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GT6_ARATH
ID   GT6_ARATH               Reviewed;         432 AA.
AC   Q9SZG1; Q0V7Q4;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Glycosyltransferase 6;
DE            Short=AtGT6;
DE            EC=2.4.-.-;
GN   Name=GT6; OrderedLocusNames=At4g37690; ORFNames=F19F18.180;
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].
RC   STRAIN=cv. Columbia;
RX   PubMed=24905498; DOI=10.1111/tpj.12577;
RA   Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA   Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA   Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA   Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA   Loque D., Scheller H.V., Heazlewood J.L.;
RT   "The plant glycosyltransferase clone collection for functional genomics.";
RL   Plant J. 79:517-529(2014).
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].
RC   STRAIN=cv. Columbia;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-432.
RG   Center for eukaryotic structural genomics (CESG);
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12032363; DOI=10.1073/pnas.102644799;
RA   Faik A., Price N.J., Raikhel N.V., Keegstra K.;
RT   "An Arabidopsis gene encoding an alpha-xylosyltransferase involved in
RT   xyloglucan biosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:7797-7802(2002).
CC   -!- FUNCTION: Probable glycosyltransferase that may be involved in the
CC       biosynthesis of xyloglucan. {ECO:0000250|UniProtKB:Q9CA75}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 34 family.
CC       {ECO:0000305}.
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DR   EMBL; KJ138718; AHL38658.1; -; mRNA.
DR   EMBL; AL035605; CAB38308.1; -; Genomic_DNA.
DR   EMBL; AL161592; CAB80434.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86828.1; -; Genomic_DNA.
DR   EMBL; BT026516; ABH04623.1; -; mRNA.
DR   EMBL; BT015600; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T04726; T04726.
DR   RefSeq; NP_680773.1; NM_148407.3.
DR   AlphaFoldDB; Q9SZG1; -.
DR   SMR; Q9SZG1; -.
DR   BioGRID; 15205; 1.
DR   STRING; 3702.AT4G37690.1; -.
DR   CAZy; GT34; Glycosyltransferase Family 34.
DR   PaxDb; Q9SZG1; -.
DR   PRIDE; Q9SZG1; -.
DR   ProteomicsDB; 247310; -.
DR   DNASU; 829924; -.
DR   EnsemblPlants; AT4G37690.1; AT4G37690.1; AT4G37690.
DR   GeneID; 829924; -.
DR   Gramene; AT4G37690.1; AT4G37690.1; AT4G37690.
DR   KEGG; ath:AT4G37690; -.
DR   Araport; AT4G37690; -.
DR   TAIR; locus:2120145; AT4G37690.
DR   eggNOG; KOG4748; Eukaryota.
DR   HOGENOM; CLU_034328_0_0_1; -.
DR   InParanoid; Q9SZG1; -.
DR   OMA; MDLIDTW; -.
DR   OrthoDB; 1223199at2759; -.
DR   PhylomeDB; Q9SZG1; -.
DR   BioCyc; ARA:AT4G37690-MON; -.
DR   PRO; PR:Q9SZG1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SZG1; baseline and differential.
DR   GO; GO:0005768; C:endosome; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR   GO; GO:0008378; F:galactosyltransferase activity; IMP:TAIR.
DR   GO; GO:0016758; F:hexosyltransferase activity; IBA:GO_Central.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR008630; Glyco_trans_34.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR31311; PTHR31311; 1.
DR   Pfam; PF05637; Glyco_transf_34; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..432
FT                   /note="Glycosyltransferase 6"
FT                   /id="PRO_0000215174"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..432
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        393
FT                   /note="I -> T (in Ref. 5; BT015600)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   432 AA;  50295 MW;  3BBA5F10B196BB7C CRC64;
     MGKPGGAKTR TAVCLSDGVF FLAGAFMSLT LVWSYFSIFS PSFTSLRHDG KPVQCSGLDM
     QFDPSEPGFY DDPDLSYSIE KPITKWDEKR NQWFESHPSF KPGSENRIVM VTGSQSSPCK
     NPIGDHLLLR CFKNKVDYAR IHGHDIFYSN SLLHPKMNSY WAKLPVVKAA MLAHPEAEWI
     WWVDSDAIFT DMEFKPPLHR YRQHNLVVHG WPNIIYEKQS WTALNAGVFL IRNCQWSMDL
     IDTWKSMGPV SPDYKKWGPI QRSIFKDKLF PESDDQTALI YLLYKHKELY YPKIYLEAEY
     YLQGYWIGVF GDFANVTERY LEMEREDDTL RRRHAEKVSE RYGAFREERF LKGEFGGRGS
     RRRAFITHFT GCQPCSGDHN PSYDGDTCWN EMIRALNFAD NQVMRVYGYV HSDLSKTSPL
     QPLPFDYPNE AW
 
 
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