SIA4A_PIG
ID SIA4A_PIG Reviewed; 343 AA.
AC Q02745;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1;
DE Short=Alpha 2,3-ST 1;
DE Short=Beta-galactoside alpha-2,3-sialyltransferase 1;
DE EC=2.4.99.4 {ECO:0000269|PubMed:19820709, ECO:0000269|PubMed:8288606};
DE AltName: Full=Gal-NAc6S;
DE AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase;
DE AltName: Full=Monosialoganglioside sialyltransferase;
DE EC=2.4.99.2 {ECO:0000269|PubMed:8288606};
DE AltName: Full=ST3Gal I;
DE Short=ST3GalI;
DE AltName: Full=ST3GalA.1;
DE AltName: Full=ST3O;
DE AltName: Full=Sialyltransferase 4A;
DE Short=SIAT4-A;
GN Name=ST3GAL1; Synonyms=SIAT4A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 8-29 AND 56-77, AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Liver, and Salivary gland;
RX PubMed=1383214; DOI=10.1016/s0021-9258(19)36789-4;
RA Gillespie W.M., Kelm S., Paulson J.C.;
RT "Cloning and expression of the Gal beta 1, 3GalNAc alpha 2,3-
RT sialyltransferase.";
RL J. Biol. Chem. 267:21004-21010(1992).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8288606; DOI=10.1016/s0021-9258(17)42271-x;
RA Kitagawa H., Paulson J.C.;
RT "Cloning of a novel alpha 2,3-sialyltransferase that sialylates
RT glycoprotein and glycolipid carbohydrate groups.";
RL J. Biol. Chem. 269:1394-1401(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 46-343 IN COMPLEXES WITH CMP AND
RP N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE, CATALYTIC ACTIVITY, FUNCTION, AND
RP DISULFIDE BONDS.
RX PubMed=19820709; DOI=10.1038/nsmb.1685;
RA Rao F.V., Rich J.R., Rakic B., Buddai S., Schwartz M.F., Johnson K.,
RA Bowe C., Wakarchuk W.W., Defrees S., Withers S.G., Strynadka N.C.;
RT "Structural insight into mammalian sialyltransferases.";
RL Nat. Struct. Mol. Biol. 16:1186-1188(2009).
CC -!- FUNCTION: A beta-galactoside alpha2-3 sialyltransferase involved in
CC terminal sialylation of glycoproteins and glycolipids (PubMed:19820709,
CC PubMed:8288606). Catalyzes the transfer of sialic acid (N-acetyl-
CC neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac
CC onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates through
CC an alpha2-3 linkage (PubMed:19820709, PubMed:8288606). Adds sialic acid
CC to the core 1 O-glycan, Galbeta-(1->3)-GalNAc-O-Ser/Thr, which is a
CC major structure of mucin-type O-glycans (PubMed:19820709,
CC PubMed:8288606). As part of a homeostatic mechanism that regulates CD8-
CC positive T cell numbers, sialylates core 1 O-glycans of T cell
CC glycoproteins, SPN/CD43 and PTPRC/CD45. Prevents premature apoptosis of
CC thymic CD8-positive T cells prior to peripheral emigration, whereas in
CC the secondary lymphoid organs controls the survival of CD8-positive
CC memory T cells generated following a successful immune response (By
CC similarity). Transfers sialic acid to asialofetuin, presumably onto
CC Galbeta-(1->3)-GalNAc-O-Ser (PubMed:8288606). Sialylates GM1a, GA1 and
CC GD1b gangliosides to form GD1a, GM1b and GT1b, respectively
CC (PubMed:8288606) (By similarity). {ECO:0000250|UniProtKB:P54751,
CC ECO:0000269|PubMed:19820709, ECO:0000269|PubMed:8288606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:21616,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133470, ChEBI:CHEBI:139596; EC=2.4.99.4;
CC Evidence={ECO:0000269|PubMed:19820709, ECO:0000269|PubMed:8288606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617;
CC Evidence={ECO:0000305|PubMed:19820709, ECO:0000305|PubMed:8288606};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 (d18:1(4E)) =
CC CMP + ganglioside GD1a (d18:1(4E)) + H(+); Xref=Rhea:RHEA:18021,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:77709, ChEBI:CHEBI:78445; EC=2.4.99.2;
CC Evidence={ECO:0000269|PubMed:8288606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022;
CC Evidence={ECO:0000305|PubMed:8288606};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1
CC (d18:1(4E)/18:0) = CMP + ganglioside GD1a (18:1(4E)/18:0) + H(+);
CC Xref=Rhea:RHEA:48248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:90153;
CC Evidence={ECO:0000250|UniProtKB:P54751};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48249;
CC Evidence={ECO:0000250|UniProtKB:P54751};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1 (d18:1(4E)) =
CC CMP + ganglioside GM1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47560,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27938, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78568;
CC Evidence={ECO:0000269|PubMed:8288606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561;
CC Evidence={ECO:0000305|PubMed:8288606};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1b = CMP +
CC ganglioside GT1b + H(+); Xref=Rhea:RHEA:48240, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82939,
CC ChEBI:CHEBI:82940; Evidence={ECO:0000250|UniProtKB:P54751};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48241;
CC Evidence={ECO:0000250|UniProtKB:P54751};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:8288606}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:8288606}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:Q11201}; Single-pass type II membrane protein
CC {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q11201}; Single-pass type II membrane protein
CC {ECO:0000255}. Secreted. Note=Membrane-bound form in medial and trans
CC cisternae of Golgi (By similarity). Secreted into the body fluid.
