ID   SIAT2_TAKRU             Reviewed;         537 AA.
AC   Q5QQ37;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
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   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
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}.
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DR   EMBL; AJ866779; CAI29184.1; -; mRNA.
DR   RefSeq; XP_011606552.1; XM_011608250.1.
DR   RefSeq; XP_011606557.1; XM_011608255.1.
DR   AlphaFoldDB; Q5QQ37; -.
DR   SMR; Q5QQ37; -.
DR   STRING; 31033.ENSTRUP00000034080; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   GeneID; 777969; -.
DR   KEGG; tru:777969; -.
DR   CTD; 403116; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   InParanoid; Q5QQ37; -.
DR   OrthoDB; 494294at2759; -.
DR   BRENDA; 2.4.99.1; 6209.
DR   Proteomes; UP000005226; Unplaced.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
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..537
FT                   /note="Beta-galactoside alpha-2,6-sialyltransferase 2"
FT                   /id="PRO_0000314791"
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..537
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          83..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..182
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        265..535
FT                   /evidence="ECO:0000250"
FT   DISULFID        312..464
FT                   /evidence="ECO:0000250"
FT   DISULFID        482..493
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   537 AA;  60688 MW;  7A4FCBD7FF7B0629 CRC64;
     MKSWVRQGRR LVLVGMLAWV LLFLALLSYF LDARVNEPLT STGSVLYQHP DTRRLASIQA
     SQLHNTNLGS RPELASTLTA TYTRDEPRPS ATPEFSLEAS QSPDSAPLAI YGGPEGIHQD
     YLDPQSLAAW SSFGTENIGS QSDPVIQSRE RTSQNHGSIT RYRGGEEEEE EEEEEERQEN
     EDEDVANGLR NTAARKPGGD SSELEKYYFS KSISVVQRLW RGHVSADMLS PRLQRAMKDY
     VSANKHQVSY RGRRRPSQSA KELLCEMKAQ ARLQMVDGTQ QPFSSLGWAS LVPSLPLEQL
     HKRPDQGSFK SCAVVTSAGA ILRSGLGREI DAHDAVLRFN AAPTEGYERD VGNKTTIRII
     NSQILANPNH RFNTSSLYKD VVLVAWDPAP YTLDLHKWYA SPDYNLFGPY MEHRRAHPDQ
     PFYILHPRYV WRLWDVIQGN TQENIQPNPP SSGFIGILLM MTLCEQVHVY EYIPSMRQSD
     LCHYHERYYD AACTLGAYHP LLYEKSLIQR INTGPGSDLR RKGRVTLPGF STVDCDI