Full text data of ST8SIA3
ST8SIA3
(SIAT8C)
[Confidence: low (only semi-automatic identification from reviews)]
Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase; 2.4.99.- (Alpha-2,8-sialyltransferase 8C; Alpha-2,8-sialyltransferase III; ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3; Sialyltransferase 8C; SIAT8-C; Sialyltransferase St8Sia III; ST8SiaIII)
Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase; 2.4.99.- (Alpha-2,8-sialyltransferase 8C; Alpha-2,8-sialyltransferase III; ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3; Sialyltransferase 8C; SIAT8-C; Sialyltransferase St8Sia III; ST8SiaIII)
UniProt
O43173
ID SIA8C_HUMAN Reviewed; 380 AA.
AC O43173; A8K0F2; Q6B085; Q9NS41;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase;
DE EC=2.4.99.-;
DE AltName: Full=Alpha-2,8-sialyltransferase 8C;
DE AltName: Full=Alpha-2,8-sialyltransferase III;
DE AltName: Full=ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3;
DE AltName: Full=Sialyltransferase 8C;
DE Short=SIAT8-C;
DE AltName: Full=Sialyltransferase St8Sia III;
DE Short=ST8SiaIII;
GN Name=ST8SIA3; Synonyms=SIAT8C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9826427; DOI=10.1006/abbi.1998.0909;
RA Lee Y.-C., Kim Y.-J., Lee K.-Y., Kim K.-S., Kim B.-U., Kim H.-N.,
RA Kim C.-H., Do S.-I.;
RT "Cloning and expression of cDNA for a human Sia alpha 2,3Gal beta
RT 1,4GlcNA:alpha 2,8-sialyltransferase (hST8Sia III).";
RL Arch. Biochem. Biophys. 360:41-46(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Fetal brain;
RX PubMed=10766765; DOI=10.1074/jbc.M910204199;
RA Angata K., Suzuki M., McAuliffe J., Ding Y., Hindsgaul O., Fukuda M.;
RT "Differential biosynthesis of polysialic acid on neural cell adhesion
RT molecule (NCAM) and oligosaccharide acceptors by three distinct
RT alpha2,8-Sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and
RT ST8Sia III.";
RL J. Biol. Chem. 275:18594-18601(2000).
RN [3]
RP SEQUENCE REVISION TO 19; 241 AND 296.
RA Angata K., Fukuda M.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May transfer sialic acid through alpha-2,8-linkages to
CC alpha-2,3-linked and alpha-2,8-linked sialic acid of N-linked
CC oligosaccharides of glycoproteins and glycolipids. It can form
CC polysialic acid in vitro directly on alpha-2,3-, alpha-2,6-, or
CC alpha-2,8-linked sialic acid.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC II membrane protein (Potential).
CC -!- TISSUE SPECIFICITY: Expressed in fetal and adult brain and fetal
CC liver.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database;
CC URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/Homolog?cat=symbol&symbol;=ST8SIA3";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=ST8Sia III;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_638";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF004668; AAB87642.1; -; mRNA.
DR EMBL; AF003092; AAC15901.2; -; mRNA.
DR EMBL; AK289517; BAF82206.1; -; mRNA.
DR EMBL; AK313047; BAG35879.1; -; mRNA.
DR EMBL; BC074909; AAH74909.1; -; mRNA.
DR RefSeq; NP_056963.2; NM_015879.2.
DR UniGene; Hs.23172; -.
DR ProteinModelPortal; O43173; -.
DR SMR; O43173; 84-321.
DR STRING; 9606.ENSP00000320431; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PhosphoSite; O43173; -.
DR PaxDb; O43173; -.
DR PRIDE; O43173; -.
DR DNASU; 51046; -.
DR Ensembl; ENST00000324000; ENSP00000320431; ENSG00000177511.
DR GeneID; 51046; -.
DR KEGG; hsa:51046; -.
DR UCSC; uc002lgn.3; human.
DR CTD; 51046; -.
DR GeneCards; GC18P055019; -.
DR HGNC; HGNC:14269; ST8SIA3.
DR MIM; 609478; gene.
DR neXtProt; NX_O43173; -.
DR PharmGKB; PA37864; -.
DR eggNOG; NOG275903; -.
DR HOVERGEN; HBG056466; -.
DR InParanoid; O43173; -.
DR KO; K06613; -.
DR OMA; THELQEK; -.
DR OrthoDB; EOG7VQJD1; -.
DR PhylomeDB; O43173; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR UniPathway; UPA00378; -.
DR GenomeRNAi; 51046; -.
DR NextBio; 53604; -.
DR PRO; PR:O43173; -.
