RAB3C_MOUSE
ID RAB3C_MOUSE Reviewed; 227 AA.
AC P62823; Q62858; Q62974; Q63482; Q9CXQ1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ras-related protein Rab-3C;
GN Name=Rab3c;
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 [MRNA].
RC TISSUE=Brain;
RA Wang X., Hu B., Kilimann M.W.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Schluter O.M., Benseler F., Suedhof T.C.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RA Pavlos N.J., Xu J., Zheng M.H.;
RT "Molecular cloning and tissue expression of the mouse homolog of Rab3C.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP PROTEIN SEQUENCE OF 1-16; 21-43; 50-68; 81-91; 161-175 AND 187-209, 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 [6]
RP INTERACTION WITH RIMS1; RIMS2; RPH3A AND RPH3AL.
RX PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA Fukuda M.;
RT "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT Identification of a critical determinant of Rab3A/Rab27A recognition by
RT Rim2.";
RL J. Biol. Chem. 278:15373-15380(2003).
RN [7]
RP INTERACTION WITH MADD.
RX PubMed=18849981; DOI=10.1038/ncb1785;
RA Niwa S., Tanaka Y., Hirokawa N.;
RT "KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator
RT Rab3 occurs in a GTP-dependent manner through DENN/MADD.";
RL Nat. Cell Biol. 10:1269-1279(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [9]
RP PHOSPHORYLATION AT THR-86.
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).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RIMS1, RIMS2, RPH3A and RPH3AL
CC (PubMed:12578829). Interacts with GDI2, CHM and CHML; phosphorylation
CC at Thr-86 disrupts these interactions (By similarity). Interacts with
CC MADD (via uDENN domain); the GTP-bound form is preferred for
CC interaction (PubMed:18849981). {ECO:0000250|UniProtKB:Q96E17,
CC ECO:0000269|PubMed:12578829, ECO:0000269|PubMed:18849981}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- PTM: Phosphorylation of Thr-86 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including CHM,
CC CHML and RAB GDP dissociation inhibitor GDI2.
CC {ECO:0000250|UniProtKB:Q96E17}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AJ310532; CAC32042.1; -; mRNA.
DR EMBL; AF312037; AAG60047.1; -; mRNA.
DR EMBL; AY026947; AAK08980.1; -; mRNA.
DR EMBL; AK014132; BAB29172.1; -; mRNA.
DR CCDS; CCDS26764.1; -.
DR RefSeq; NP_076341.1; NM_023852.5.
DR AlphaFoldDB; P62823; -.
DR SMR; P62823; -.
DR BioGRID; 212082; 8.
DR IntAct; P62823; 16.
DR STRING; 10090.ENSMUSP00000132945; -.
DR iPTMnet; P62823; -.
DR PhosphoSitePlus; P62823; -.
DR jPOST; P62823; -.
DR PaxDb; P62823; -.
DR PeptideAtlas; P62823; -.
DR PRIDE; P62823; -.
DR ProteomicsDB; 253147; -.
DR Antibodypedia; 23602; 136 antibodies from 27 providers.
DR DNASU; 67295; -.
DR Ensembl; ENSMUST00000167824; ENSMUSP00000132945; ENSMUSG00000021700.
DR GeneID; 67295; -.
DR KEGG; mmu:67295; -.
DR UCSC; uc007rvo.3; mouse.
DR CTD; 115827; -.
DR MGI; MGI:1914545; Rab3c.
DR VEuPathDB; HostDB:ENSMUSG00000021700; -.
DR eggNOG; KOG0093; Eukaryota.
DR GeneTree; ENSGT00940000157368; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P62823; -.
DR OMA; WQKDASD; -.
DR OrthoDB; 1218073at2759; -.
DR PhylomeDB; P62823; -.
DR TreeFam; TF313199; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 67295; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Rab3c; mouse.
DR PRO; PR:P62823; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P62823; protein.
DR Bgee; ENSMUSG00000021700; Expressed in medial dorsal nucleus of thalamus and 122 other tissues.
DR ExpressionAtlas; P62823; baseline and differential.
DR Genevisible; P62823; MM.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR CDD; cd01865; Rab3; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR037872; Rab3.
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 Cell membrane; Direct protein sequencing; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..227
FT /note="Ras-related protein Rab-3C"
FT /id="PRO_0000121086"
FT REGION 202..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 59..67
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 37..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 56..62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63012"
FT BINDING 85..89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 143..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 173..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT MOD_RES 86
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63941"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20337"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 225
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 227
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 25872 MW; 179DF4D9B451B7B0 CRC64;
MRHEAPMQMA SAQDARFGQK DSSDQNFDYM FKLLIIGNSS VGKTSFLFRY ADDSFTSAFV
STVGIDFKVK TVFKNEKRIK LQIWDTAGQE RYRTITTAYY RGAMGFILMY DITNEESFNA
VQDWSTQIKT YSWDNAQVIL AGNKCDMEDE RVVSTERGQR LGEQLGFEFF ETSAKDNINV
KQTFERLVDI ICDKMSESLE TDPAITAAKQ STRLKETPPP PQPNCGC
