RAB5C_MOUSE
ID RAB5C_MOUSE Reviewed; 216 AA.
AC P35278; Q8R1V8; Q8R2N8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Ras-related protein Rab-5C;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P20339};
GN Name=Rab5c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Retina;
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 [2]
RP PROTEIN SEQUENCE OF 24-34; 83-111; 122-135; 185-196 AND 199-210, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-81.
RC TISSUE=Kidney;
RX PubMed=1555775; DOI=10.1016/0378-1119(92)90387-5;
RA Chavrier P., Simons K., Zerial M.;
RT "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed
RT by a PCR cloning approach.";
RL Gene 112:261-264(1992).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-182.
RX PubMed=11278565; DOI=10.1074/jbc.m009771200;
RA Merithew E., Hatherly S., Dumas J.J., Lawe D.C., Heller-Harrison R.,
RA Lambright D.G.;
RT "Structural plasticity of an invariant hydrophobic triad in the switch
RT regions of Rab GTPases is a determinant of effector recognition.";
RL J. Biol. Chem. 276:13982-13988(2001).
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; BC023027; AAH23027.1; -; mRNA.
DR EMBL; BC027378; AAH27378.1; -; mRNA.
DR EMBL; BC029678; AAH29678.1; -; mRNA.
DR EMBL; M79312; AAK14836.1; -; mRNA.
DR CCDS; CCDS36333.1; -.
DR PIR; JH0641; JH0641.
DR RefSeq; NP_077776.2; NM_024456.5.
DR PDB; 1HUQ; X-ray; 1.80 A; A=19-182.
DR PDB; 1Z07; X-ray; 1.81 A; A=19-182.
DR PDB; 1Z0D; X-ray; 2.20 A; A/C=19-183.
DR PDBsum; 1HUQ; -.
DR PDBsum; 1Z07; -.
DR PDBsum; 1Z0D; -.
DR AlphaFoldDB; P35278; -.
DR SMR; P35278; -.
DR BioGRID; 202549; 126.
DR DIP; DIP-56521N; -.
DR IntAct; P35278; 139.
DR MINT; P35278; -.
DR STRING; 10090.ENSMUSP00000019317; -.
DR iPTMnet; P35278; -.
DR PhosphoSitePlus; P35278; -.
DR SwissPalm; P35278; -.
DR EPD; P35278; -.
DR jPOST; P35278; -.
DR PaxDb; P35278; -.
DR PeptideAtlas; P35278; -.
DR PRIDE; P35278; -.
DR ProteomicsDB; 300228; -.
DR Antibodypedia; 1113; 243 antibodies from 30 providers.
DR DNASU; 19345; -.
DR Ensembl; ENSMUST00000107364; ENSMUSP00000102987; ENSMUSG00000019173.
DR GeneID; 19345; -.
DR KEGG; mmu:19345; -.
DR UCSC; uc007lme.2; mouse.
DR CTD; 5878; -.
DR MGI; MGI:105306; Rab5c.
DR VEuPathDB; HostDB:ENSMUSG00000019173; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000154971; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P35278; -.
DR OMA; TYAEEES; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 19345; 10 hits in 58 CRISPR screens.
DR ChiTaRS; Rab5c; mouse.
DR EvolutionaryTrace; P35278; -.
DR PRO; PR:P35278; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P35278; protein.
DR Bgee; ENSMUSG00000019173; Expressed in embryonic brain and 246 other tissues.
DR ExpressionAtlas; P35278; baseline and differential.
DR Genevisible; P35278; MM.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0007032; P:endosome organization; IDA:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0048227; P:plasma membrane to endosome transport; ISO:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; IDA:MGI.
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 3D-structure; Cell membrane; Direct protein sequencing; Endosome;
KW GTP-binding; Hydrolase; Lipoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..216
FT /note="Ras-related protein Rab-5C"
FT /id="PRO_0000121111"
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 202..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"
FT STRAND 20..29
FT /evidence="ECO:0007829|PDB:1HUQ"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:1HUQ"
FT STRAND 54..65
FT /evidence="ECO:0007829|PDB:1HUQ"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:1HUQ"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:1HUQ"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:1HUQ"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:1HUQ"
FT HELIX 106..122
FT /evidence="ECO:0007829|PDB:1HUQ"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1HUQ"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1HUQ"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:1HUQ"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1HUQ"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1HUQ"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:1HUQ"
SQ SEQUENCE 216 AA; 23413 MW; AA5658239D8D77ED CRC64;
MAGRGGAARP NGPAAGNKIC QFKLVLLGES AVGKSSLVLR FVKGQFHEYQ ESTIGAAFLT
QTVCLDDTTV KFEIWDTAGQ ERYHSLAPMY YRGAQAAIVV YDITNTDTFA RAKNWVKELQ
RQASPNIVIA LAGNKADLAS KRAVEFQEAQ AYADDNSLLF METSAKTAMN VNEIFMAIAK
KLPKNEPQNA AGAPGRTRGV DLQESNPASR SQCCSN
