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Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase (EC 2.4.99.8) (Alpha-2,8-sialyltransferase 8A) (Ganglioside GD3 synthase) (Sialyltransferase 8A) (SIAT8-A) (Sialyltransferase St8Sia I) (ST8SiaI)

 SIA8A_XENTR             Reviewed;         345 AA.
Q6DNG6;
16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 2.
28-MAR-2018, entry version 61.
RecName: Full=Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase {ECO:0000250|UniProtKB:Q92185};
EC=2.4.99.8;
AltName: Full=Alpha-2,8-sialyltransferase 8A;
AltName: Full=Ganglioside GD3 synthase {ECO:0000250|UniProtKB:Q6ZXA0};
AltName: Full=Sialyltransferase 8A;
Short=SIAT8-A;
AltName: Full=Sialyltransferase St8Sia I;
Short=ST8SiaI;
Name=st8sia1; Synonyms=st8siaI {ECO:0000312|EMBL:AAI70804.1};
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Silurana.
NCBI_TaxID=8364;
[1] {ECO:0000305, ECO:0000312|EMBL:AAT67042.2}
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=17333390; DOI=10.1007/s11010-006-9406-1;
Rimoldi S., Papis E., Bernardini G., Prati M., Gornati R.;
"Molecular cloning and expression of alpha2,8-sialyltransferase
(ST8Sia I, GD3 Synthase) in Xenopus.";
Mol. Cell. Biochem. 301:143-153(2007).
[2] {ECO:0000312|EMBL:AAI70804.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
NIH - Xenopus Gene Collection (XGC) project;
Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the production of gangliosides GD3 and GT3
from GM3. Gangliosides are a subfamily of complex
glycosphingolipids that contain one or more residues of sialic
acid; glycosphingolipids are required for convergence extension
movements during early development (By similarity).
{ECO:0000250|UniProtKB:Q6ZXA0}.
-!- CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + alpha-N-
acetylneuraminyl-(2->3)-beta-D-galactosyl-R = CMP + alpha-N-
acetylneuraminyl-(2->8)-alpha-N-acetylneuraminyl-(2->3)-beta-D-
galactosyl-R. {ECO:0000250|UniProtKB:Q6ZXA0}.
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000305}.
-!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
{ECO:0000250|UniProtKB:Q6ZXA0}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000250|UniProtKB:Q6ZXA0}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:Q6ZXA0}.
-!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
{ECO:0000255}.
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EMBL; AY652775; AAT67042.2; -; mRNA.
EMBL; BC170804; AAI70804.1; -; mRNA.
EMBL; BC170806; AAI70806.1; -; mRNA.
RefSeq; NP_001003659.1; NM_001003659.1.
UniGene; Str.24556; -.
SMR; Q6DNG6; -.
CAZy; GT29; Glycosyltransferase Family 29.
GeneID; 444887; -.
KEGG; xtr:444887; -.
CTD; 6489; -.
Xenbase; XB-GENE-5824739; st8sia1.
InParanoid; Q6DNG6; -.
KO; K03371; -.
BRENDA; 2.4.99.8; 8483.
UniPathway; UPA00222; -.
UniPathway; UPA00378; -.
Proteomes; UP000008143; Unassembled WGS sequence.
GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; ISS:UniProtKB.
GO; GO:0001574; P:ganglioside biosynthetic process; ISS:UniProtKB.
GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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; Developmental protein; Disulfide bond;
Glycoprotein; Glycosyltransferase; Golgi apparatus;
Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
Signal-anchor; Sphingolipid metabolism; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 345 Alpha-N-acetylneuraminide alpha-2,8-
sialyltransferase.
/FTId=PRO_0000376860.
TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.
TRANSMEM 16 36 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 37 345 Lumenal. {ECO:0000255}.
REGION 176 178 Substrate binding.
{ECO:0000250|UniProtKB:O43173}.
REGION 262 264 Substrate binding.
{ECO:0000250|UniProtKB:O43173}.
ACT_SITE 310 310 Proton donor/acceptor.
{ECO:0000250|UniProtKB:O43173}.
BINDING 154 154 Substrate.
{ECO:0000250|UniProtKB:O43173}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 233 233 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 126 275 {ECO:0000250|UniProtKB:O43173}.
DISULFID 140 335 {ECO:0000250|UniProtKB:O43173}.
SEQUENCE 345 AA; 39831 MW; 222B64EA41A2C62F CRC64;
MKLQGSRMWL CPRTRLPVGA SALGFLILCW LYVFPGYRLP GHKEMVREVL RFGPGWRKNR
TEMDSFRKLL QDCCDPPHLF SLTKVNTPLG ENLWFDGEFF HSLTIDNSTR SLFPQDTPFK
LPLKRCSVVG NGGILKNSRC GEQIDEADFV MRCNLPPLSR EYTEDVGTRT QLVTVNPSII
DKRYQNLLWS RKSFVENLRV YQQSYVYMPA FSTKRGTDPS LRVYYTLADF GTNQTVLFAN
PNFLRNVGKF WKSRGIHSKR LSTGLFMVSA ALSLCEEVTI YGFWPFQMDL GGRYISHHYY
DNTLPLSGVH AMPEEFLQLW LLHKSGVLQM QLDQCKKDVS SQKPH


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