RAB1A_PIG
ID RAB1A_PIG Reviewed; 205 AA.
AC Q52NJ2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ras-related protein Rab-1A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62820};
GN Name=RAB1A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Liu G.Y., Xiong Z.Y.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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. RAB1A regulates vesicular
CC protein transport from the endoplasmic reticulum (ER) to the Golgi
CC compartment and on to the cell surface, and plays a role in IL-8 and
CC growth hormone secretion. Required to modulate the compacted morphology
CC of the Golgi (By similarity). Regulates the level of CASR present at
CC the cell membrane. Plays a role in cell adhesion and cell migration,
CC via its role in protein trafficking. Plays a role in autophagosome
CC assembly and cellular defense reactions against pathogenic bacteria (By
CC similarity). Plays a role in microtubule-dependent protein transport by
CC early endosomes and in anterograde melanosome transport (By
CC similarity). {ECO:0000250|UniProtKB:P62820,
CC ECO:0000250|UniProtKB:P62821}.
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:0000250|UniProtKB:P62820}. 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 -!- 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; AY996813; AAY17509.1; -; mRNA.
DR RefSeq; NP_001026957.1; NM_001031787.1.
DR AlphaFoldDB; Q52NJ2; -.
DR SMR; Q52NJ2; -.
DR STRING; 9823.ENSSSCP00000008922; -.
DR PaxDb; Q52NJ2; -.
DR PeptideAtlas; Q52NJ2; -.
DR PRIDE; Q52NJ2; -.
DR GeneID; 595116; -.
DR KEGG; ssc:595116; -.
DR CTD; 5861; -.
DR eggNOG; KOG0084; Eukaryota.
DR InParanoid; Q52NJ2; -.
DR OrthoDB; 1149105at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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: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: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:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; 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 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_0000121058"
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"
SQ SEQUENCE 205 AA; 22606 MW; 64739ADB525B3F74 CRC64;
MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI
KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQGSFN NVKQWLQEID RYASENVNKL
LVGNKCDLTT KKVVDYTTAK EFADSLGIPF LETSAKNATN VEQSFMTMAA EIKKRMGPGA
TAGGAEKSNV KIQSTPVKQS GGGCC
