ID   SIAT2_PANTR             Reviewed;         529 AA.
AC   Q701R4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
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. Has alpha-2,6-
CC       sialyltransferase activity toward oligosaccharides that have the Gal-
CC       beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate
CC       groups, but it has weak or no activities toward glycoproteins and
CC       glycolipids. {ECO:0000250|UniProtKB:Q96JF0}.
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; AJ627625; CAF29493.1; -; mRNA.
DR   RefSeq; NP_001181861.1; NM_001194932.1.
DR   AlphaFoldDB; Q701R4; -.
DR   SMR; Q701R4; -.
DR   STRING; 9598.ENSPTRP00000040768; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   PaxDb; Q701R4; -.
DR   GeneID; 450198; -.
DR   KEGG; ptr:450198; -.
DR   CTD; 84620; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   InParanoid; Q701R4; -.
DR   BRENDA; 2.4.99.1; 4497.
DR   Proteomes; UP000002277; 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; ISS:UniProtKB.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; ISS:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   Gene3D; 3.90.1480.20; -; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   SUPFAM; SSF88713; SSF88713; 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..529
FT                   /note="Beta-galactoside alpha-2,6-sialyltransferase 2"
FT                   /id="PRO_0000314787"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..529
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          142..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        253..519
FT                   /evidence="ECO:0000250"
FT   DISULFID        296..448
FT                   /evidence="ECO:0000250"
FT   DISULFID        466..477
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   529 AA;  59957 MW;  E580804485A5F39E CRC64;
     MKPHLKQWRQ RMLFGLFAGG LLFLLIFIYF TDSNPAEPVP SSLSFLETRR LLPVQGKQRA
     IMGAAHEPSP PGGLDARQAL PRAHPAGSFH AGPGDLQKWA QSQDGFEHKE FFSSQVGRKS
     QSAFYPEDDD YFFAAGQPGW HSHSQGTLGF PSPGEPGPRE GAFPAAQVQR RRVKKRHRRQ
     RRSHVLEEGD DGDRLYSSMS RAFLYRLWKG NVSSKMLNPR LQKAMKDYLT ANKHGVRFRG
     KREAGLSRAQ LLCQLRSRAR VRTLDGTEAP FSALGWRRLV PAVPLSQLHP RGLRSCAVVM
     SAGAILNSSL GEEIDSHDAV LRFNSAPTRG YEKDVGNKTT VRIINSQILT NPSHHFVDSS
     LYKDVILVAW DPAPYSANLN LWYKKPDYNL FTPYIQHRQR NPNQPFYILH PKFIWQLWDI
     IQENTKEKIQ PNPPSSGFIG ILIMMSMCRE VHVYEYIPSV RQTELCHYHE LYYDAACTLG
     AYHPLLYEKL LVQRLNTGTQ GDLHRKGKVV LPGFQAVHCP APSPVIPHS