RAB5C_HUMAN
ID RAB5C_HUMAN Reviewed; 216 AA.
AC P51148; F8W1H5; Q6FH55; Q9P0Y5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Ras-related protein Rab-5C;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P20339};
DE AltName: Full=L1880;
DE AltName: Full=RAB5L;
GN Name=RAB5C; Synonyms=RABL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8646882; DOI=10.1159/000134325;
RA Han H.J., Sudo K., Inazawa J., Nakamura Y.;
RT "Isolation and mapping of a human gene (RABL) encoding a small GTP-binding
RT protein homologous to the Ras-related RAB gene.";
RL Cytogenet. Cell Genet. 73:137-139(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7951316; DOI=10.1038/ng0894-472;
RA Albertsen H.M., Smith S.A., Mazoyer S., Fujimoto E., Stevens J.,
RA Williams B., Rodriguez P., Cropp C.S., Slijepcevic P., Carlson M.,
RA Robertson M., Bradley P., Lawrence E., Harrington T., Sheng Z.M.,
RA Hoopes R., Sternberg N., Brothman A., Callahan R., Ponder B.A.J., White R.;
RT "A physical map and candidate genes in the BRCA1 region on chromosome
RT 17q12-21.";
RL Nat. Genet. 7:472-479(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=10768959; DOI=10.1128/iai.68.5.2671-2684.2000;
RA Clemens D.L., Lee B.-Y., Horwitz M.A.;
RT "Deviant expression of Rab5 on phagosomes containing the intracellular
RT pathogens Mycobacterium tuberculosis and Legionella pneumophila is
RT associated with altered phagosomal fate.";
RL Infect. Immun. 68:2671-2684(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [11]
RP INTERACTION WITH EEA1.
RX PubMed=12493736; DOI=10.1074/jbc.m211514200;
RA Merithew E., Stone C., Eathiraj S., Lambright D.G.;
RT "Determinants of Rab5 interaction with the N-terminus of early endosome
RT antigen 1.";
RL J. Biol. Chem. 278:8494-8500(2003).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP INTERACTION WITH INCA1.
RX PubMed=21750715; DOI=10.1371/journal.pone.0021505;
RA Zhang F., Baeumer N., Rode M., Ji P., Zhang T., Berdel W.E.,
RA Mueller-Tidow C.;
RT "The inhibitor of growth protein 5 (ING5) depends on INCA1 as a co-factor
RT for its antiproliferative effects.";
RL PLoS ONE 6:E21505-E21505(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP INTERACTION WITH GDI1; GDI2; CHML AND CHM, PHOSPHORYLATION AT SER-85, AND
RP MUTAGENESIS OF SER-85.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
RN [17]
RP GLYCOSYLATION (MICROBIAL INFECTION).
RX PubMed=32974215; DOI=10.3389/fcimb.2020.00419;
RA Gan J., Scott N.E., Newson J.P.M., Wibawa R.R., Wong Fok Lung T.,
RA Pollock G.L., Ng G.Z., van Driel I., Pearson J.S., Hartland E.L.,
RA Giogha C.;
RT "The Salmonella effector SseK3 targets small Rab GTPases.";
RL Front. Cell. Infect. Microbiol. 10:419-419(2020).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-40.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 (PubMed:12493736). Interacts with INCA1
CC (PubMed:21750715). Interacts with GDI1, GDI2, CHML and CHM;
CC phosphorylation at Ser-85 disrupts this interaction (PubMed:29125462).
CC {ECO:0000269|PubMed:12493736, ECO:0000269|PubMed:21750715,
CC ECO:0000269|PubMed:29125462}.
CC -!- INTERACTION:
CC P51148; Q60I27: ALS2CL; NbExp=3; IntAct=EBI-1054923, EBI-12078276;
CC P51148; Q8NEU8: APPL2; NbExp=8; IntAct=EBI-1054923, EBI-741261;
CC P51148; Q15075: EEA1; NbExp=3; IntAct=EBI-1054923, EBI-298113;
CC P51148; Q0VD86: INCA1; NbExp=2; IntAct=EBI-1054923, EBI-6509505;
CC P51148; Q5ZRP9: vipD; Xeno; NbExp=7; IntAct=EBI-1054923, EBI-26364295;
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:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV.
CC {ECO:0000269|PubMed:17081065}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51148-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51148-2; Sequence=VSP_046035;
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:0000269|PubMed:29125462}.
CC -!- PTM: (Microbial infection) Glycosylated on arginine residues by
CC S.typhimurium protein Ssek3. {ECO:0000269|PubMed:32974215}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; U18420; AAB08927.1; -; mRNA.
DR EMBL; U11293; AAA74081.1; -; mRNA.
DR EMBL; AF141304; AAF66594.1; -; mRNA.
DR EMBL; AF498938; AAM21086.1; -; mRNA.
DR EMBL; AK310234; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR541901; CAG46699.1; -; mRNA.
DR EMBL; BT019484; AAV38291.1; -; mRNA.
DR EMBL; AC003104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60805.1; -; Genomic_DNA.
DR EMBL; BC106039; AAI06040.1; -; mRNA.
DR EMBL; BC114439; AAI14440.1; -; mRNA.
