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   27-MAR-2024, entry version 194.
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,
RC   Pancreas, 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; 129.
DR   DIP; DIP-56521N; -.
DR   IntAct; P35278; 140.
DR   MINT; P35278; -.
DR   STRING; 10090.ENSMUSP00000019317; -.
DR   GlyGen; P35278; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P35278; -.
DR   PhosphoSitePlus; P35278; -.
DR   SwissPalm; P35278; -.
DR   EPD; P35278; -.
DR   jPOST; P35278; -.
DR   PaxDb; 10090-ENSMUSP00000019317; -.
DR   PeptideAtlas; P35278; -.
DR   ProteomicsDB; 300228; -.
DR   Pumba; P35278; -.
DR   Antibodypedia; 1113; 277 antibodies from 30 providers.
DR   DNASU; 19345; -.
DR   Ensembl; ENSMUST00000107364.8; ENSMUSP00000102987.2; ENSMUSG00000019173.12.
DR   GeneID; 19345; -.
DR   KEGG; mmu:19345; -.
DR   UCSC; uc007lme.2; mouse.
DR   AGR; MGI:105306; -.
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; DTFHDNT; -.
DR   OrthoDB; 5483572at2759; -.
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; 11 hits in 61 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 250 other cell types or tissues.
DR   ExpressionAtlas; P35278; baseline and differential.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
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   CDD; cd01860; Rab5_related; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47978; -; 1.
DR   PANTHER; PTHR47978:SF65; RAB43, MEMBER RAS ONCOGENE FAMILY; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   Genevisible; P35278; MM.
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
//