RAB30_MOUSE
ID RAB30_MOUSE Reviewed; 203 AA.
AC Q923S9; Q3UQR3; Q9D3Q6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ras-related protein Rab-30;
DE Flags: Precursor;
GN Name=Rab30; Synonyms=Rsb30;
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 STRAIN=C57BL/6J;
RA Hong W.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, Ovary, and Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [4]
RP IDENTIFICATION BY 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).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus, trans-
CC Golgi network {ECO:0000250}. Cytoplasm {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF399756; AAK94019.1; -; mRNA.
DR EMBL; AK017185; BAB30625.1; -; mRNA.
DR EMBL; AK142206; BAE24976.1; -; mRNA.
DR EMBL; BC017550; AAH17550.1; -; mRNA.
DR CCDS; CCDS21450.1; -.
DR RefSeq; NP_083770.2; NM_029494.2.
DR RefSeq; XP_006508356.1; XM_006508293.3.
DR RefSeq; XP_006508357.1; XM_006508294.2.
DR AlphaFoldDB; Q923S9; -.
DR SMR; Q923S9; -.
DR IntAct; Q923S9; 5.
DR MINT; Q923S9; -.
DR STRING; 10090.ENSMUSP00000032879; -.
DR iPTMnet; Q923S9; -.
DR PhosphoSitePlus; Q923S9; -.
DR jPOST; Q923S9; -.
DR MaxQB; Q923S9; -.
DR PaxDb; Q923S9; -.
DR PRIDE; Q923S9; -.
DR ProteomicsDB; 300376; -.
DR Antibodypedia; 31346; 300 antibodies from 26 providers.
DR DNASU; 75985; -.
DR Ensembl; ENSMUST00000032879; ENSMUSP00000032879; ENSMUSG00000030643.
DR Ensembl; ENSMUST00000107180; ENSMUSP00000102798; ENSMUSG00000030643.
DR GeneID; 75985; -.
DR KEGG; mmu:75985; -.
DR UCSC; uc009iif.1; mouse.
DR CTD; 27314; -.
DR MGI; MGI:1923235; Rab30.
DR VEuPathDB; HostDB:ENSMUSG00000030643; -.
DR eggNOG; KOG0095; Eukaryota.
DR GeneTree; ENSGT00940000156875; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q923S9; -.
DR OMA; VYDVSCQ; -.
DR OrthoDB; 1149105at2759; -.
DR PhylomeDB; Q923S9; -.
DR TreeFam; TF300097; -.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 75985; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Rab30; mouse.
DR PRO; PR:Q923S9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q923S9; protein.
DR Bgee; ENSMUSG00000030643; Expressed in small intestine Peyer's patch and 212 other tissues.
DR ExpressionAtlas; Q923S9; baseline and differential.
DR Genevisible; Q923S9; MM.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0031985; C:Golgi cisterna; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007030; P:Golgi organization; ISS: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 Cytoplasm; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..200
FT /note="Ras-related protein Rab-30"
FT /id="PRO_0000121231"
FT PROPEP 201..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370827"
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 /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
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 CONFLICT 67
FT /note="G -> V (in Ref. 2; BAB30625)"
FT /evidence="ECO:0000305"
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
