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   24-JAN-2024, entry version 184.
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; 11.
DR   IntAct; Q96E17; 14.
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; 9606-ENSP00000282878; -.
DR   PeptideAtlas; Q96E17; -.
DR   ProteomicsDB; 76365; -.
DR   Pumba; Q96E17; -.
DR   Antibodypedia; 23602; 141 antibodies from 26 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   AGR; HGNC:30269; -.
DR   CTD; 115827; -.
DR   GeneCards; RAB3C; -.
DR   HGNC; HGNC:30269; RAB3C.
DR   HPA; ENSG00000152932; Tissue enhanced (adrenal gland, 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; PSSQCNC; -.
DR   OrthoDB; 8685at2759; -.
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 1144 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 120 other cell types or tissues.
DR   GO; GO:0005768; C:endosome; 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:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR037872; Rab3.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47980; LD44762P; 1.
DR   PANTHER; PTHR47980:SF15; RAS-RELATED PROTEIN RAB-3C; 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.
DR   Genevisible; Q96E17; HS.
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
//