTree; ENSGT00940000154958; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q6NYB7; -.
DR OrthoDB; 1149105at2759; -.
DR PhylomeDB; Q6NYB7; -.
DR Reactome; R-RNO-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:Q6NYB7; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000004992; Expressed in stomach and 20 other tissues.
DR ExpressionAtlas; Q6NYB7; baseline and differential.
DR Genevisible; Q6NYB7; RN.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0042470; C:melanosome; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IDA:SynGO-UCL.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:MGI.
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; ISO:RGD.
DR GO; GO:1903020; P:positive regulation of glycoprotein metabolic process; ISO:RGD.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0032482; P:Rab protein signal transduction; IC:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB.
DR GO; GO:0019068; P:virion assembly; ISO:RGD.
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_0000121059"
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; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT CONFLICT 158..159
FT /note="AT -> EK (in Ref. 1; AAA42006)"
FT /evidence="ECO:0000305"
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
