ID   SIAT2_ORYLA             Reviewed;         509 AA.
AC   Q5K027;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 76.
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   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090;
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; AJ871601; CAI39644.1; -; mRNA.
DR   RefSeq; NP_001098242.1; NM_001104772.1.
DR   RefSeq; XP_011487504.1; XM_011489202.1.
DR   AlphaFoldDB; Q5K027; -.
DR   SMR; Q5K027; -.
DR   STRING; 8090.ENSORLP00000015721; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   Ensembl; ENSORLT00000015722; ENSORLP00000015721; ENSORLG00000012556.
DR   GeneID; 100049381; -.
DR   KEGG; ola:100049381; -.
DR   CTD; 403116; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   GeneTree; ENSGT00940000158714; -.
DR   InParanoid; Q5K027; -.
DR   OrthoDB; 494294at2759; -.
DR   BRENDA; 2.4.99.1; 3199.
DR   Proteomes; UP000001038; Chromosome 21.
DR   Proteomes; UP000265180; Unplaced.
DR   Proteomes; UP000265200; Unplaced.
DR   Bgee; ENSORLG00000012556; Expressed in mesonephros and 14 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: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..509
FT                   /note="Beta-galactoside alpha-2,6-sialyltransferase 2"
FT                   /id="PRO_0000314792"
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..509
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          42..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        237..507
FT                   /evidence="ECO:0000250"
FT   DISULFID        284..436
FT                   /evidence="ECO:0000250"
FT   DISULFID        454..465
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   509 AA;  57528 MW;  1748521D1688AE1A CRC64;
     MRFSMRQWRK LVLAAILAWA LLFLGLLSYF LDNRVEEPLT PAGSLVSQHS DTRRLTSIQS
     SQQQQQPVPG LRSEQGLNSI RTSHGNQPEA GVLSSSETPG NMVNHIPSSS PYQTYGSQEA
     NHQNDLDPQS LAAWSSFGTQ NVDSNFNIAS QHRERASQSI FSNNVEDEEL PNEISPLVER
     RADADNVVQH MWRGTVSSGM LSPRLKRAMN DYINANKHHV SYQRHRKVAR SAKELLCQMK
     NQSQLRTVDG SEQPFSSLGW ADFVPLVPLQ RWNKQRGGRS FRTCAVVSSA GAILHSGLGK
     EIDSHDAVLR FNAAPTEGYE QDVGTKTTIR IINSQILANP KHEFKTSSIY KNITLVAWDP
     APYTLNLDEW FASPDYDLFG PYVEHRKNHA EQLFYILHPS YLWQLWDLIQ SNTQEKIQPN
     PPSSGFIGIL TMMALCDKLH VYEYIPSMRQ TDLCHYHENY YDAACTLGAY HPLIYEKNLI
     RRINLGSEKD LLKKGRVTLP GFSTLTCGA