SIA7B_CHICK
ID SIA7B_CHICK Reviewed; 404 AA.
AC Q92184;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2;
DE EC=2.4.99.3 {ECO:0000269|PubMed:8034663};
DE AltName: Full=Gal-beta-1,3-GalNAc alpha-2,6-sialyltransferase;
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase II;
DE AltName: Full=ST6GalNAc II;
DE Short=ST6GalNAcII;
DE AltName: Full=Sialyltransferase 7B;
DE Short=SIAT7-B;
GN Name=ST6GALNAC2; Synonyms=SIAT7B;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=8034663; DOI=10.1016/s0021-9258(17)32272-x;
RA Kurosawa N., Kojima N., Inoue M., Hamamoto T., Tsuji S.;
RT "Cloning and expression of Gal beta 1,3GalNAc-specific GalNAc alpha 2,6-
RT sialyltransferase.";
RL J. Biol. Chem. 269:19048-19053(1994).
CC -!- FUNCTION: Catalyzes the transfer of N-acetylneuraminyl groups onto
CC glycan chains in glycoproteins (PubMed:8034663). Shows a preference for
CC N-acetylgalactosamine (GalNAc) residues already modified by the
CC addition of galactose or galactose followed by sialic acid in alpha-2,3
CC linkage (PubMed:8034663). {ECO:0000269|PubMed:8034663}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = a beta-D-galactosyl-
CC (1->3)-[N-acetyl-alpha-neuraminyl-(2->6)]-N-acetyl-alpha-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:11136,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133470, ChEBI:CHEBI:140764; EC=2.4.99.3;
CC Evidence={ECO:0000269|PubMed:8034663};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11137;
CC Evidence={ECO:0000269|PubMed:8034663};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:8034663}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Heart, kidney, testes, brain, liver and lung.
CC {ECO:0000269|PubMed:8034663}.
CC -!- DEVELOPMENTAL STAGE: Abundantly expressed at all embryonic stages but
CC not present in adult tissues. {ECO:0000269|PubMed:8034663}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; X77775; CAA54813.1; -; mRNA.
DR PIR; A54871; A54871.
DR RefSeq; NP_990564.1; NM_205233.1.
DR AlphaFoldDB; Q92184; -.
DR SMR; Q92184; -.
DR STRING; 9031.ENSGALP00000002914; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q92184; -.
DR GeneID; 396159; -.
DR KEGG; gga:396159; -.
DR CTD; 10610; -.
DR VEuPathDB; HostDB:geneid_396159; -.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q92184; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q92184; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q92184; -.
DR Proteomes; UP000000539; 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:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:1990743; P:protein sialylation; 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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..404
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 2"
FT /id="PRO_0000149274"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..404
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 77..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT BINDING 209
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT BINDING 334
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT BINDING 366
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..178
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT DISULFID 181..347
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
SQ SEQUENCE 404 AA; 45826 MW; DCC177AA01ABB60A CRC64;
MGSPRWKRFC FLLLAAFTSS LLLYGHYYAT VDVRSGPRVV TSLLQPELLF LVRPDTPHPD
NSHHKELRGT VKSREFFSQP SSELEKPKPS GKQPTPCPRS VAATAKADPT FGELFQFDIP
VLMWDQHFNP ETWDRLKARR VPYGWQGLSQ AAVGSTLRLL NTSSNTRLFD RHLFPGGCIR
CAVVGNGGIL NGSRQGRAID AHDLVFRLNG AITKGFEEDV GSKVSFYGFT VNTMKNSLIA
YEAYGFTRTP QGKDLKYIFI PSDARDYIML RSAIQGSPVP EGLDKGDEPQ KYFGLEASAE
KFKLLHPDFL HYLTTRFLRS ELLDMQYGHL YMPSTGALML LTALHTCDQV SAYGFITANY
EQFSDHYYEP EKKPLVFYAN HDMLLEAELW RSLHRAGIME LYQR
