位置:首页 > 蛋白库 > SIAT2_BOVIN
SIAT2_BOVIN
ID   SIAT2_BOVIN             Reviewed;         495 AA.
AC   A5D7T4; Q2I130; Q5QQ36;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Beta-galactoside alpha-2,6-sialyltransferase 2;
DE            Short=Alpha 2,6-ST 2;
DE            EC=2.4.99.1 {ECO:0000250|UniProtKB:Q96JF0};
DE   AltName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2;
DE   AltName: Full=ST6Gal II;
DE            Short=ST6GalII;
DE   AltName: Full=Sialyltransferase 2;
GN   Name=ST6GAL2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15843597; DOI=10.1093/glycob/cwi063;
RA   Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R.;
RT   "The animal sialyltransferases and sialyltransferase-related genes: a
RT   phylogenetic approach.";
RL   Glycobiology 15:805-817(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Laporte B.J., Petit J.-M.;
RT   "Characterization of the bovine ST6GalII gene product.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal brain;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers sialic acid from the donor of substrate CMP-sialic
CC       acid to galactose containing acceptor substrates. Has alpha-2,6-
CC       sialyltransferase activity toward oligosaccharides that have the Gal-
CC       beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate
CC       groups, but it has weak or no activities toward glycoproteins and
CC       glycolipids. {ECO:0000250|UniProtKB:Q96JF0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N-
CC         acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP +
CC         H(+); Xref=Rhea:RHEA:52104, ChEBI:CHEBI:15378, ChEBI:CHEBI:28034,
CC         ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:136398;
CC         EC=2.4.99.1; Evidence={ECO:0000250|UniProtKB:Q96JF0};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ866780; CAI29185.1; -; mRNA.
DR   EMBL; DQ353938; ABC97371.1; -; mRNA.
DR   EMBL; BC140674; AAI40675.1; -; mRNA.
DR   RefSeq; NP_001008668.2; NM_001008668.2.
DR   RefSeq; XP_005212804.1; XM_005212747.3.
DR   AlphaFoldDB; A5D7T4; -.
DR   SMR; A5D7T4; -.
DR   STRING; 9913.ENSBTAP00000000937; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   PaxDb; A5D7T4; -.
DR   PRIDE; A5D7T4; -.
DR   Ensembl; ENSBTAT00000000937; ENSBTAP00000000937; ENSBTAG00000000703.
DR   Ensembl; ENSBTAT00000070130; ENSBTAP00000058792; ENSBTAG00000000703.
DR   GeneID; 493992; -.
DR   KEGG; bta:493992; -.
DR   CTD; 84620; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000703; -.
DR   VGNC; VGNC:35338; ST6GAL2.
DR   eggNOG; KOG2692; Eukaryota.
DR   GeneTree; ENSGT00940000158714; -.
DR   HOGENOM; CLU_038334_1_0_1; -.
DR   InParanoid; A5D7T4; -.
DR   OMA; WRQRMLC; -.
DR   OrthoDB; 494294at2759; -.
DR   TreeFam; TF323961; -.
DR   BRENDA; 2.4.99.1; 908.
DR   Reactome; R-BTA-4085001; Sialic acid metabolism.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000000703; Expressed in occipital lobe and 32 other tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003835; F:beta-galactoside alpha-2,6-sialyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; IEA:Ensembl.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   GO; GO:0097503; P:sialylation; IBA:GO_Central.
DR   Gene3D; 3.90.1480.20; -; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..495
FT                   /note="Beta-galactoside alpha-2,6-sialyltransferase 2"
FT                   /id="PRO_0000314784"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..495
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          63..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        225..491
FT                   /evidence="ECO:0000250"
FT   DISULFID        268..420
FT                   /evidence="ECO:0000250"
FT   DISULFID        438..449
FT                   /evidence="ECO:0000250"
FT   CONFLICT        228
FT                   /note="R -> Q (in Ref. 2; ABC97371)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        288
FT                   /note="S -> P (in Ref. 2; ABC97371)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354
FT                   /note="W -> R (in Ref. 1; CAI29185)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   495 AA;  55418 MW;  37B2B435264400CB CRC64;
     MKPHLKQWRQ GMLCGVFAWG LFFVVIFLYF TDSSPAKPAP SSFSFLETRR LLPAQGRQRA
     IMGASEGLPE GADLRRGSPR GLPSGPLRTW AGDGFEREQE FLSVQTGRTS LSSFAPEDSA
     PGTSGRLFPG DPGPEGARPP RAAPGRRAKR GPRRQSLSAR GEDGERLYSS MSRALLRRLW
     KGDASARMLH PRLQKAMGAY LRANKHGVRF RGRRASGRSR TELLCALRGR VQVRTLDGTE
     PPFSALGWRA LVPPVPLSRL LPRRLRTCAV VTSAGAILNS SLGEEIDSHD AVLRFNSAPT
     RGYEKDVGNK TTVRIINSQI LTNPSYHFMD SALYKDVILV AWDPAPYSAN LNLWYKKPDY
     NLFTPYVQHR QRNPNQPFYI LHPKFIWQLW DIIQENTKEK IQPNPPSSGF IGILLMMNLC
     GEVHVYEYVP SVRQTDLCHY HEPYHDAACT LGAYHPLLYE KLLVQRLNVG THGDLHRKGK
     VVLPGLQAVR CPPGA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024