RAB5C_CANLF
ID RAB5C_CANLF Reviewed; 216 AA.
AC P51147;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ras-related protein Rab-5C;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P20339};
GN Name=RAB5C;
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].
RX PubMed=7789520; DOI=10.1016/0014-5793(95)00477-q;
RA Bucci C., Lutcke A., Steele Mortimer O., Olkkonen V.M., Dupree P.,
RA Chiariello M., Bruni C.B., Simons K., Zerial M.;
RT "Co-operative regulation of endocytosis by three Rab5 isoforms.";
RL FEBS Lett. 366:65-71(1995).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic.
CC {ECO:0000250|UniProtKB:P20339}.
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:P20339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P20339};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP.
CC {ECO:0000250|UniProtKB:P18066}.
CC -!- SUBUNIT: Interacts with EEA1 and INCA1 (By similarity). Interacts with
CC GDI1, GDI2, CHML and CHM; phosphorylation at Ser-85 disrupts this
CC interaction (By similarity). {ECO:0000250|UniProtKB:P51148}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20339};
CC Lipid-anchor {ECO:0000250|UniProtKB:P20339}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P20339}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P20339}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P20339}. Melanosome
CC {ECO:0000250|UniProtKB:P51148}.
CC -!- PTM: Phosphorylation of Ser-85 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:P51148}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; Z27110; CAA81626.1; -; mRNA.
DR PIR; S65933; S65933.
DR RefSeq; NP_001003261.1; NM_001003261.1.
DR RefSeq; XP_005624384.1; XM_005624327.2.
DR RefSeq; XP_013971941.1; XM_014116466.1.
DR AlphaFoldDB; P51147; -.
DR SMR; P51147; -.
DR STRING; 9615.ENSCAFP00000022977; -.
DR PaxDb; P51147; -.
DR PRIDE; P51147; -.
DR Ensembl; ENSCAFT00030000322; ENSCAFP00030000278; ENSCAFG00030000204.
DR Ensembl; ENSCAFT00040016248; ENSCAFP00040014080; ENSCAFG00040008714.
DR Ensembl; ENSCAFT00845018023; ENSCAFP00845014042; ENSCAFG00845010240.
DR GeneID; 403941; -.
DR KEGG; cfa:403941; -.
DR CTD; 5878; -.
DR VEuPathDB; HostDB:ENSCAFG00845010240; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000154971; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P51147; -.
DR OMA; TYAEEES; -.
DR OrthoDB; 1340129at2759; -.
DR TreeFam; TF300199; -.
DR Reactome; R-CFA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-CFA-6798695; Neutrophil degranulation.
DR Reactome; R-CFA-8854214; TBC/RABGAPs.
DR Reactome; R-CFA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-CFA-8873719; RAB geranylgeranylation.
DR Reactome; R-CFA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000015629; Expressed in granulocyte and 46 other tissues.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
DR GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
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:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0048227; P:plasma membrane to endosome transport; IEA:Ensembl.
DR GO; GO:0030100; P:regulation of endocytosis; 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; Endosome; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..216
FT /note="Ras-related protein Rab-5C"
FT /id="PRO_0000121109"
FT REGION 185..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 50..58
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 199..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28..36
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT BINDING 47..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT BINDING 76..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT BINDING 164..166
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51148"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P20339"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P20339"
SQ SEQUENCE 216 AA; 23456 MW; AA5642006EF7AD2D CRC64;
MAGRGGAARP NGPAAGNKIC QFKLVLLGES AVGKSSLVLR FVKGQFHEYQ ESTIGAAFLT
QTVCLDDTTV KFEIWDTAGQ ERYHSLAPMY YRGAQAAIVV YDITNTDTFA RAKNWVKELQ
RQASPNIVIA LAGNKADLAS KRAVEFQEAQ AYADDNSLLF METSAKTAMN VNEIFMAIAK
KLPKNEPQNA AGAPSRNRGV DLQENSPASR SQCCSN
