ID   SIAT2_CHICK             Reviewed;         528 AA.
AC   Q701R0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
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; AJ627629; CAF29497.1; -; mRNA.
DR   RefSeq; NP_001161219.1; NM_001167747.1.
DR   AlphaFoldDB; Q701R0; -.
DR   SMR; Q701R0; -.
DR   STRING; 9031.ENSGALP00000027075; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   PaxDb; Q701R0; -.
DR   GeneID; 403122; -.
DR   KEGG; gga:403122; -.
DR   CTD; 84620; -.
DR   VEuPathDB; HostDB:geneid_403122; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   InParanoid; Q701R0; -.
DR   OrthoDB; 494294at2759; -.
DR   PhylomeDB; Q701R0; -.
DR   BRENDA; 2.4.99.1; 1306.
DR   PRO; PR:Q701R0; -.
DR   Proteomes; UP000000539; 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..528
FT                   /note="Beta-galactoside alpha-2,6-sialyltransferase 2"
FT                   /id="PRO_0000314789"
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..528
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        254..519
FT                   /evidence="ECO:0000250"
FT   DISULFID        297..448
FT                   /evidence="ECO:0000250"
FT   DISULFID        466..477
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   528 AA;  61043 MW;  E890384CA0E4AC40 CRC64;
     MKPNLKQWKQ LMLFGIFAWG LLFLVIFIYF TDSNSAEPVP SSFSYIETKR LLPLQGKQRV
     IMGAIHDPSF SEAIDGNEVL LNEDLLDTFK SETGSIKKWT DLEDAFRSED EFFPSQIGRK
     SKSAFYQVND DYLFAAGQPM SHNSFQEIAK FISADEDNPK ESILQNNWSR QRRMRRRSTK
     HRRSQMLDES DDWDGLYSTM SKSFLYKLWK GDVSSKMLNP RLQKAMKDYL STNKHGVRFK
     GKRNSKLTGD QLFCELKERV DVKTIDGKEA PFSTLGWEKH VPQIPLGKLY THGFGSCAVV
     MSAGAILNSS LGDEIDSHDA VLRFNSAPTR GYEKDVGNKT TMRIINSQIL TNPNHHFVDS
     SLYKDVILVA WDPAPYSANL NWYKKPDYNL FTPYVQHRKK NPNQPFYILH PKFIWQLWDI
     IQENTKEKIQ PNPPSSGFIG ILIMMSMCNE VHVYEYIPSV RQTDLCHYHE LYYDAACTLG
     AYHPLLYEKL LVQRMNKGLQ DDLYRKGKVI LPGFKSVKCP ERNNFPPL