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GAUT3_ARATH
ID   GAUT3_ARATH             Reviewed;         680 AA.
AC   Q0WQD2; F4JTM1; Q9SVF8;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Probable galacturonosyltransferase 3;
DE            EC=2.4.1.-;
GN   Name=GAUT3; OrderedLocusNames=At4g38270; ORFNames=F22I13.40;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16540543; DOI=10.1073/pnas.0600120103;
RA   Sterling J.D., Atmodjo M.A., Inwood S.E., Kumar Kolli V.S., Quigley H.F.,
RA   Hahn M.G., Mohnen D.;
RT   "Functional identification of an Arabidopsis pectin biosynthetic
RT   homogalacturonan galacturonosyltransferase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5236-5241(2006).
RN   [5]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=19825675; DOI=10.1093/mp/ssp062;
RA   Caffall K.H., Pattathil S., Phillips S.E., Hahn M.G., Mohnen D.;
RT   "Arabidopsis thaliana T-DNA mutants implicate GAUT genes in the
RT   biosynthesis of pectin and xylan in cell walls and seed testa.";
RL   Mol. Plant 2:1000-1014(2009).
CC   -!- FUNCTION: May be involved in pectin and/or xylans biosynthesis in cell
CC       walls. {ECO:0000250}.
CC   -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q0WQD2-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, inflorescences, siliques,
CC       leaves and stems. {ECO:0000269|PubMed:19825675}.
CC   -!- DISRUPTION PHENOTYPE: No changes in the cell wall content.
CC       {ECO:0000269|PubMed:19825675}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB37483.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80492.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL035539; CAB37483.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161593; CAB80492.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86907.1; -; Genomic_DNA.
DR   EMBL; AK228767; BAF00667.1; -; mRNA.
DR   PIR; T05655; T05655.
DR   RefSeq; NP_195540.2; NM_119989.5. [Q0WQD2-1]
DR   AlphaFoldDB; Q0WQD2; -.
DR   SMR; Q0WQD2; -.
DR   BioGRID; 15264; 2.
DR   STRING; 3702.AT4G38270.1; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   PaxDb; Q0WQD2; -.
DR   PRIDE; Q0WQD2; -.
DR   ProteomicsDB; 222161; -. [Q0WQD2-1]
DR   EnsemblPlants; AT4G38270.1; AT4G38270.1; AT4G38270. [Q0WQD2-1]
DR   GeneID; 829984; -.
DR   Gramene; AT4G38270.1; AT4G38270.1; AT4G38270. [Q0WQD2-1]
DR   KEGG; ath:AT4G38270; -.
DR   Araport; AT4G38270; -.
DR   TAIR; locus:2121753; AT4G38270.
DR   eggNOG; ENOG502QREV; Eukaryota.
DR   InParanoid; Q0WQD2; -.
DR   OMA; NIWRLQF; -.
DR   UniPathway; UPA00845; -.
DR   PRO; PR:Q0WQD2; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q0WQD2; baseline and differential.
DR   Genevisible; Q0WQD2; AT.
DR   GO; GO:0005768; C:endosome; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005797; C:Golgi medial cisterna; 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:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR   GO; GO:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; ISS:TAIR.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045489; P:pectin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR029993; GAUT.
DR   InterPro; IPR002495; Glyco_trans_8.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR32116; PTHR32116; 1.
DR   Pfam; PF01501; Glyco_transf_8; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell wall biogenesis/degradation; Glycoprotein;
KW   Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..680
FT                   /note="Probable galacturonosyltransferase 3"
FT                   /id="PRO_0000392556"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..680
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          118..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        578
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        610
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        631
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        515
FT                   /note="A -> V (in Ref. 3; BAF00667)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   680 AA;  77771 MW;  92C4C9C4DDCACCD5 CRC64;
     MTTFSTCAAF LSLVVVLHAV HVGGAILESQ APHRELKAYR PLQDNNLQEV YASSAAAVHY
     DPDLKDVNIV ATYSDHYGNI RLGRVKMGDL SPSWVLENPA YQVSRKTKGS QLVIPRDSFQ
     NDTGMEDNAS HSTTNQTDES ENQFPNVDFA SPAKLKRQIL RQERRGQRTL ELIRQEKETD
     EQMQEAAIQK SMSFENSVIG KYSIWRRDYE SPNADAILKL MRDQIIMAKA YANIAKSKNV
     TNLYVFLMQQ CGENKRVIGK ATSDADLPSS ALDQAKAMGH ALSLAKDELY DCHELAKKFR
     AILQSTERKV DGLKKKGTFL IQLAAKTFPK PLHCLSLQLA ADYFILGFNE EDAVKEDVSQ
     KKLEDPSLYH YAIFSDNVLA TSVVVNSTVL NAKEPQRHVF HIVTDKLNFG AMKMWFRINA
     PADATIQVEN INDFKWLNSS YCSVLRQLES ARLKEYYFKA NHPSSISAGA DNLKYRNPKY
     LSMLNHLRFY LPEVYPKLEK ILFLDDDIVV QKDLAPLWEI DMQGKVNGAV ETCKESFHRF
     DKYLNFSNPK ISENFDAGAC GWAFGMNMFD LKEWRKRNIT GIYHYWQDLN EDRTLWKLGS
     LPPGLITFYN LTYAMDRSWH VLGLGYDPAL NQTAIENAAV VHYNGNYKPW LGLAFAKYKP
     YWSKYVEYDN PYLRRCDINE
 
 
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