DR ArrayExpress; O43173; -.
DR Bgee; O43173; -.
DR CleanEx; HS_ST8SIA3; -.
DR Genevestigator; O43173; -.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030173; C:integral to Golgi membrane; IEA:InterPro.
DR GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0033691; F:sialic acid binding; IC:BHF-UCL.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0006491; P:N-glycan processing; IDA:BHF-UCL.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR InterPro; IPR001675; Glyco_trans_29.
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 Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Polymorphism; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 380 Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha
FT 2,8-sialyltransferase.
FT /FTId=PRO_0000149289.
FT TOPO_DOM 1 9 Cytoplasmic (Potential).
FT TRANSMEM 10 33 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 34 380 Lumenal (Potential).
FT CARBOHYD 93 93 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 113 113 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 206 206 N-linked (GlcNAc...) (Potential).
FT DISULFID 162 313 By similarity.
FT VARIANT 91 91 K -> T (in dbSNP:rs3745060).
FT /FTId=VAR_020249.
FT CONFLICT 173 174 GS -> FI (in Ref. 1; AAB87642).
FT CONFLICT 178 178 Q -> R (in Ref. 1; AAB87642).
FT CONFLICT 194 194 T -> S (in Ref. 1; AAB87642).
SQ SEQUENCE 380 AA; 43970 MW; 70D782A2CAD2666A CRC64;
MRNCKMARVA SVLGLVMLSV ALLILSLISY VSLKKENIFT TPKYASPGAP RMYMFHAGFR
SQFALKFLDP SFVPITNSLT QELQEKPSKW KFNRTAFLHQ RQEILQHVDV IKNFSLTKNS
VRIGQLMHYD YSSHKYVFSI SNNFRSLLPD VSPIMNKHYN ICAVVGNSGI LTGSQCGQEI
DKSDFVFRCN FAPTEAFQRD VGRKTNLTTF NPSILEKYYN NLLTIQDRNN FFLSLKKLDG
AILWIPAFFF HTSATVTRTL VDFFVEHRGQ LKVQLAWPGN IMQHVNRYWK NKHLSPKRLS
TGILMYTLAS AICEEIHLYG FWPFGFDPNT REDLPYHYYD KKGTKFTTKW QESHQLPAEF
QLLYRMHGEG LTKLTLSHCA
//
ID SIA8C_HUMAN Reviewed; 380 AA.
AC O43173; A8K0F2; Q6B085; Q9NS41;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase;
DE EC=2.4.99.-;
DE AltName: Full=Alpha-2,8-sialyltransferase 8C;
DE AltName: Full=Alpha-2,8-sialyltransferase III;
DE AltName: Full=ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3;
DE AltName: Full=Sialyltransferase 8C;
DE Short=SIAT8-C;
DE AltName: Full=Sialyltransferase St8Sia III;
DE Short=ST8SiaIII;
GN Name=ST8SIA3; Synonyms=SIAT8C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9826427; DOI=10.1006/abbi.1998.0909;
RA Lee Y.-C., Kim Y.-J., Lee K.-Y., Kim K.-S., Kim B.-U., Kim H.-N.,
RA Kim C.-H., Do S.-I.;
RT "Cloning and expression of cDNA for a human Sia alpha 2,3Gal beta
RT 1,4GlcNA:alpha 2,8-sialyltransferase (hST8Sia III).";
RL Arch. Biochem. Biophys. 360:41-46(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Fetal brain;
RX PubMed=10766765; DOI=10.1074/jbc.M910204199;
RA Angata K., Suzuki M., McAuliffe J., Ding Y., Hindsgaul O., Fukuda M.;
RT "Differential biosynthesis of polysialic acid on neural cell adhesion
RT molecule (NCAM) and oligosaccharide acceptors by three distinct
RT alpha2,8-Sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and
RT ST8Sia III.";
RL J. Biol. Chem. 275:18594-18601(2000).
RN [3]
RP SEQUENCE REVISION TO 19; 241 AND 296.
RA Angata K., Fukuda M.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May transfer sialic acid through alpha-2,8-linkages to
CC alpha-2,3-linked and alpha-2,8-linked sialic acid of N-linked
CC oligosaccharides of glycoproteins and glycolipids. It can form
CC polysialic acid in vitro directly on alpha-2,3-, alpha-2,6-, or
CC alpha-2,8-linked sialic acid.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC II membrane protein (Potential).
CC -!- TISSUE SPECIFICITY: Expressed in fetal and adult brain and fetal
CC liver.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database;
CC URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/Homolog?cat=symbol&symbol;=ST8SIA3";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=ST8Sia III;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_638";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF004668; AAB87642.1; -; mRNA.
