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