CC {ECO:0000250|UniProtKB:Q11201}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q02745-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q02745-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: The long isoform is abundant in salivary gland,
CC liver, lung, and colon mucosa. Both long and short forms are detected
CC in submaxillary salivary glands.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
CC -!- MISCELLANEOUS: [Isoform Short]: Seems to lack a 40 residues internal
CC segment. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; M97753; AAA31125.1; -; mRNA.
DR PIR; A45073; A45073.
DR RefSeq; NP_001004047.1; NM_001004047.1. [Q02745-1]
DR PDB; 2WML; X-ray; 1.90 A; A=46-343.
DR PDB; 2WNB; X-ray; 1.55 A; A=46-343.
DR PDB; 2WNF; X-ray; 1.25 A; A=46-343.
DR PDBsum; 2WML; -.
DR PDBsum; 2WNB; -.
DR PDBsum; 2WNF; -.
DR AlphaFoldDB; Q02745; -.
DR SMR; Q02745; -.
DR STRING; 9823.ENSSSCP00000006354; -.
DR SwissLipids; SLP:000001385; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q02745; -.
DR PeptideAtlas; Q02745; -.
DR PRIDE; Q02745; -.
DR GeneID; 445537; -.
DR KEGG; ssc:445537; -.
DR CTD; 6482; -.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q02745; -.
DR BRENDA; 2.4.99.4; 6170.
DR UniPathway; UPA00378; -.
DR EvolutionaryTrace; Q02745; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:1990675; C:Golgi medial cisterna membrane; ISS:UniProtKB.
DR GO; GO:1990676; C:Golgi trans cisterna membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047288; F:monosialoganglioside sialyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; IDA:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0097503; P:sialylation; IDA: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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Secreted; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..343
FT /note="CMP-N-acetylneuraminate-beta-galactosamide-alpha-
FT 2,3-sialyltransferase 1"
FT /id="PRO_0000149256"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..343
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19820709"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19820709"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19820709"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19820709"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19820709"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19820709"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19820709"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19820709"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19820709"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..67
FT /evidence="ECO:0000269|PubMed:19820709"
FT DISULFID 64..142
FT /evidence="ECO:0000269|PubMed:19820709"
FT DISULFID 145..284
FT /evidence="ECO:0000269|PubMed:19820709"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:2WNF"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2WNF"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:2WNF"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2WNF"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:2WNF"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:2WNF"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:2WNF"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2WNF"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:2WNF"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2WNF"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2WNF"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:2WNF"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:2WNF"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:2WNF"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:2WNF"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:2WNF"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:2WNF"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:2WNF"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:2WNF"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:2WNF"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2WNF"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2WNF"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:2WNF"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:2WNF"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:2WNF"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:2WNF"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:2WML"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:2WNF"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:2WNF"
SQ SEQUENCE 343 AA; 39769 MW; 1840274CEDA0E46D CRC64;
MAPMRKKSTL KLLTLLVLFI FLTSFFLNYS HTVVTTAWFP KQMVIELSEN FKKLMKYPYR
PCTCTRCIEE QRVSAWFDER FNRSMQPLLT AKNAHLEEDT YKWWLRLQRE KQPNNLNDTI
RELFQVVPGN VDPLLEKRLV SCRRCAVVGN SGNLKESYYG PQIDSHDFVL RMNKAPTEGF
EADVGSKTTH HFVYPESFRE LAQEVSMILV PFKTTDLEWV ISATTTGRIS HTYVPVPAKI
KVKKEKILIY HPAFIKYVFD RWLQGHGRYP STGILSVIFS LHICDEVDLY GFGADSKGNW
HHYWENNPSA GAFRKTGVHD GDFESNVTTI LASINKIRIF KGR
