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GAUTC_ARATH
ID   GAUTC_ARATH             Reviewed;         535 AA.
AC   Q9FH36;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Probable galacturonosyltransferase 12;
DE            EC=2.4.1.-;
DE   AltName: Full=Like glycosyl transferase 6;
DE   AltName: Full=Protein IRREGULAR XYLEM 8;
GN   Name=GAUT12; Synonyms=IRX8, LGT6; OrderedLocusNames=At5g54690;
GN   ORFNames=K5F14.3;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
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].
RA   Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=10809443; DOI=10.1023/a:1006368316413;
RA   Tavares R., Aubourg S., Lecharny A., Kreis M.;
RT   "Organization and structural evolution of four multigene families in
RT   Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2.";
RL   Plant Mol. Biol. 42:703-717(2000).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15980264; DOI=10.1105/tpc.105.031542;
RA   Brown D.M., Zeef L.A.H., Ellis J., Goodacre R., Turner S.R.;
RT   "Identification of novel genes in Arabidopsis involved in secondary cell
RT   wall formation using expression profiling and reverse genetics.";
RL   Plant Cell 17:2281-2295(2005).
RN   [7]
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   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=17237350; DOI=10.1105/tpc.106.047720;
RA   Persson S., Caffall K.H., Freshour G., Hilley M.T., Bauer S.,
RA   Poindexter P., Hahn M.G., Mohnen D., Somerville C.;
RT   "The Arabidopsis irregular xylem8 mutant is deficient in glucuronoxylan and
RT   homogalacturonan, which are essential for secondary cell wall integrity.";
RL   Plant Cell 19:237-255(2007).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17322407; DOI=10.1105/tpc.106.049320;
RA   Pena M.J., Zhong R., Zhou G.K., Richardson E.A., O'Neill M.A.,
RA   Darvill A.G., York W.S., Ye Z.H.;
RT   "Arabidopsis irregular xylem8 and irregular xylem9: implications for the
RT   complexity of glucuronoxylan biosynthesis.";
RL   Plant Cell 19:549-563(2007).
RN   [10]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=17944810; DOI=10.1111/j.1365-313x.2007.03307.x;
RA   Brown D.M., Goubet F., Wong V.W., Goodacre R., Stephens E., Dupree P.,
RA   Turner S.R.;
RT   "Comparison of five xylan synthesis mutants reveals new insight into the
RT   mechanisms of xylan synthesis.";
RL   Plant J. 52:1154-1168(2007).
RN   [11]
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: Involved in pectin assembly and/or distribution, and in the
CC       synthesis of secondary wall glucuronoxylan. Probably involved in the
CC       synthesis of the glycosyl sequence at the glucuronoxylan reducing end.
CC       May be involved in synthesis of a complex glycan primer for xylan
CC       synthesis. {ECO:0000269|PubMed:15980264, ECO:0000269|PubMed:17237350,
CC       ECO:0000269|PubMed:17322407, ECO:0000269|PubMed:17944810}.
CC   -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:17322407}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:17322407}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in stems. Detected in roots,
CC       inflorescences, siliques, and leaves. Expressed in cells undergoing
CC       secondary wall thickening, including interfascicular fibers and primary
CC       and secondary xylem. {ECO:0000269|PubMed:17237350,
CC       ECO:0000269|PubMed:17322407, ECO:0000269|PubMed:17944810,
CC       ECO:0000269|PubMed:19825675}.
CC   -!- DISRUPTION PHENOTYPE: Severe dwarfing and seedling lethality. Collapsed
CC       xylem vessels. Reduced glucuronoxylan and homogalacturonan content in
CC       cell wall. {ECO:0000269|PubMed:15980264, ECO:0000269|PubMed:17237350,
CC       ECO:0000269|PubMed:17322407, ECO:0000269|PubMed:17944810,
CC       ECO:0000269|PubMed:19825675}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR   EMBL; AB022214; BAB09935.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96527.1; -; Genomic_DNA.
DR   EMBL; BT023729; AAZ23921.1; -; mRNA.
DR   EMBL; AK229580; BAF01430.1; -; mRNA.
DR   RefSeq; NP_200280.1; NM_124850.4.
DR   AlphaFoldDB; Q9FH36; -.
DR   SMR; Q9FH36; -.
DR   STRING; 3702.AT5G54690.1; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   iPTMnet; Q9FH36; -.
DR   PaxDb; Q9FH36; -.
DR   PRIDE; Q9FH36; -.
DR   ProteomicsDB; 221907; -.
DR   EnsemblPlants; AT5G54690.1; AT5G54690.1; AT5G54690.
DR   GeneID; 835558; -.
DR   Gramene; AT5G54690.1; AT5G54690.1; AT5G54690.
DR   KEGG; ath:AT5G54690; -.
DR   Araport; AT5G54690; -.
DR   TAIR; locus:2157543; AT5G54690.
DR   eggNOG; ENOG502QTN8; Eukaryota.
DR   HOGENOM; CLU_010770_5_1_1; -.
DR   InParanoid; Q9FH36; -.
DR   OMA; HEHSTNS; -.
DR   OrthoDB; 404188at2759; -.
DR   PhylomeDB; Q9FH36; -.
DR   UniPathway; UPA00845; -.
DR   PRO; PR:Q9FH36; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FH36; baseline and differential.
DR   Genevisible; Q9FH36; AT.
DR   GO; GO:0005794; C:Golgi apparatus; IDA: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:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; ISS:TAIR.
DR   GO; GO:0071555; P:cell wall organization; IMP:TAIR.
DR   GO; GO:0010417; P:glucuronoxylan biosynthetic process; IMP:TAIR.
DR   GO; GO:0010413; P:glucuronoxylan metabolic process; IMP:TAIR.
DR   GO; GO:0045489; P:pectin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045492; P:xylan biosynthetic process; TAS:TAIR.
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   Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..535
FT                   /note="Probable galacturonosyltransferase 12"
FT                   /id="PRO_0000392562"
FT   TOPO_DOM        1..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..535
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        430
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   535 AA;  60880 MW;  3D55D9E9B0FBB570 CRC64;
     MQLHISPSLR HVTVVTGKGL REFIKVKVGS RRFSYQMVFY SLLFFTFLLR FVFVLSTVDT
     IDGDPSPCSS LACLGKRLKP KLLGRRVDSG NVPEAMYQVL EQPLSEQELK GRSDIPQTLQ
     DFMSEVKRSK SDAREFAQKL KEMVTLMEQR TRTAKIQEYL YRHVASSSIP KQLHCLALKL
     ANEHSINAAA RLQLPEAELV PMLVDNNYFH FVLASDNILA ASVVAKSLVQ NALRPHKIVL
     HIITDRKTYF PMQAWFSLHP LSPAIIEVKA LHHFDWLSKG KVPVLEAMEK DQRVRSQFRG
     GSSVIVANNK ENPVVVAAKL QALSPKYNSL MNHIRIHLPE LFPSLNKVVF LDDDIVIQTD
     LSPLWDIDMN GKVNGAVETC RGEDKFVMSK KFKSYLNFSN PTIAKNFNPE ECAWAYGMNV
     FDLAAWRRTN ISSTYYHWLD ENLKSDLSLW QLGTLPPGLI AFHGHVQTID PFWHMLGLGY
     QETTSYADAE SAAVVHFNGR AKPWLDIAFP HLRPLWAKYL DSSDRFIKSC HIRAS
 
 
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