RAB3C_HUMAN
ID RAB3C_HUMAN Reviewed; 227 AA.
AC Q96E17;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ras-related protein Rab-3C;
GN Name=RAB3C;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=12296628; DOI=10.1023/a:1019834901190;
RA Cheng H., Ma Y., Ni X., Jiang M., Luo Y., Ying K., Xie Y., Ma Y.;
RT "Cloning, mapping, and characterization of the human Rab3C gene.";
RL Biochem. Genet. 40:263-272(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP INTERACTION WITH GDI2; CHM AND CHML, PHOSPHORYLATION AT THR-94, AND
RP MUTAGENESIS OF THR-94.
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 (By similarity).
CC Interacts with GDI2, CHM and CHML; phosphorylation at Thr-94 disrupts
CC these interactions (PubMed:29125462). Interacts with MADD (via uDENN
CC domain); the GTP-bound form is preferred for interaction (By
CC similarity). {ECO:0000250|UniProtKB:P62823,
CC ECO:0000269|PubMed:29125462}.
CC -!- INTERACTION:
CC Q96E17; P27797: CALR; NbExp=3; IntAct=EBI-4287022, EBI-1049597;
CC Q96E17; Q15078: CDK5R1; NbExp=3; IntAct=EBI-4287022, EBI-746189;
CC Q96E17; P36957: DLST; NbExp=3; IntAct=EBI-4287022, EBI-351007;
CC Q96E17; Q9Y287: ITM2B; NbExp=3; IntAct=EBI-4287022, EBI-2866431;
CC Q96E17; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-4287022, EBI-1055945;
CC Q96E17; P47224: RABIF; NbExp=5; IntAct=EBI-4287022, EBI-713992;
CC Q96E17; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-4287022, EBI-11952721;
CC Q96E17; Q9H8Y1: VRTN; NbExp=3; IntAct=EBI-4287022, EBI-12894399;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, placenta and lung.
CC {ECO:0000269|PubMed:12296628}.
CC -!- PTM: Phosphorylation of Thr-94 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:0000269|PubMed:29125462}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AY026936; AAK08968.1; -; mRNA.
DR EMBL; BC013033; AAH13033.1; -; mRNA.
DR CCDS; CCDS3976.1; -.
DR RefSeq; NP_001304844.1; NM_001317915.1.
DR RefSeq; NP_612462.1; NM_138453.3.
DR PDB; 6Y7G; X-ray; 2.30 A; A/B=1-227.
DR PDBsum; 6Y7G; -.
DR AlphaFoldDB; Q96E17; -.
DR SMR; Q96E17; -.
DR BioGRID; 125459; 8.
DR IntAct; Q96E17; 13.
DR STRING; 9606.ENSP00000282878; -.
DR iPTMnet; Q96E17; -.
DR PhosphoSitePlus; Q96E17; -.
DR SwissPalm; Q96E17; -.
DR BioMuta; RAB3C; -.
DR DMDM; 23396832; -.
DR EPD; Q96E17; -.
DR jPOST; Q96E17; -.
DR MassIVE; Q96E17; -.
DR MaxQB; Q96E17; -.
DR PaxDb; Q96E17; -.
DR PeptideAtlas; Q96E17; -.
DR PRIDE; Q96E17; -.
DR ProteomicsDB; 76365; -.
DR Antibodypedia; 23602; 136 antibodies from 27 providers.
DR DNASU; 115827; -.
DR Ensembl; ENST00000282878.6; ENSP00000282878.4; ENSG00000152932.8.
DR GeneID; 115827; -.
DR KEGG; hsa:115827; -.
DR MANE-Select; ENST00000282878.6; ENSP00000282878.4; NM_138453.4; NP_612462.1.
DR UCSC; uc003jrp.4; human.
DR CTD; 115827; -.
DR GeneCards; RAB3C; -.
DR HGNC; HGNC:30269; RAB3C.
DR HPA; ENSG00000152932; Tissue enriched (brain).
DR MIM; 612829; gene.
DR neXtProt; NX_Q96E17; -.
DR OpenTargets; ENSG00000152932; -.
DR PharmGKB; PA134874100; -.
DR VEuPathDB; HostDB:ENSG00000152932; -.
DR eggNOG; KOG0093; Eukaryota.
DR GeneTree; ENSGT00940000157368; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q96E17; -.
DR OMA; WQKDASD; -.
DR OrthoDB; 1218073at2759; -.
DR PhylomeDB; Q96E17; -.
DR TreeFam; TF313199; -.
DR PathwayCommons; Q96E17; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q96E17; -.
DR SIGNOR; Q96E17; -.
DR BioGRID-ORCS; 115827; 7 hits in 1066 CRISPR screens.
DR ChiTaRS; RAB3C; human.
DR GeneWiki; RAB3C; -.
DR GenomeRNAi; 115827; -.
DR Pharos; Q96E17; Tbio.
DR PRO; PR:Q96E17; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96E17; protein.
DR Bgee; ENSG00000152932; Expressed in lateral nuclear group of thalamus and 118 other tissues.
DR Genevisible; Q96E17; HS.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
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; IBA:GO_Central.
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 3D-structure; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW 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_0000121085"
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 94
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:0000250|UniProtKB:P62823"
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"
FT MUTAGEN 94
FT /note="T->A: Loss of phosphorylation. No effect on GDI2,
FT CHM and CHML binding."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 94
FT /note="T->E: Phosphomimetic mutant. Loss of GDI2, CHM and
FT CHML binding."
FT /evidence="ECO:0000269|PubMed:29125462"
FT STRAND 28..38
FT /evidence="ECO:0007829|PDB:6Y7G"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:6Y7G"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:6Y7G"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:6Y7G"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:6Y7G"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:6Y7G"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:6Y7G"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:6Y7G"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:6Y7G"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:6Y7G"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:6Y7G"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:6Y7G"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:6Y7G"
FT HELIX 180..196
FT /evidence="ECO:0007829|PDB:6Y7G"
SQ SEQUENCE 227 AA; 25952 MW; 7352E205DEFAC72D CRC64;
MRHEAPMQMA SAQDARYGQK DSSDQNFDYM FKLLIIGNSS VGKTSFLFRY ADDSFTSAFV
STVGIDFKVK TVFKNEKRIK LQIWDTAGQE RYRTITTAYY RGAMGFILMY DITNEESFNA
VQDWSTQIKT YSWDNAQVIL VGNKCDMEDE RVISTERGQH LGEQLGFEFF ETSAKDNINV
KQTFERLVDI ICDKMSESLE TDPAITAAKQ NTRLKETPPP PQPNCAC
