ID   SIAT2_XENTR             Reviewed;         517 AA.
AC   Q701R1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
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   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
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).
CC   -!- FUNCTION: Transfers sialic acid from the donor of substrate CMP-sialic
CC       acid to galactose containing acceptor substrates. {ECO:0000250}.
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; AJ627628; CAF29496.1; -; mRNA.
DR   AlphaFoldDB; Q701R1; -.
DR   SMR; Q701R1; -.
DR   STRING; 8364.ENSXETP00000001964; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   PaxDb; Q701R1; -.
DR   PRIDE; Q701R1; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   InParanoid; Q701R1; -.
DR   BRENDA; 2.4.99.1; 8483.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
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:0006486; P:protein glycosylation; IEA:InterPro.
DR   GO; GO:0097503; P:sialylation; IBA:GO_Central.
DR   Gene3D; 3.90.1480.20; -; 1.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   Pfam; PF00777; Glyco_transf_29; 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..517
FT                   /note="Beta-galactoside alpha-2,6-sialyltransferase 2"
FT                   /id="PRO_0000314793"
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..517
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        244..510
FT                   /evidence="ECO:0000250"
FT   DISULFID        287..439
FT                   /evidence="ECO:0000250"
FT   DISULFID        457..468
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   517 AA;  59959 MW;  1A8651A3BED6DE60 CRC64;
     MKPNLKQWKQ FMLFGICAWG LLFLVIFVYF TDSNSVEPVP SAFSYVESKK HFPLQGKQRA
     IMGAHQDQLF SYAIDDQDLL KEGILDSFIV GPGSMKKMAG ADNYFESEQE FIMSKKTQKS
     TSNNHEDDDD EIYLHKNIDS VSGKKAPAYG KRYYHDTQRQ HKKIRRNMQR KKQHMIEDSY
     DWNGFSSSMS KSFLQKLWKG NVSSKMLTPR LQKARREYLR ANKLGVNFNG KQNSRKLNPQ
     ELLCVLKDRA QVKTLDGKDA PFSSLGWEKY FPKIALNKLY PHGFSTCAVV SSAGAILNSS
     LGAEIDSHDA VLRFNSAPTR NYEKDVGNKT TLRIINSQIL TNPNHHFTDS SLYKDVTLIA
     WDPSPYYADL HMWYHKPDYN LFPPYEKHRK RNPDQPFYIL HPKFTWELWK IIQENSNEKI
     QPNPPSSGFI GILIMMSMCR TVHVYEYIPS YRQTDLCHYH EQYYDAACTL GAYHPLLYEK
     MLIQRINQGT EDNLLRKGKV ILPGFSSIHC PIKDHIT