RAB30_HUMAN
ID RAB30_HUMAN Reviewed; 203 AA.
AC Q15771; Q6FGK1; Q6MZH2; Q96CI8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Ras-related protein Rab-30;
DE Flags: Precursor;
GN Name=RAB30;
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] (ISOFORM 1).
RC TISSUE=Melanocyte;
RX PubMed=8863739; DOI=10.1016/0378-1119(96)00509-4;
RA Chen D., Guo J., Miki T., Tachibana M., Gahl W.A.;
RT "Molecular cloning of two novel rab genes from human melanocytes.";
RL Gene 174:129-134(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22188167; DOI=10.1111/boc.201100080;
RA Kelly E.E., Giordano F., Horgan C.P., Jollivet F., Raposo G.,
RA McCaffrey M.W.;
RT "Rab30 is required for the morphological integrity of the Golgi
RT apparatus.";
RL Biol. Cell 104:84-101(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-184 IN COMPLEX WITH GTP ANALOG.
RG Structural genomics consortium (SGC);
RT "Crystal structure of RAB30 in complex with a GTP analogue.";
RL Submitted (FEB-2009) to the PDB data bank.
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 set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion (By similarity). Required for
CC maintaining the structural integrity of the Golgi apparatus, possibly
CC by mediating interactions with cytoplasmic scaffolding proteins.
CC {ECO:0000250, ECO:0000269|PubMed:22188167}.
CC -!- INTERACTION:
CC Q15771; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-3924277, EBI-11522760;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus, trans-
CC Golgi network {ECO:0000269|PubMed:22188167}. Cytoplasm
CC {ECO:0000269|PubMed:22188167}. Golgi apparatus
CC {ECO:0000269|PubMed:22188167}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15771-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15771-2; Sequence=VSP_055833, VSP_055834;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; U57092; AAC50774.1; -; mRNA.
DR EMBL; AF498956; AAM21104.1; -; mRNA.
DR EMBL; CR542106; CAG46903.1; -; mRNA.
DR EMBL; BX641138; CAE46061.1; -; mRNA.
DR EMBL; AP000893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014213; AAH14213.1; -; mRNA.
DR CCDS; CCDS8264.1; -. [Q15771-1]
DR PIR; JC4962; JC4962.
DR RefSeq; NP_001272988.1; NM_001286059.1. [Q15771-1]
DR RefSeq; NP_001272989.1; NM_001286060.1. [Q15771-1]
DR RefSeq; NP_001272990.1; NM_001286061.1. [Q15771-1]
DR RefSeq; NP_055303.2; NM_014488.4. [Q15771-1]
DR PDB; 2EW1; X-ray; 2.00 A; A=2-184.
DR PDBsum; 2EW1; -.
DR AlphaFoldDB; Q15771; -.
DR SMR; Q15771; -.
DR BioGRID; 118132; 32.
DR DIP; DIP-60519N; -.
DR IntAct; Q15771; 27.
DR STRING; 9606.ENSP00000435189; -.
DR iPTMnet; Q15771; -.
DR PhosphoSitePlus; Q15771; -.
DR BioMuta; RAB30; -.
DR DMDM; 38258937; -.
DR EPD; Q15771; -.
DR jPOST; Q15771; -.
DR MassIVE; Q15771; -.
DR MaxQB; Q15771; -.
DR PaxDb; Q15771; -.
DR PeptideAtlas; Q15771; -.
DR PRIDE; Q15771; -.
DR ProteomicsDB; 60750; -. [Q15771-1]
DR ProteomicsDB; 66570; -.
DR Antibodypedia; 31346; 300 antibodies from 26 providers.
DR DNASU; 27314; -.
DR Ensembl; ENST00000260056.6; ENSP00000260056.2; ENSG00000137502.10. [Q15771-1]
DR Ensembl; ENST00000527633.6; ENSP00000435089.1; ENSG00000137502.10. [Q15771-1]
DR Ensembl; ENST00000533486.5; ENSP00000435189.1; ENSG00000137502.10. [Q15771-1]
DR Ensembl; ENST00000534141.5; ENSP00000434974.1; ENSG00000137502.10. [Q15771-2]
DR Ensembl; ENST00000612684.4; ENSP00000478702.1; ENSG00000137502.10. [Q15771-1]
DR GeneID; 27314; -.
DR KEGG; hsa:27314; -.
DR MANE-Select; ENST00000527633.6; ENSP00000435089.1; NM_001286060.2; NP_001272989.1.
DR UCSC; uc001ozu.5; human. [Q15771-1]
DR CTD; 27314; -.
DR DisGeNET; 27314; -.
DR GeneCards; RAB30; -.
DR HGNC; HGNC:9770; RAB30.
DR HPA; ENSG00000137502; Tissue enhanced (brain).
DR MIM; 605693; gene.
DR neXtProt; NX_Q15771; -.
DR OpenTargets; ENSG00000137502; -.
DR PharmGKB; PA34121; -.
DR VEuPathDB; HostDB:ENSG00000137502; -.
DR eggNOG; KOG0095; Eukaryota.
DR GeneTree; ENSGT00940000156875; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q15771; -.
DR OMA; VYDVSCQ; -.
DR PhylomeDB; Q15771; -.
DR TreeFam; TF300097; -.
DR PathwayCommons; Q15771; -.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q15771; -.
DR BioGRID-ORCS; 27314; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; RAB30; human.
DR EvolutionaryTrace; Q15771; -.
DR GenomeRNAi; 27314; -.
DR Pharos; Q15771; Tbio.
DR PRO; PR:Q15771; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q15771; protein.
DR Bgee; ENSG00000137502; Expressed in medial globus pallidus and 177 other tissues.
DR ExpressionAtlas; Q15771; baseline and differential.
DR Genevisible; Q15771; HS.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0031985; C:Golgi cisterna; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005795; C:Golgi stack; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04114; Rab30; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041820; Rab30.
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; Alternative splicing; Cytoplasm; Golgi apparatus;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Reference proteome.
FT CHAIN 1..200
FT /note="Ras-related protein Rab-30"
FT /id="PRO_0000121230"
FT PROPEP 201..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370826"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 200
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 199
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 120..164
FT /note="VGNKIDLAERREVSQQRAEEFSEAQDMYYLETSAKESDNVEKLFL -> ATR
FT LTWLKGERFPSSELKNSQKLRTCIIWRPQPRNLIMWRNSSLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_055833"
FT VAR_SEQ 165..203
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_055834"
FT CONFLICT 45
FT /note="D -> G (in Ref. 1; AAC50774)"
FT /evidence="ECO:0000305"
FT STRAND 7..17
FT /evidence="ECO:0007829|PDB:2EW1"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:2EW1"
FT STRAND 43..53
FT /evidence="ECO:0007829|PDB:2EW1"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:2EW1"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2EW1"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2EW1"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2EW1"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:2EW1"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:2EW1"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:2EW1"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:2EW1"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:2EW1"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:2EW1"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2EW1"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2EW1"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:2EW1"
SQ SEQUENCE 203 AA; 23058 MW; 935E56DBD48DD7C2 CRC64;
MSMEDYDFLF KIVLIGNAGV GKTCLVRRFT QGLFPPGQGA TIGVDFMIKT VEINGEKVKL
QIWDTAGQER FRSITQSYYR SANALILTYD ITCEESFRCL PEWLREIEQY ASNKVITVLV
GNKIDLAERR EVSQQRAEEF SEAQDMYYLE TSAKESDNVE KLFLDLACRL ISEARQNTLV
NNVSSPLPGE GKSISYLTCC NFN
