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RAG3A_ARATH
ID   RAG3A_ARATH             Reviewed;         206 AA.
AC   Q948K8; A2RVP8; Q3EA61; Q9SZ88;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Ras-related protein RABG3a;
DE            Short=AtRABG3a;
DE   AltName: Full=Ras-related protein Rab76;
DE            Short=AtRab76;
GN   Name=RABG3A; Synonyms=RAB76; OrderedLocusNames=At4g09720;
GN   ORFNames=F17A8.70;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Ueda T., Wada Y., Nakano A.;
RT   "Rab7 homologs in Arabidopsis thaliana.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-206.
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12644670; DOI=10.1104/pp.013052;
RA   Vernoud V., Horton A.C., Yang Z., Nielsen E.;
RT   "Analysis of the small GTPase gene superfamily of Arabidopsis.";
RL   Plant Physiol. 131:1191-1208(2003).
CC   -!- FUNCTION: Intracellular vesicle trafficking and protein transport.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q948K8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q948K8-2; Sequence=VSP_040948;
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB39639.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78095.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB071851; BAB68376.1; -; mRNA.
DR   EMBL; AL049482; CAB39639.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161515; CAB78095.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82783.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82784.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66968.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66969.1; -; Genomic_DNA.
DR   EMBL; AK229171; BAF01041.1; -; mRNA.
DR   EMBL; BT029504; ABL66760.1; -; mRNA.
DR   EMBL; BT030039; ABN04777.1; -; mRNA.
DR   PIR; T04019; T04019.
DR   RefSeq; NP_001319888.1; NM_001340630.1. [Q948K8-2]
DR   RefSeq; NP_001328831.1; NM_001340631.1. [Q948K8-2]
DR   RefSeq; NP_192710.1; NM_117040.4. [Q948K8-1]
DR   RefSeq; NP_849347.1; NM_179016.1. [Q948K8-2]
DR   AlphaFoldDB; Q948K8; -.
DR   SMR; Q948K8; -.
DR   STRING; 3702.AT4G09720.3; -.
DR   iPTMnet; Q948K8; -.
DR   PRIDE; Q948K8; -.
DR   ProteomicsDB; 235092; -. [Q948K8-1]
DR   EnsemblPlants; AT4G09720.1; AT4G09720.1; AT4G09720. [Q948K8-1]
DR   EnsemblPlants; AT4G09720.2; AT4G09720.2; AT4G09720. [Q948K8-2]
DR   EnsemblPlants; AT4G09720.5; AT4G09720.5; AT4G09720. [Q948K8-2]
DR   EnsemblPlants; AT4G09720.6; AT4G09720.6; AT4G09720. [Q948K8-2]
DR   GeneID; 826558; -.
DR   Gramene; AT4G09720.1; AT4G09720.1; AT4G09720. [Q948K8-1]
DR   Gramene; AT4G09720.2; AT4G09720.2; AT4G09720. [Q948K8-2]
DR   Gramene; AT4G09720.5; AT4G09720.5; AT4G09720. [Q948K8-2]
DR   Gramene; AT4G09720.6; AT4G09720.6; AT4G09720. [Q948K8-2]
DR   KEGG; ath:AT4G09720; -.
DR   Araport; AT4G09720; -.
DR   eggNOG; KOG0394; Eukaryota.
DR   HOGENOM; CLU_041217_10_6_1; -.
DR   InParanoid; Q948K8; -.
DR   OMA; DSLENWH; -.
DR   PhylomeDB; Q948K8; -.
DR   PRO; PR:Q948K8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q948K8; baseline and differential.
DR   Genevisible; Q948K8; AT.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
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   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Prenylation; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..206
FT                   /note="Ras-related protein RABG3a"
FT                   /id="PRO_0000407362"
FT   MOTIF           37..45
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..128
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..159
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         206
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           204
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           206
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..34
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_040948"
SQ   SEQUENCE   206 AA;  22751 MW;  922AF5A59C4A77BA CRC64;
     MATRRRTLLK VIVLGDSGVG KTSLMNQYVH KKFSMQYKAT IGADFVTKEL QIGEKLVTLQ
     IWDTAGQERF QSLGAAFYRG ADCCALVYDV NVLRSFDNLE TWHEEFLKQA SPSDPKTFPF
     IVLGNKIDVD GGSSRVVSDK KAADWCASNG NIPYFETSAK DDFNVDEAFL TIAKTALANE
     HEQDIYFQGI PDAVTENEPK GGGCAC
 
 
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