RAB1C_HUMAN
ID RAB1C_HUMAN Reviewed; 201 AA.
AC Q92928;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Putative Ras-related protein Rab-1C;
DE Short=hRab1c;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62820};
GN Name=RAB1C;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-119.
RC TISSUE=Melanoma;
RX PubMed=9030196; DOI=10.1016/s0167-4889(96)00169-3;
RA Chen D., Guo J., Gahl W.A.;
RT "RAB GTPases expressed in human melanoma cells.";
RL Biochim. Biophys. Acta 1355:1-6(1997).
RN [3]
RP INTERACTION WITH L.PNEUMOPHILA ANKX (MICROBIAL INFECTION), AND
RP PHOSPHORYLATION AT SER-76 (MICROBIAL INFECTION).
RX PubMed=21822290; DOI=10.1038/nature10335;
RA Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
RT "Modulation of Rab GTPase function by a protein phosphocholine
RT transferase.";
RL Nature 477:103-106(2011).
RN [4]
RP INTERACTION WITH L.PNEUMOPHILA LEM3 (MICROBIAL INFECTION), AND
RP PHOSPHORYLATION AT SER-76 (MICROBIAL INFECTION).
RX PubMed=22158903; DOI=10.1073/pnas.1114023109;
RA Tan Y., Arnold R.J., Luo Z.Q.;
RT "Legionella pneumophila regulates the small GTPase Rab1 activity by
RT reversible phosphorylcholination.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011).
RN [5]
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).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC similarity). {ECO:0000250|UniProtKB:P62820}.
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:P62820};
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P62820}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62820}.
CC -!- PTM: (Microbial infection) Phosphocholinated at Ser-76 by L.pneumophila
CC AnkX, leading to displace GDP dissociation inhibitors (GDI)
CC (PubMed:21822290). Both GDP-bound and GTP-bound forms can be
CC phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, restoring
CC accessibility to L.pneumophila GTPase effector LepB (PubMed:22158903).
CC {ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903}.
CC -!- PTM: (Microbial infection) Glycosylated by S.typhimurium protein Ssek3:
CC arginine GlcNAcylation prevents GTPase activity, thereby disrupting
CC vesicular protein transport from the endoplasmic reticulum (ER) to the
CC Golgi compartment. {ECO:0000269|PubMed:32974215}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AL513165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U66622; AAC51197.1; -; mRNA.
DR AlphaFoldDB; Q92928; -.
DR SMR; Q92928; -.
DR IntAct; Q92928; 5.
DR MINT; Q92928; -.
DR iPTMnet; Q92928; -.
DR MetOSite; Q92928; -.
DR PhosphoSitePlus; Q92928; -.
DR SwissPalm; Q92928; -.
DR BioMuta; HGNC:23683; -.
DR jPOST; Q92928; -.
DR MassIVE; Q92928; -.
DR MaxQB; Q92928; -.
DR PeptideAtlas; Q92928; -.
DR PRIDE; Q92928; -.
DR ProteomicsDB; 75609; -.
DR GeneCards; RAB1C; -.
DR HGNC; HGNC:23683; RAB1C.
DR neXtProt; NX_Q92928; -.
DR InParanoid; Q92928; -.
DR PhylomeDB; Q92928; -.
DR PathwayCommons; Q92928; -.
DR SignaLink; Q92928; -.
DR Pharos; Q92928; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q92928; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein 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 5: Uncertain;
KW Cytoplasm; Glycoprotein; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..201
FT /note="Putative Ras-related protein Rab-1C"
FT /id="PRO_0000343568"
FT REGION 174..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 151..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 76
FT /note="(Microbial infection) O-(2-cholinephosphoryl)serine"
FT /evidence="ECO:0000269|PubMed:21822290,
FT ECO:0000269|PubMed:22158903"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62820"
SQ SEQUENCE 201 AA; 22017 MW; D6E22F1D13FBD22C CRC64;
MNPGYDCLFK LLLIGDSGVG KSCLLLRFAD DPYTESYIST IGVDFKIQTI ELDGKTIKLQ
IWDTAGQERF WTITSSYYRG AHGFLVVYDV TDQESYANVK QWLQEIDRHA SENVNKLLVG
NKSDLTTKKV VDNTTAKEFA DSLGIPFLET SAKNATNVEQ AFMTMAAEIK KQMGPGAASG
GERPNLKIDS TPVKPAGGGC C
