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CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 (Alpha 2,3-ST 1) (Beta-galactoside alpha-2,3-sialyltransferase 1) (EC 2.4.99.4) (Gal-NAc6S) (Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase) (SIATFL) (ST3Gal I) (ST3GalI) (ST3GalA.1) (ST3O) (Sialyltransferase 4A) (SIAT4-A)

 SIA4A_HUMAN             Reviewed;         340 AA.
Q11201; O60677; Q9UN51;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-APR-2018, entry version 162.
RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1;
Short=Alpha 2,3-ST 1;
Short=Beta-galactoside alpha-2,3-sialyltransferase 1;
EC=2.4.99.4 {ECO:0000250|UniProtKB:P54751};
AltName: Full=Gal-NAc6S;
AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase;
AltName: Full=SIATFL;
AltName: Full=ST3Gal I;
Short=ST3GalI;
AltName: Full=ST3GalA.1;
AltName: Full=ST3O;
AltName: Full=Sialyltransferase 4A;
Short=SIAT4-A;
Name=ST3GAL1; Synonyms=SIAT4, SIAT4A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8027041;
Kitagawa H., Paulson J.C.;
"Differential expression of five sialyltransferase genes in human
tissues.";
J. Biol. Chem. 269:17872-17878(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Submandibular gland;
PubMed=7655169; DOI=10.1093/glycob/5.3.319;
Chang M.-L., Eddy R.L., Shows T.B., Lau J.T.Y.;
"Three genes that encode human beta-galactoside alpha 2,3-
sialyltransferases. Structural analysis and chromosomal mapping
studies.";
Glycobiology 5:319-325(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal liver;
PubMed=10504389; DOI=10.1046/j.1432-1327.1999.00733.x;
Shang J., Qiu R., Wang J., Liu J., Zhou R., Ding H., Yang S.,
Zhang S., Jin C.;
"Molecular cloning and expression of Galbeta1,3GalNAc alpha2, 3-
sialyltransferase from human fetal liver.";
Eur. J. Biochem. 265:580-588(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Responsible for the synthesis of the sequence NeuAc-
alpha-2,3-Gal-beta-1,3-GalNAc- found on sugar chains O-linked to
Thr or Ser and also as a terminal sequence on certain
gangliosides. SIAT4A and SIAT4B sialylate the same acceptor
substrates but exhibit different Km values.
{ECO:0000250|UniProtKB:P54751}.
-!- CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + beta-D-galactosyl-
1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-
acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-
galactosaminyl-R. {ECO:0000250|UniProtKB:P54751}.
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane;
Single-pass type II membrane protein. Secreted. Note=Membrane-
bound form in trans cisternae of Golgi. Secreted into the body
fluid.
-!- TISSUE SPECIFICITY: Expressed in several tissues. Highest
expression in lung, liver, skeletal muscle, kidney, pancreas,
spleen and placenta.
-!- PTM: The soluble form derives from the membrane form by
proteolytic processing.
-!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=ST3Gal I;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_622";
-----------------------------------------------------------------------
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EMBL; L29555; AAA36612.1; -; mRNA.
EMBL; L13972; AAC37574.1; -; mRNA.
EMBL; AF059321; AAC17874.1; -; mRNA.
EMBL; BC018357; AAH18357.1; -; mRNA.
CCDS; CCDS6373.1; -.
PIR; I54229; I54229.
RefSeq; NP_003024.1; NM_003033.3.
RefSeq; NP_775479.1; NM_173344.2.
RefSeq; XP_005251082.1; XM_005251025.4.
RefSeq; XP_006716680.1; XM_006716617.1.
RefSeq; XP_011515527.1; XM_011517225.1.
RefSeq; XP_016869225.1; XM_017013736.1.
RefSeq; XP_016869226.1; XM_017013737.1.
UniGene; Hs.374257; -.
ProteinModelPortal; Q11201; -.
SMR; Q11201; -.
BioGrid; 112375; 16.
IntAct; Q11201; 1.
STRING; 9606.ENSP00000318445; -.
BindingDB; Q11201; -.
ChEMBL; CHEMBL3596074; -.
CAZy; GT29; Glycosyltransferase Family 29.
PhosphoSitePlus; Q11201; -.
BioMuta; ST3GAL1; -.
DMDM; 1705559; -.
EPD; Q11201; -.
MaxQB; Q11201; -.
PaxDb; Q11201; -.
PeptideAtlas; Q11201; -.
PRIDE; Q11201; -.
DNASU; 6482; -.
Ensembl; ENST00000399640; ENSP00000414073; ENSG00000008513.
