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   02-SEP-2026, entry version 168.
DE   RecName: Full=Ras-related protein Rab-3C;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P10949};
GN   Name=Rab3c {ECO:0000312|MGI:MGI:1914545};
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: The small GTPases Rab are key regulators of intracellular
CC       membrane trafficking, from the formation of transport vesicles to their
CC       fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC       and an active GTP-bound form that is able to recruit to membranes
CC       different sets of downstream effectors directly responsible for vesicle
CC       formation, movement, tethering and fusion.
CC       {ECO:0000250|UniProtKB:P10949}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); 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:P10949};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P10949};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P10949};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) which promote the exchange of bound GDP for free GTP. Regulated
CC       by GTPase activating proteins (GAPs) which increase the GTP hydrolysis
CC       activity. Inhibited by GDP dissociation inhibitors (GDIs) which prevent
CC       Rab-GDP dissociation. {ECO:0000250|UniProtKB:P20336}.
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   -!- DOMAIN: Switch 1, switch 2 and the interswitch regions are
CC       characteristic of Rab GTPases and mediate the interactions with Rab
CC       downstream effectors. The switch regions undergo conformational changes
CC       upon nucleotide binding which drives interaction with specific sets of
CC       effector proteins, with most effectors only binding to GTP-bound Rab.
CC       {ECO:0000250|UniProtKB:P10949}.
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; 10.
DR   FunCoup; P62823; 1001.
DR   IntAct; P62823; 16.
DR   STRING; 10090.ENSMUSP00000132945; -.
DR   GlyGen; P62823; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62823; -.
DR   MetOSite; P62823; -.
DR   PhosphoSitePlus; P62823; -.
DR   SwissPalm; P62823; -.
DR   jPOST; P62823; -.
DR   PaxDb; 10090-ENSMUSP00000132945; -.
DR   PeptideAtlas; P62823; -.
DR   ProteomicsDB; 253147; -.
DR   Pumba; P62823; -.
DR   Antibodypedia; 23602; 131 antibodies from 26 providers.
DR   DNASU; 67295; -.
DR   Ensembl; ENSMUST00000167824.3; ENSMUSP00000132945.2; ENSMUSG00000021700.11.
DR   GeneID; 67295; -.
DR   KEGG; mmu:67295; -.
DR   UCSC; uc007rvo.3; mouse.
DR   AGR; MGI:1914545; -.
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; FDMEDER; -.
DR   OrthoDB; 9989112at2759; -.
DR   PhylomeDB; P62823; -.
DR   Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR   BioGRID-ORCS; 67295; 1 hit in 78 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:P62823; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; P62823; protein.
DR   Bgee; ENSMUSG00000021700; Expressed in medial dorsal nucleus of thalamus and 124 other cell types or tissues.
DR   ExpressionAtlas; P62823; baseline and differential.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; ISO:GO_Central.
DR   GO; GO:0031982; C:vesicle; ISO:GO_Central.
DR   GO; GO:0003925; F:G protein activity; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0030742; F:GTP-dependent protein binding; IPI:MGI.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0031489; F:myosin V binding; ISO:GO_Central.
DR   GO; GO:0019882; P:antigen processing and presentation; ISO:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR   CDD; cd01865; Rab3; 1.
DR   FunFam; 3.40.50.300:FF:000206; Ras-related protein Rab-3C; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR037872; Rab3.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR050305; Small_GTPase_Rab.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47980; LD44762P; 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.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; GTP-binding; Hydrolase;
KW   Lipoprotein; Magnesium; Membrane; Metal-binding; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW   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           53..66
FT                   /note="Switch 1"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   MOTIF           86..104
FT                   /note="Switch 2"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   COMPBIAS        217..227
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         42
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         43
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         44
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         56
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         57
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         62
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         144
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         174
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
FT   BINDING         175
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10949"
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
//