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RAB5C_BOVIN
ID   RAB5C_BOVIN             Reviewed;         216 AA.
AC   Q58DS9; Q17QR1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Ras-related protein Rab-5C;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P20339};
GN   Name=RAB5C;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; BT021518; AAX46365.1; -; mRNA.
DR   EMBL; BC118226; AAI18227.1; -; mRNA.
DR   RefSeq; NP_001029915.1; NM_001034743.2.
DR   RefSeq; XP_005220807.1; XM_005220750.2.
DR   RefSeq; XP_005220808.1; XM_005220751.3.
DR   AlphaFoldDB; Q58DS9; -.
DR   SMR; Q58DS9; -.
DR   STRING; 9913.ENSBTAP00000015581; -.
DR   PaxDb; Q58DS9; -.
DR   PeptideAtlas; Q58DS9; -.
DR   PRIDE; Q58DS9; -.
DR   Ensembl; ENSBTAT00000015581; ENSBTAP00000015581; ENSBTAG00000006982.
DR   GeneID; 613749; -.
DR   KEGG; bta:613749; -.
DR   CTD; 5878; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006982; -.
DR   VGNC; VGNC:50253; RAB5C.
DR   eggNOG; KOG0092; Eukaryota.
DR   GeneTree; ENSGT00940000154971; -.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; Q58DS9; -.
DR   OrthoDB; 1340129at2759; -.
DR   TreeFam; TF300199; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000006982; Expressed in monocyte and 107 other tissues.
DR   ExpressionAtlas; Q58DS9; baseline and differential.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
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:0032456; P:endocytic recycling; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   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_0000226291"
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"
SQ   SEQUENCE   216 AA;  23467 MW;  AA57E9996EED76EC CRC64;
     MAGRGGAARP NGPAAGNKIC QFKLVLLGES AVGKSSLVLR FVKGQFHEYQ ESTIGAAFLT
     QTVCLDDTTV KFEIWDTAGQ ERYHSLAPMY YRGAQAAIVV YDITNTDTFA RAKNWVKELQ
     RQASPNIVIA LAGNKADLAS KRAVEFQEAQ AYAEDNSLLF METSAKTAMN VNEIFMAIAK
     KLPKNEPQNA AGAPGRNRGV DLQENNPASR SQCCSN
 
 
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