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B3GTB_ARATH
ID   B3GTB_ARATH             Reviewed;         338 AA.
AC   Q94F27; Q2V2Z0; Q9FK08;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Hydroxyproline O-galactosyltransferase HPGT1 {ECO:0000303|PubMed:25600942};
DE            EC=2.4.1.- {ECO:0000269|PubMed:25600942};
DE   AltName: Full=Beta-1,3-galactosyltransferase 11 {ECO:0000305};
GN   Name=HPTG1 {ECO:0000303|PubMed:25600942};
GN   Synonyms=B3GALT11 {ECO:0000305|PubMed:18548197};
GN   OrderedLocusNames=At5g53340; ORFNames=K19E1.14;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18548197; DOI=10.1007/s11103-008-9351-3;
RA   Qu Y., Egelund J., Gilson P.R., Houghton F., Gleeson P.A., Schultz C.J.,
RA   Bacic A.;
RT   "Identification of a novel group of putative Arabidopsis thaliana beta-
RT   (1,3)-galactosyltransferases.";
RL   Plant Mol. Biol. 68:43-59(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=25600942; DOI=10.1111/tpj.12764;
RA   Ogawa-Ohnishi M., Matsubayashi Y.;
RT   "Identification of three potent hydroxyproline O-galactosyltransferases in
RT   Arabidopsis.";
RL   Plant J. 81:736-746(2015).
CC   -!- FUNCTION: Possesses hydroxyproline O-galactosyltransferase activity.
CC       Transfers galactose from UDP-galactose to hydroxyproline residues in
CC       the arabinogalactan proteins (AGPs). Is specific for AGPs containing
CC       non-contiguous peptidyl hydroxyproline residues. The addition of
CC       galactose onto the peptidyl hydroxyproline residues in AGP core
CC       proteins represents the first committed step in arabinogalactan
CC       polysaccharide addition. AGP glycans play essential roles in both
CC       vegetative and reproductive plant growth.
CC       {ECO:0000269|PubMed:25600942}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:A7XDQ9};
CC   -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:25600942}; Single-pass type II membrane protein
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q94F27-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q94F27-2; Sequence=VSP_036148;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, cauline leaves,
CC       stems, flowers and siliques. {ECO:0000269|PubMed:25600942}.
CC   -!- DISRUPTION PHENOTYPE: Reduced levels of arabinogalactan proteins.
CC       {ECO:0000269|PubMed:25600942}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC       site. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09796.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB013388; BAB09796.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED96341.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96342.1; -; Genomic_DNA.
DR   EMBL; AF386942; AAK62387.1; -; mRNA.
DR   EMBL; AY081533; AAM10095.1; -; mRNA.
DR   RefSeq; NP_001032067.1; NM_001036990.2. [Q94F27-2]
DR   RefSeq; NP_568791.1; NM_124713.4. [Q94F27-1]
DR   AlphaFoldDB; Q94F27; -.
DR   SMR; Q94F27; -.
DR   STRING; 3702.AT5G53340.1; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   PaxDb; Q94F27; -.
DR   PRIDE; Q94F27; -.
DR   ProteomicsDB; 241182; -. [Q94F27-1]
DR   EnsemblPlants; AT5G53340.1; AT5G53340.1; AT5G53340. [Q94F27-1]
DR   EnsemblPlants; AT5G53340.2; AT5G53340.2; AT5G53340. [Q94F27-2]
DR   GeneID; 835415; -.
DR   Gramene; AT5G53340.1; AT5G53340.1; AT5G53340. [Q94F27-1]
DR   Gramene; AT5G53340.2; AT5G53340.2; AT5G53340. [Q94F27-2]
DR   KEGG; ath:AT5G53340; -.
DR   Araport; AT5G53340; -.
DR   TAIR; locus:2154247; AT5G53340.
DR   eggNOG; KOG2288; Eukaryota.
DR   InParanoid; Q94F27; -.
DR   OMA; TYETNGT; -.
DR   PhylomeDB; Q94F27; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q94F27; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q94F27; baseline and differential.
DR   Genevisible; Q94F27; 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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:1990714; F:hydroxyproline O-galactosyltransferase activity; IDA:TAIR.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0010405; P:arabinogalactan protein metabolic process; IMP:UniProtKB.
DR   GO; GO:0018258; P:protein O-linked glycosylation via hydroxyproline; IDA:UniProtKB.
DR   InterPro; IPR025298; DUF4094.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF13334; DUF4094; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycosyltransferase; Golgi apparatus; Manganese;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..338
FT                   /note="Hydroxyproline O-galactosyltransferase HPGT1"
FT                   /id="PRO_0000359421"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        13..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..338
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   VAR_SEQ         332
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036148"
SQ   SEQUENCE   338 AA;  37768 MW;  613C2D79C82A2E39 CRC64;
     MARKGSSIRL SSSRISTLLL FMFATFASFY VAGRLWQESQ TRVHLINELD RVTGQGKSAI
     SVDDTLKIIA CREQKKTLAA LEMELSSARQ EGFVSKSPKL ADGTETKKRP LVVIGIMTSL
     GNKKKRDAVR QAWMGTGASL KKLESEKGVI ARFVIGRSAN KGDSMDKSID TENSQTDDFI
     ILDDVVEAPE EASKKVKLFF AYAADRWDAQ FYAKAIDNIY VNIDALGTTL AAHLENPRAY
     IGCMKSGEVF SEPNHKWYEP EWWKFGDKKA YFRHAYGEMY VITHALARFV SINRDILHSY
     AHDDVSTGSW FVGLDVKHVD EGKFCCSAWS SEAICAGV
 
 
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