ID   RAB3B_HUMAN             Reviewed;         219 AA.
AC   P20337; Q5VUL2; Q9BSI1;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2003, sequence version 2.
DT   24-JAN-2024, entry version 211.
DE   RecName: Full=Ras-related protein Rab-3B;
GN   Name=RAB3B;
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].
RX   PubMed=2501306; DOI=10.1016/s0021-9258(18)63872-4;
RA   Zahraoui A., Touchot N., Chardin P., Tavitian A.;
RT   "The human Rab genes encode a family of GTP-binding proteins related to
RT   yeast YPT1 and SEC4 products involved in secretion.";
RL   J. Biol. Chem. 264:12394-12401(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [6]
RP   INTERACTION WITH GDI2; CHM AND CHML, PHOSPHORYLATION AT THR-86, AND
RP   MUTAGENESIS OF 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).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-190 IN COMPLEX WITH GDP.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human RAB3B GTPase bound with GDP.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RIMS1, RIMS2, RPH3A and RPH3AL. The GTP-bound
CC       form interacts with GAS8/DRC4 (via coiled-coil domains) (By
CC       similarity). Interacts with GDI2, CHM and CHML; phosphorylation at Thr-
CC       86 disrupts these interactions (PubMed:29125462). Interacts with MADD
CC       (via uDENN domain); the GTP-bound form is preferred for interaction (By
CC       similarity). {ECO:0000250|UniProtKB:Q9CZT8,
CC       ECO:0000269|PubMed:29125462}.
CC   -!- INTERACTION:
CC       P20337; P47224: RABIF; NbExp=5; IntAct=EBI-12894629, EBI-713992;
CC       P20337; Q9H8Y1: VRTN; NbExp=3; IntAct=EBI-12894629, EBI-12894399;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q9CZT8}. Note=Colocalizes with GAS8/DRC4 in the
CC       Golgi apparatus. {ECO:0000250|UniProtKB:Q9CZT8}.
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:0000269|PubMed:29125462}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; M28214; AAA60243.1; -; mRNA.
DR   EMBL; AF498932; AAM21080.1; -; mRNA.
DR   EMBL; AL589663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005035; AAH05035.1; -; mRNA.
DR   CCDS; CCDS560.1; -.
DR   PIR; D34323; D34323.
DR   RefSeq; NP_002858.2; NM_002867.3.
DR   RefSeq; XP_016857447.1; XM_017001958.1.
DR   PDB; 3DZ8; X-ray; 1.90 A; A=18-190.
DR   PDB; 8A4B; X-ray; 2.80 A; B/D=17-190.
DR   PDB; 8A4C; X-ray; 2.75 A; B/D=1-219.
DR   PDBsum; 3DZ8; -.
DR   PDBsum; 8A4B; -.
DR   PDBsum; 8A4C; -.
DR   AlphaFoldDB; P20337; -.
DR   SMR; P20337; -.
DR   BioGRID; 111803; 364.
DR   IntAct; P20337; 20.
DR   MINT; P20337; -.
DR   STRING; 9606.ENSP00000360718; -.
DR   GlyGen; P20337; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P20337; -.
DR   MetOSite; P20337; -.
DR   PhosphoSitePlus; P20337; -.
DR   SwissPalm; P20337; -.
DR   BioMuta; RAB3B; -.
DR   DMDM; 38258903; -.
DR   EPD; P20337; -.
DR   jPOST; P20337; -.
DR   MassIVE; P20337; -.
DR   MaxQB; P20337; -.
DR   PaxDb; 9606-ENSP00000360718; -.
DR   PeptideAtlas; P20337; -.
DR   ProteomicsDB; 53749; -.
DR   Pumba; P20337; -.
DR   Antibodypedia; 19062; 194 antibodies from 26 providers.
DR   DNASU; 5865; -.
DR   Ensembl; ENST00000371655.4; ENSP00000360718.3; ENSG00000169213.7.
DR   GeneID; 5865; -.
DR   KEGG; hsa:5865; -.
DR   MANE-Select; ENST00000371655.4; ENSP00000360718.3; NM_002867.4; NP_002858.2.
DR   UCSC; uc001cth.3; human.
DR   AGR; HGNC:9778; -.
DR   CTD; 5865; -.
DR   DisGeNET; 5865; -.
DR   GeneCards; RAB3B; -.