DR CCDS; CCDS11419.1; -. [P51148-1]
DR CCDS; CCDS58551.1; -. [P51148-2]
DR PIR; I38703; I38703.
DR RefSeq; NP_001238968.1; NM_001252039.1. [P51148-2]
DR RefSeq; NP_004574.2; NM_004583.3. [P51148-1]
DR RefSeq; NP_958842.1; NM_201434.2. [P51148-1]
DR RefSeq; XP_011523392.1; XM_011525090.1.
DR RefSeq; XP_011523393.1; XM_011525091.1.
DR PDB; 4KYI; X-ray; 3.08 A; B/D/F/H=18-182.
DR PDBsum; 4KYI; -.
DR AlphaFoldDB; P51148; -.
DR SMR; P51148; -.
DR BioGRID; 111816; 572.
DR IntAct; P51148; 155.
DR MINT; P51148; -.
DR STRING; 9606.ENSP00000447053; -.
DR GlyGen; P51148; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51148; -.
DR MetOSite; P51148; -.
DR PhosphoSitePlus; P51148; -.
DR SwissPalm; P51148; -.
DR BioMuta; RAB5C; -.
DR DMDM; 38258923; -.
DR EPD; P51148; -.
DR jPOST; P51148; -.
DR MassIVE; P51148; -.
DR MaxQB; P51148; -.
DR PaxDb; P51148; -.
DR PeptideAtlas; P51148; -.
DR PRIDE; P51148; -.
DR ProteomicsDB; 29618; -.
DR ProteomicsDB; 56283; -. [P51148-1]
DR TopDownProteomics; P51148-1; -. [P51148-1]
DR Antibodypedia; 1113; 243 antibodies from 30 providers.
DR DNASU; 5878; -.
DR Ensembl; ENST00000346213.9; ENSP00000345689.5; ENSG00000108774.15. [P51148-1]
DR Ensembl; ENST00000393860.7; ENSP00000377440.3; ENSG00000108774.15. [P51148-1]
DR Ensembl; ENST00000547517.5; ENSP00000447053.1; ENSG00000108774.15. [P51148-2]
DR GeneID; 5878; -.
DR KEGG; hsa:5878; -.
DR MANE-Select; ENST00000346213.9; ENSP00000345689.5; NM_004583.4; NP_004574.2.
DR UCSC; uc002hza.4; human. [P51148-1]
DR CTD; 5878; -.
DR DisGeNET; 5878; -.
DR GeneCards; RAB5C; -.
DR HGNC; HGNC:9785; RAB5C.
DR HPA; ENSG00000108774; Low tissue specificity.
DR MIM; 604037; gene.
DR neXtProt; NX_P51148; -.
DR OpenTargets; ENSG00000108774; -.
DR PharmGKB; PA34145; -.
DR VEuPathDB; HostDB:ENSG00000108774; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000154971; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P51148; -.
DR OMA; TYAEEES; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; P51148; -.
DR TreeFam; TF300199; -.
DR PathwayCommons; P51148; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P51148; -.
DR SIGNOR; P51148; -.
DR BioGRID-ORCS; 5878; 73 hits in 1086 CRISPR screens.
DR ChiTaRS; RAB5C; human.
DR GeneWiki; RAB5C; -.
DR GenomeRNAi; 5878; -.
DR Pharos; P51148; Tbio.
DR PRO; PR:P51148; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P51148; protein.
DR Bgee; ENSG00000108774; Expressed in monocyte and 204 other tissues.
DR ExpressionAtlas; P51148; baseline and differential.
DR Genevisible; P51148; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
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; IMP:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Endosome; Glycoprotein;
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_0000121110"
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; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462"
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 VAR_SEQ 1
FT /note="M -> MELSWRSPSPLSASLHSTSPHPHALWTTTAGRAM (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046035"
FT VARIANT 40
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1280509335)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036414"
FT MUTAGEN 85
FT /note="S->A: Loss of phosphorylation. No effect on GDI1,
FT GDI2, CHML and CHM binding."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 85
FT /note="S->E: Phosphomimetic mutant. Loss of GDI1, GDI2,
FT CHML and CHM binding."
FT /evidence="ECO:0000269|PubMed:29125462"
FT CONFLICT 8
FT /note="A -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:4KYI"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:4KYI"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:4KYI"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:4KYI"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:4KYI"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:4KYI"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:4KYI"
FT HELIX 106..122
FT /evidence="ECO:0007829|PDB:4KYI"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:4KYI"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4KYI"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:4KYI"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4KYI"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:4KYI"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:4KYI"
SQ SEQUENCE 216 AA; 23483 MW; AA42096C6EED77ED CRC64;
MAGRGGAARP NGPAAGNKIC QFKLVLLGES AVGKSSLVLR FVKGQFHEYQ ESTIGAAFLT
QTVCLDDTTV KFEIWDTAGQ ERYHSLAPMY YRGAQAAIVV YDITNTDTFA RAKNWVKELQ
RQASPNIVIA LAGNKADLAS KRAVEFQEAQ AYADDNSLLF METSAKTAMN VNEIFMAIAK
KLPKNEPQNA TGAPGRNRGV DLQENNPASR SQCCSN
