RAB12_CANLF
ID RAB12_CANLF Reviewed; 208 AA.
AC P51152;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ras-related protein Rab-12;
DE Flags: Fragment;
GN Name=RAB12;
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], AND SUBCELLULAR LOCATION.
RX PubMed=8126105; DOI=10.1242/jcs.106.4.1249;
RA Olkkonen V.M., Dupree P., Killisch I., Luetcke A., Simons K., Zerial M.;
RT "Molecular cloning and subcellular localization of three GTP-binding
RT proteins of the rab subfamily.";
RL J. Cell Sci. 106:1249-1261(1993).
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 set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab may play a role in
CC protein transport from recycling endosomes to lysosomes regulating, for
CC instance, the degradation of the transferrin receptor. Involved in
CC autophagy (By similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP). That Rab is
CC activated by DENND3, a guanine exchange factor (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RABIF and OPTN (By similarity). Interacts with
CC LRRK2; interaction facilitates phosphorylation of Ser-70 (By
CC similarity). Interacts with GDI1, GDI2, CHM and CHML; these
CC interactions are disrupted by phosphorylation on Ser-70 (By
CC similarity). Interacts with RILPL1 and RILPL2; these interactions are
CC dependent on phosphorylation of Ser-70 (By similarity).
CC {ECO:0000250|UniProtKB:Q6IQ22}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000305|PubMed:8126105}; Lipid-anchor
CC {ECO:0000305|PubMed:8126105}; Cytoplasmic side
CC {ECO:0000305|PubMed:8126105}. Lysosome membrane
CC {ECO:0000305|PubMed:8126105}; Lipid-anchor
CC {ECO:0000305|PubMed:8126105}; Cytoplasmic side
CC {ECO:0000305|PubMed:8126105}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:8126105}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000250|UniProtKB:P35283}.
CC -!- PTM: Phosphorylation of Ser-70 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including CHM,
CC CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.
CC {ECO:0000250|UniProtKB:Q6IQ22}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; Z22818; CAA80471.1; -; mRNA.
DR PIR; S40207; S40207.
DR AlphaFoldDB; P51152; -.
DR SMR; P51152; -.
DR STRING; 9612.ENSCAFP00000027554; -.
DR PaxDb; P51152; -.
DR PRIDE; P51152; -.
DR eggNOG; KOG0078; Eukaryota.
DR eggNOG; KOG0092; Eukaryota.
DR InParanoid; P51152; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032593; C:insulin-responsive compartment; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; ISS:UniProtKB.
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:0032482; P:Rab protein signal transduction; IEA:InterPro.
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 CDD; cd04120; Rab12; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041830; Rab12.
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 Autophagy; Cytoplasmic vesicle; Endosome; Golgi apparatus; GTP-binding;
KW Lipoprotein; Lysosome; Membrane; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN <1..208
FT /note="Ras-related protein Rab-12"
FT /id="PRO_0000121179"
FT MOTIF 35..43
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 13..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 119..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 151..152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ22"
FT LIPID 207
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 208
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 208 AA; 23834 MW; F6B3C894AB818303 CRC64;
RPADFKLQVI IIGSRGVGKT SLMERFTDDT FCEACKSTVG VDFKIKTVEL RGKKIRLQIW
DTAGQERFNS ITSAYYRSAK GIILVYDITK KETFDDLPKW MKMIDKYASE DAELLLVGNK
LDCETDREIT RQQGEKFAHE ITGMRFCEAS AKDNFNVDEI FLKLVDDILK KMPLDILRNE
LSNSILSLQP EPEIPPELPP PRPHVRCC