DR   HGNC; HGNC:9778; RAB3B.
DR   HPA; ENSG00000169213; Tissue enhanced (brain, pituitary gland, prostate).
DR   MIM; 179510; gene.
DR   neXtProt; NX_P20337; -.
DR   OpenTargets; ENSG00000169213; -.
DR   PharmGKB; PA34133; -.
DR   VEuPathDB; HostDB:ENSG00000169213; -.
DR   eggNOG; KOG0093; Eukaryota.
DR   GeneTree; ENSGT00940000159943; -.
DR   HOGENOM; CLU_041217_10_1_1; -.
DR   InParanoid; P20337; -.
DR   OMA; AICEKMS; -.
DR   OrthoDB; 8685at2759; -.
DR   PhylomeDB; P20337; -.
DR   TreeFam; TF313199; -.
DR   PathwayCommons; P20337; -.
DR   Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR   SignaLink; P20337; -.
DR   BioGRID-ORCS; 5865; 9 hits in 1154 CRISPR screens.
DR   ChiTaRS; RAB3B; human.
DR   EvolutionaryTrace; P20337; -.
DR   GeneWiki; RAB3B; -.
DR   GenomeRNAi; 5865; -.
DR   Pharos; P20337; Tbio.
DR   PRO; PR:P20337; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P20337; Protein.
DR   Bgee; ENSG00000169213; Expressed in islet of Langerhans and 103 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0098691; C:dopaminergic synapse; IDA:SynGO.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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; IDA:SynGO.
DR   GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR   GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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:0051586; P:positive regulation of dopamine uptake involved in synaptic transmission; IDA: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:0098693; P:regulation of synaptic vesicle cycle; IDA:SynGO.
DR   GO; GO:0097494; P:regulation of vesicle size; IDA:UniProtKB.
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:SF22; RAS-RELATED PROTEIN RAB-3B; 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; P20337; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Golgi apparatus; GTP-binding;
KW   Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW   Prenylation; Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   CHAIN           2..219
FT                   /note="Ras-related protein Rab-3B"
FT                   /id="PRO_0000121081"
FT   MOTIF           51..59
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         29..37
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0007744|PDB:3DZ8"
FT   BINDING         48..54
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P63012"
FT   BINDING         77..81
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0007744|PDB:3DZ8"
FT   BINDING         165..167
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0007744|PDB:3DZ8"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   MOD_RES         86
FT                   /note="Phosphothreonine; by LRRK2"
FT                   /evidence="ECO:0000269|PubMed:29125462"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63941"
FT   MOD_RES         190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         219
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           217
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           219
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         86
FT                   /note="T->A: Loss of phosphorylation. No effect on GDI2,
FT                   CHM and CHML binding."
FT                   /evidence="ECO:0000269|PubMed:29125462"
FT   MUTAGEN         86
FT                   /note="T->E: Phosphomimetic mutant. Loss of GDI2, CHM and
FT                   CHML binding."
FT                   /evidence="ECO:0000269|PubMed:29125462"
FT   CONFLICT        9
FT                   /note="T -> H (in Ref. 1; AAA60243)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40
FT                   /note="F -> L (in Ref. 1; AAA60243)"
FT                   /evidence="ECO:0000305"
FT   STRAND          18..21
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   STRAND          23..30
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   HELIX           35..45
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   STRAND          51..55
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   STRAND          59..66
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   TURN            67..70
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   STRAND          71..76
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   HELIX           78..83
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   HELIX           85..92
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   STRAND          97..103
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   HELIX           107..111
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   HELIX           113..123
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   HELIX           140..142
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   HELIX           147..157
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   STRAND          160..163
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   TURN            166..169
FT                   /evidence="ECO:0007829|PDB:3DZ8"
FT   HELIX           172..186
FT                   /evidence="ECO:0007829|PDB:3DZ8"
SQ   SEQUENCE   219 AA;  24758 MW;  B73A014B4295A60D CRC64;
     MASVTDGKTG VKDASDQNFD YMFKLLIIGN SSVGKTSFLF RYADDTFTPA FVSTVGIDFK
     VKTVYRHEKR VKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWATQI
     KTYSWDNAQV ILVGNKCDME EERVVPTEKG QLLAEQLGFD FFEASAKENI SVRQAFERLV
     DAICDKMSDS LDTDPSMLGS SKNTRLSDTP PLLQQNCSC
//