ID   SIA10_RAT               Reviewed;         331 AA.
AC   P61943;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Type 2 lactosamine alpha-2,3-sialyltransferase;
DE            EC=2.4.99.-;
DE   AltName: Full=CMP-NeuAc:beta-galactoside alpha-2,3-sialyltransferase VI;
DE   AltName: Full=ST3Gal VI;
DE            Short=ST3GalVI;
DE   AltName: Full=Sialyltransferase 10;
GN   Name=St3gal6; Synonyms=Siat10;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Harduin-Lepers A., Martinez-Duncker I., Mollicone R., Delannoy P.,
RA   Oriol R.;
RT   "Phylogeny of sialyltransferases.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the synthesis of sialyl-paragloboside, a
CC       precursor of sialyl-Lewis X determinant. Has a alpha-2,3-
CC       sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on
CC       glycoproteins and glycolipids. Has a restricted substrate specificity,
CC       it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and
CC       neolactotetraosylceramide and neolactohexaosylceramide, but not
CC       lactotetraosylceramide, lactosylceramide or asialo-GM1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ626743; CAF25053.1; -; mRNA.
DR   AlphaFoldDB; P61943; -.
DR   SMR; P61943; -.
DR   STRING; 10116.ENSRNOP00000002255; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   GlyGen; P61943; 5 sites.
DR   iPTMnet; P61943; -.
DR   PhosphoSitePlus; P61943; -.
DR   PaxDb; P61943; -.
DR   UCSC; RGD:1303279; rat.
DR   RGD; 1303279; St3gal6.
DR   eggNOG; KOG2692; Eukaryota.
DR   InParanoid; P61943; -.
DR   PhylomeDB; P61943; -.
DR   Reactome; R-RNO-2022854; Keratan sulfate biosynthesis.
DR   Reactome; R-RNO-4085001; Sialic acid metabolism.
DR   Reactome; R-RNO-9037629; Lewis blood group biosynthesis.
DR   PRO; PR:P61943; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052798; F:beta-galactoside alpha-2,3-sialyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008373; F:sialyltransferase activity; IBA:GO_Central.
DR   GO; GO:0071354; P:cellular response to interleukin-6; ISS:UniProtKB.
DR   GO; GO:0006664; P:glycolipid metabolic process; ISS:UniProtKB.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; ISS:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR   GO; GO:0036211; P:protein modification process; ISS:UniProtKB.
DR   Gene3D; 3.90.1480.20; -; 1.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   InterPro; IPR012163; Sialyl_trans.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   PIRSF; PIRSF005557; Sialyl_trans; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..331
FT                   /note="Type 2 lactosamine alpha-2,3-sialyltransferase"
FT                   /id="PRO_0000149308"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..25
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..331
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
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        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   331 AA;  38145 MW;  DAFCC3BB681C1C8F CRC64;
     MKGYVVAIFL SSIFLYYVLY CILWGTNGYW FPNEEMKSKN NVKNCFKKPA FASLLRFPQF
     YPFLCKADFV KVAATYGTNN FLLPYGVKTF ESYFRSGLSK LQSCDLVGQF DTVPCKRCVV
     VGNGGVLKNK TLGAKIDSYD VIIRMNNGPV LGHEEEVGKR TTFRLFYPES VFSDPSHYDP
     NTTAVLVVFK PQDLRWLMEI LIGKKINTDG FWKKPALKLI YKQYQIRILD PYIIREAAFQ
     LLRFPRVFPK DQKPKHPTTG IIALTLAFHI CSEVHLAGFK YNFYTPDSPL HYYGNATMSL
     MKKNAYHNLT AEQLFLKNLI KKKMVINLTQ N