Ensembl; ENST00000521180; ENSP00000428540; ENSG00000008513.
Ensembl; ENST00000522652; ENSP00000430515; ENSG00000008513.
GeneID; 6482; -.
KEGG; hsa:6482; -.
UCSC; uc003yuk.3; human.
CTD; 6482; -.
DisGeNET; 6482; -.
EuPathDB; HostDB:ENSG00000008513.14; -.
GeneCards; ST3GAL1; -.
HGNC; HGNC:10862; ST3GAL1.
HPA; HPA040466; -.
MIM; 607187; gene.
neXtProt; NX_Q11201; -.
OpenTargets; ENSG00000008513; -.
PharmGKB; PA35764; -.
eggNOG; KOG2692; Eukaryota.
eggNOG; ENOG410XT8P; LUCA.
GeneTree; ENSGT00760000119095; -.
HOGENOM; HOG000126811; -.
HOVERGEN; HBG054227; -.
InParanoid; Q11201; -.
KO; K00780; -.
OMA; TWFPKQM; -.
OrthoDB; EOG091G08DE; -.
PhylomeDB; Q11201; -.
TreeFam; TF354325; -.
BioCyc; MetaCyc:HS00250-MONOMER; -.
BRENDA; 2.4.99.4; 2681.
BRENDA; 2.4.99.6; 2681.
Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
Reactome; R-HSA-4085001; Sialic acid metabolism.
Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
SIGNOR; Q11201; -.
UniPathway; UPA00378; -.
ChiTaRS; ST3GAL1; human.
GenomeRNAi; 6482; -.
PRO; PR:Q11201; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000008513; -.
CleanEx; HS_ST3GAL1; -.
ExpressionAtlas; Q11201; baseline and differential.
Genevisible; Q11201; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IDA:CACAO.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
GO; GO:0006054; P:N-acetylneuraminate metabolic process; ISS:UniProtKB.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
GO; GO:0097503; P:sialylation; ISS:UniProtKB.
Gene3D; 3.90.1480.20; -; 1.
InterPro; IPR001675; Glyco_trans_29.
InterPro; IPR038578; GT29-like_sf.
InterPro; IPR012163; Sialyl_trans.
Pfam; PF00777; Glyco_transf_29; 1.
PIRSF; PIRSF005557; Sialyl_trans; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Membrane; Polymorphism; Reference proteome; Secreted;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 340 CMP-N-acetylneuraminate-beta-
galactosamide-alpha-2,3-sialyltransferase
1.
/FTId=PRO_0000149253.
TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.
TRANSMEM 14 34 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 35 340 Lumenal. {ECO:0000255}.
BINDING 105 105 Substrate. {ECO:0000250}.
BINDING 147 147 Substrate. {ECO:0000250}.
BINDING 170 170 Substrate. {ECO:0000250}.
BINDING 230 230 Substrate. {ECO:0000250}.
BINDING 266 266 Substrate. {ECO:0000250}.
BINDING 270 270 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 290 290 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 299 299 Substrate. {ECO:0000250}.
BINDING 316 316 Substrate. {ECO:0000250}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 59 64 {ECO:0000250}.
DISULFID 61 139 {ECO:0000250}.
DISULFID 142 281 {ECO:0000250}.
VARIANT 111 111 N -> S (in dbSNP:rs116342938).
/FTId=VAR_049225.
CONFLICT 12 12 L -> V (in Ref. 2; AAA36612).
{ECO:0000305}.
CONFLICT 86 86 L -> V (in Ref. 3; AAC17874).
{ECO:0000305}.
CONFLICT 219 219 S -> R (in Ref. 3; AAC17874).
{ECO:0000305}.
SEQUENCE 340 AA; 39075 MW; A3E81D9C85446843 CRC64;
MVTLRKRTLK VLTFLVLFIF LTSFFLNYSH TMVATTWFPK QMVLELSENL KRLIKHRPCT
CTHCIGQRKL SAWFDERFNQ TMQPLLTAQN ALLEDDTYRW WLRLQREKKP NNLNDTIKEL
FRVVPGNVDP MLEKRSVGCR RCAVVGNSGN LRESSYGPEI DSHDFVLRMN KAPTAGFEAD
VGTKTTHHLV YPESFRELGD NVSMILVPFK TIDLEWVVSA ITTGTISHTY IPVPAKIRVK
QDKILIYHPA FIKYVFDNWL QGHGRYPSTG ILSVIFSMHV CDEVDLYGFG ADSKGNWHHY
WENNPSAGAF RKTGVHDADF ESNVTATLAS INKIRIFKGR


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