SIA10_PONAB
ID SIA10_PONAB Reviewed; 331 AA.
AC Q5RE85;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-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}.
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DR EMBL; CR857649; CAH89922.1; -; mRNA.
DR RefSeq; NP_001124903.1; NM_001131431.1.
DR AlphaFoldDB; Q5RE85; -.
DR SMR; Q5RE85; -.
DR STRING; 9601.ENSPPYP00000015216; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GeneID; 100171770; -.
DR KEGG; pon:100171770; -.
DR CTD; 10402; -.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q5RE85; -.
DR OrthoDB; 891104at2759; -.
DR Proteomes; UP000001595; 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: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; IEA:InterPro.
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_0000331506"
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 282
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; 38186 MW; CC118B5D90652A79 CRC64;
MRGYLVAIFL SAVFLYYVLH CILWGTNVYW AAPVEMKRRN KIQPCLSKPA FASLLRFHQF
HPFLCAADFR KIASLYGSDK FDLPYGMRTS AEYFRLALSK LQSCDLFDEF DNIPCKKCVV
VGNGGVLKNK TLGEKIDSYD VIIRMNNGPV LGHEEEVGRR TTFRLFYPES VFSDPIHNDP
NTTVILTAFK PHDLRWLLEL LMGDKINTNG FWKKPALNLI YKPYQIRILD PFIIRTAAYE
LLHFPKVFPK NQKPKHPTTG IIAITLAFYI CHEVHLAGFK YNFSDLKSPL HYYGNATMSL
MNKNAYHNVT AEQLFLKDII EKNLVINLTQ D