SIAT6_RAT
ID SIAT6_RAT Reviewed; 374 AA.
AC Q02734;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 132.
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;
DE Contains:
DE RecName: Full=CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase soluble form;
GN Name=St3gal3; Synonyms=Siat6;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=1400416; DOI=10.1016/s0021-9258(19)36790-0;
RA Wen D.X., Livingston B.D., Medzihradszky K.F., Kelm S., Burlingame A.L.,
RA Paulson J.C.;
RT "Primary structure of Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase
RT determined by mass spectrometry sequence analysis and molecular cloning.
RT Evidence for a protein motif in the sialyltransferase gene family.";
RL J. Biol. Chem. 267:21011-21019(1992).
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; Single-
CC pass type II membrane protein. Secreted. Note=Membrane-bound form in
CC trans cisternae of Golgi. Secreted into the body fluid.
CC -!- TISSUE SPECIFICITY: Found in all tissues tested. High expression found
CC in brain, liver, kidney, colon, heart and lung.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
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; M97754; AAA42146.1; -; mRNA.
DR PIR; A45074; A45074.
DR RefSeq; NP_113885.1; NM_031697.1.
DR AlphaFoldDB; Q02734; -.
DR SMR; Q02734; -.
DR STRING; 10116.ENSRNOP00000053685; -.
DR BindingDB; Q02734; -.
DR ChEMBL; CHEMBL3211; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q02734; 2 sites.
DR PaxDb; Q02734; -.
DR PRIDE; Q02734; -.
DR GeneID; 64445; -.
DR KEGG; rno:64445; -.
DR UCSC; RGD:68414; rat.
DR CTD; 6487; -.
DR RGD; 68414; St3gal3.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q02734; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q02734; -.
DR BRENDA; 2.4.99.6; 5301.
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 Reactome; R-RNO-977068; Termination of O-glycan biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q02734; -.
DR Proteomes; UP000002494; 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:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; ISO:RGD.
DR GO; GO:0008118; F:N-acetyllactosaminide alpha-2,3-sialyltransferase activity; TAS:RGD.
DR GO; GO:0008373; F:sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0010706; P:ganglioside biosynthetic process via lactosylceramide; ISO:RGD.
DR GO; GO:0006486; P:protein glycosylation; ISO:RGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Secreted; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..374
FT /note="CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-
FT 2,3-sialyltransferase"
FT /id="PRO_0000012143"
FT CHAIN 48..374
FT /note="CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-
FT 2,3-sialyltransferase soluble form"
FT /id="PRO_0000012144"
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..374
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 46..47
FT /note="Cleavage; partial"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 159..313
FT /evidence="ECO:0000250"
SQ SEQUENCE 374 AA; 42082 MW; 16BAD1458963024C CRC64;
MGLLVFVRNL LLALCLFLVL GFLYYSAWKL HLLQWEDSNS LILSLDSAGQ TLGTEYDRLG
FLLKLDSKLP AELATKYANF SEGACKPGYA SAMMTAIFPR FSKPAPMFLD DSFRKWARIR
EFVPPFGIKG QDNLIKAILS VTKEYRLTPA LDSLHCRRCI IVGNGGVLAN KSLGSRIDDY
DIVIRLNSAP VKGFEKDVGS KTTLRITYPE GAMQRPEQYE RDSLFVLAGF KWQDFKWLKY
IVYKERVSAS DGFWKSVATR VPKEPPEIRI LNPYFIQEAA FTLIGLPFNN GLMGRGNIPT
LGSVAVTMAL DGCDEVAVAG FGYDMNTPNA PLHYYETVRM AAIKESWTHN IQREKEFLRK
LVKARVITDL SSGI
