ID   SIAT6_PANTR             Reviewed;         375 AA.
AC   P61132;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase;
DE            EC=2.4.99.6 {ECO:0000250|UniProtKB:P97325};
DE   AltName: Full=Beta-galactoside alpha-2,3-sialyltransferase 3;
DE            Short=Alpha 2,3-ST 3;
DE   AltName: Full=Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase;
DE   AltName: Full=N-acetyllactosaminide alpha-2,3-sialyltransferase;
DE   AltName: Full=ST3Gal III;
DE            Short=ST3GalIII;
DE   AltName: Full=ST3N;
DE   AltName: Full=Sialyltransferase 6;
GN   Name=ST3GAL3; Synonyms=SIAT6;
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].
RA   Harduin-Lepers A., Martinez-Duncker I., Mollicone R., Delannoy P.,
RA   Oriol R.;
RT   "Phylogeny of sialyltransferases.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-
CC       GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- and NeuAc-alpha-2,3-Gal-
CC       beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of
CC       glycoproteins and glycolipids. The highest activity is toward Gal-beta-
CC       1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc.
CC       {ECO:0000250|UniProtKB:P97325}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC         derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC         neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
CC         glucosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:52316,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:133507, ChEBI:CHEBI:136545; EC=2.4.99.6;
CC         Evidence={ECO:0000250|UniProtKB:P97325};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC       Secreted {ECO:0000250}. Note=Membrane-bound form in trans cisternae of
CC       Golgi. Secreted into the body fluid. {ECO:0000250}.
CC   -!- PTM: The soluble form derives from the membrane form by proteolytic
CC       processing. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ626819; CAF25177.1; -; mRNA.
DR   RefSeq; NP_001032376.1; NM_001037299.1.
DR   RefSeq; XP_016807822.1; XM_016952333.1.
DR   AlphaFoldDB; P61132; -.
DR   SMR; P61132; -.
DR   STRING; 9598.ENSPTRP00000054125; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   GeneID; 456832; -.
DR   KEGG; ptr:456832; -.
DR   CTD; 6487; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   InParanoid; P61132; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0008118; F:N-acetyllactosaminide alpha-2,3-sialyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008373; F:sialyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
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   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Secreted; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..375
FT                   /note="CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-
FT                   2,3-sialyltransferase"
FT                   /id="PRO_0000149268"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..375
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        160..314
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  42171 MW;  C9B7B61AD580EC2E CRC64;
     MGLLVFVRNL LLALCLFLVL GFLYYSAWKL HLLQWEEDSN SVVLSFDSAG QTLGSEYDRL
     GFLLNLDSKL PAELATKYAN FSEGACKPGY ASALMTAIFP RFSKPAPMFL DDSFRKWARI
     REFVPPFGIK GQDNLIKAIL SVTKEYRLTP ALDSLRCRRC IIVGNGGVLA NKSLGSRIDD
     YDIVVRLNSA PVKGFEKDVG SKTTLRITYP EGAMQRPEQY ERDSLFVLAG FKWQDFKWLK
     YIVYKERVSA SDGFWKSVAT RVPKEPPEIR ILNPYFIQEA AFTLIGLPFN NGLMGRGNIP
     TLGSVAVTMA LHGCDEVAVA GFGYDMSTPN APLHYYETVR MAAIKESWTH NIQREKEFLR
     KLVKARVITD LSSGI