SIA8D_PANTR
ID SIA8D_PANTR Reviewed; 359 AA.
AC P61645;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase;
DE EC=2.4.99.-;
DE AltName: Full=Alpha-2,8-sialyltransferase 8D;
DE AltName: Full=Polysialyltransferase-1;
DE AltName: Full=Sialyltransferase 8D;
DE Short=SIAT8-D;
DE AltName: Full=Sialyltransferase St8Sia IV;
DE Short=ST8SiaIV;
GN Name=ST8SIA4; Synonyms=SIAT8D;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Harduin-Lepers A., Martinez-Duncker I., Mollicone R., Delannoy P.,
RA Oriol R.;
RT "Phylogeny of sialyltransferases.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the polycondensation of alpha-2,8-linked sialic
CC acid required for the synthesis of polysialic acid (PSA), which is
CC present on the embryonic neural cell adhesion molecule (N-CAM),
CC necessary for plasticity of neural cells. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
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; AJ697661; CAG26899.1; -; mRNA.
DR RefSeq; NP_001032379.1; NM_001037302.1.
DR AlphaFoldDB; P61645; -.
DR SMR; P61645; -.
DR STRING; 9598.ENSPTRP00000029282; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; P61645; -.
DR Ensembl; ENSPTRT00000104834; ENSPTRP00000091792; ENSPTRG00000042921.
DR GeneID; 461971; -.
DR KEGG; ptr:461971; -.
DR CTD; 7903; -.
DR VGNC; VGNC:13603; ST8SIA4.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR HOGENOM; CLU_048583_3_0_1; -.
DR InParanoid; P61645; -.
DR OMA; HAAEGWK; -.
DR OrthoDB; 825014at2759; -.
DR TreeFam; TF352820; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000042921; Expressed in lymph node and 17 other tissues.
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:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IEA:Ensembl.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..359
FT /note="CMP-N-acetylneuraminate-poly-alpha-2,8-
FT sialyltransferase"
FT /id="PRO_0000149295"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..20
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 21..359
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 331
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 191..193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 279..281
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 314..315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..292
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 156..356
FT /evidence="ECO:0000250|UniProtKB:O43173"
SQ SEQUENCE 359 AA; 41295 MW; C53FFDF658926D61 CRC64;
MRSIRKRWTI CTISLLLIFY KTKEIARTEE HQETQLIGDG ELSLSRSLVN SSDKIIRKAG
SSIFQHNVEG WKINSSLVLE IRKNILRFLD AERDVSVVKS SFKPGDVIHY VLDRRRTLNI
SHDLHSLLPE VSPMKNRRFK TCAVVGNSGI LLDSECGKEI DSHNFVIRCN LAPVVEFAAD
VGTKSDFITM NPSVVQRAFG GFRNESDREK FVHRLSMLND SVLWIPAFMV KGGEKHVEWV
NALILKNKLK VRTAYPSLRL IHAVRGYWLT NKVPIKRPST GLLMYTLATR FCDEIHLYGF
WPFPKDLNGK AVKYHYYDDL KYRYFSNASP HRMPLEFKTL NVLHNRGALK LTTGKCVKQ
