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B3GT8_ARATH
ID   B3GT8_ARATH             Reviewed;         395 AA.
AC   Q9C809;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Probable beta-1,3-galactosyltransferase 8;
DE            EC=2.4.1.-;
GN   Name=B3GALT8; OrderedLocusNames=At1g33430; ORFNames=F10C21.10;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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].
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
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).
CC   -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from
CC       UDP-galactose to substrates with a terminal glycosyl residue.
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
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=Q9C809-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BX813522; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AC051630; AAG51207.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31593.1; -; Genomic_DNA.
DR   EMBL; BX813522; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A86458; A86458.
DR   RefSeq; NP_174609.1; NM_103068.2. [Q9C809-1]
DR   AlphaFoldDB; Q9C809; -.
DR   SMR; Q9C809; -.
DR   BioGRID; 25470; 1.
DR   IntAct; Q9C809; 1.
DR   STRING; 3702.AT1G33430.2; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   iPTMnet; Q9C809; -.
DR   PaxDb; Q9C809; -.
DR   EnsemblPlants; AT1G33430.1; AT1G33430.1; AT1G33430. [Q9C809-1]
DR   GeneID; 840236; -.
DR   Gramene; AT1G33430.1; AT1G33430.1; AT1G33430. [Q9C809-1]
DR   KEGG; ath:AT1G33430; -.
DR   Araport; AT1G33430; -.
DR   eggNOG; KOG2288; Eukaryota.
DR   HOGENOM; CLU_040730_3_0_1; -.
DR   InParanoid; Q9C809; -.
DR   PhylomeDB; Q9C809; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q9C809; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C809; differential.
DR   Genevisible; Q9C809; AT.
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:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Manganese; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..395
FT                   /note="Probable beta-1,3-galactosyltransferase 8"
FT                   /id="PRO_0000359418"
FT   TRANSMEM        5..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   395 AA;  44732 MW;  7C289A6881DAB366 CRC64;
     MRAKAASGKA IIVLCLASFL AGSLFMSRTL SRSYIPEEED HHLTKHLSKH LEIQKDCDEH
     KRKLIESKSR DIIGEVSRTH QAVKSLERTM STLEMELAAA RTSDRSSEFW SERSAKNQSR
     LQKVFAVIGI NTAFSSKKRR DSVRQTWMPT GEKLKKIEKE KGIVVRFVIG HSATPGGVLD
     KAIDEEDSEH KDFLRLKHIE GYHQLSTKTR LYFSTATAMY DAEFYVKVDD DVHVNLGMLV
     TTLARYQSRP RIYIGCMKSG PVLSQKGVKY HEPEFWKFGE EGNKYFRHAT GQIYAISKDL
     ATYISTNQGI LHRYANEDVS LGAWMLGLEV EHVDERSMCC GTPPDCQWKA QAGNVCAASF
     DWSCSGICKS VDRMARVHRA CAEGDTPLAN FRFFV
 
 
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