ID   SIAT2_DANRE             Reviewed;         514 AA.
AC   Q701R2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
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   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
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   Lehmann F.;
RT   "Phylogeny of sialyltransferases.";
RL   Submitted (MAY-2004) 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. {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; AJ627627; CAF29495.1; -; mRNA.
DR   EMBL; AJ705078; CAG29200.1; -; mRNA.
DR   AlphaFoldDB; Q701R2; -.
DR   SMR; Q701R2; -.
DR   STRING; 7955.ENSDARP00000122397; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   PaxDb; Q701R2; -.
DR   ZFIN; ZDB-GENE-060322-4; st6gal2a.
DR   eggNOG; KOG2692; Eukaryota.
DR   InParanoid; Q701R2; -.
DR   PhylomeDB; Q701R2; -.
DR   BRENDA; 2.4.99.1; 928.
DR   PRO; PR:Q701R2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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; ISS:ZFIN.
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..514
FT                   /note="Beta-galactoside alpha-2,6-sialyltransferase 2"
FT                   /id="PRO_0000314790"
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..514
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          70..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..166
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        246..512
FT                   /evidence="ECO:0000250"
FT   DISULFID        289..441
FT                   /evidence="ECO:0000250"
FT   DISULFID        459..470
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   514 AA;  58533 MW;  934DDA4D1E74B0B9 CRC64;
     MKSSLKQWRR LALGLILVWA LLFLALLSYF MESRVDDPHA AAALSYTDTR RLTSLQGNPR
     TIMATHLGLA TSSAPSTSSN TQQEQSQEEN PSADPQPSPL SQEAYPYPDP QSLAAWSAFG
     TQDVGSRSTG VSRNRERQEY NQDSPQEDED EEEEVIGGEE EDEEGGDEGR GRTTKRVARH
     GSSDPHEYYV PRYKSIVHGL WKGSLSMGML SPRLQRAMKD YLNNNKHGVA YRGHRKAKQS
     RQQVLCELKK REKIRTLDGA EMPFSKLGWQ KIVPALPLSQ IHRPGLKTCA VVTSAGAMLH
     SGLGKEIDSH DAVLRFNTAP TVGYERDVGN KTTIRIINSQ ILANPMHRFN RSSLYKNVTL
     VAWDPAPYTL NLHQWYSNPD YNLFTPYMEY RMRFPSQPFY ILHPKYIWQL WDVIQANNLE
     NIQPNPPSSG FIGILLMMSL CEEVHVYEYI PSLRQTDLCH YHERYYDAAC TLGAYHPLLY
     EKMLIQRMNI GSEDELKRKG KVTLPGFNKV HCEP