DR EMBL; AF003092; AAC15901.2; -; mRNA.
DR EMBL; AK289517; BAF82206.1; -; mRNA.
DR EMBL; AK313047; BAG35879.1; -; mRNA.
DR EMBL; BC074909; AAH74909.1; -; mRNA.
DR RefSeq; NP_056963.2; NM_015879.2.
DR UniGene; Hs.23172; -.
DR ProteinModelPortal; O43173; -.
DR SMR; O43173; 84-321.
DR STRING; 9606.ENSP00000320431; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PhosphoSite; O43173; -.
DR PaxDb; O43173; -.
DR PRIDE; O43173; -.
DR DNASU; 51046; -.
DR Ensembl; ENST00000324000; ENSP00000320431; ENSG00000177511.
DR GeneID; 51046; -.
DR KEGG; hsa:51046; -.
DR UCSC; uc002lgn.3; human.
DR CTD; 51046; -.
DR GeneCards; GC18P055019; -.
DR HGNC; HGNC:14269; ST8SIA3.
DR MIM; 609478; gene.
DR neXtProt; NX_O43173; -.
DR PharmGKB; PA37864; -.
DR eggNOG; NOG275903; -.
DR HOVERGEN; HBG056466; -.
DR InParanoid; O43173; -.
DR KO; K06613; -.
DR OMA; THELQEK; -.
DR OrthoDB; EOG7VQJD1; -.
DR PhylomeDB; O43173; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR UniPathway; UPA00378; -.
DR GenomeRNAi; 51046; -.
DR NextBio; 53604; -.
DR PRO; PR:O43173; -.
DR ArrayExpress; O43173; -.
DR Bgee; O43173; -.
DR CleanEx; HS_ST8SIA3; -.
DR Genevestigator; O43173; -.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030173; C:integral to Golgi membrane; IEA:InterPro.
DR GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0033691; F:sialic acid binding; IC:BHF-UCL.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0006491; P:N-glycan processing; IDA:BHF-UCL.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR InterPro; IPR001675; Glyco_trans_29.
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 Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Polymorphism; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 380 Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha
FT 2,8-sialyltransferase.
FT /FTId=PRO_0000149289.
FT TOPO_DOM 1 9 Cytoplasmic (Potential).
FT TRANSMEM 10 33 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 34 380 Lumenal (Potential).
FT CARBOHYD 93 93 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 113 113 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 206 206 N-linked (GlcNAc...) (Potential).
FT DISULFID 162 313 By similarity.
FT VARIANT 91 91 K -> T (in dbSNP:rs3745060).
FT /FTId=VAR_020249.
FT CONFLICT 173 174 GS -> FI (in Ref. 1; AAB87642).
FT CONFLICT 178 178 Q -> R (in Ref. 1; AAB87642).
FT CONFLICT 194 194 T -> S (in Ref. 1; AAB87642).
SQ SEQUENCE 380 AA; 43970 MW; 70D782A2CAD2666A CRC64;
MRNCKMARVA SVLGLVMLSV ALLILSLISY VSLKKENIFT TPKYASPGAP RMYMFHAGFR
SQFALKFLDP SFVPITNSLT QELQEKPSKW KFNRTAFLHQ RQEILQHVDV IKNFSLTKNS
VRIGQLMHYD YSSHKYVFSI SNNFRSLLPD VSPIMNKHYN ICAVVGNSGI LTGSQCGQEI
DKSDFVFRCN FAPTEAFQRD VGRKTNLTTF NPSILEKYYN NLLTIQDRNN FFLSLKKLDG
AILWIPAFFF HTSATVTRTL VDFFVEHRGQ LKVQLAWPGN IMQHVNRYWK NKHLSPKRLS
TGILMYTLAS AICEEIHLYG FWPFGFDPNT REDLPYHYYD KKGTKFTTKW QESHQLPAEF
QLLYRMHGEG LTKLTLSHCA
//
MIM
609478
*RECORD*
*FIELD* NO
609478
*FIELD* TI
*609478 ST8 ALPHA-N-ACETYL-NEURAMINIDE ALPHA-2,8-SIALYLTRANSFERASE 3; ST8SIA3
;;ALPHA-2,8-SIALYLTRANSFERASE III;;
read moreST8SIA III
*FIELD* TX
DESCRIPTION
ST8SIA3 belongs to a family of sialyltransferases that form
sialyl-alpha-2,8-sialyl-R linkages at the nonreducing termini of
glycoconjugates (Lee et al., 1998).
CLONING
By PCR of a brain cDNA library using primers designed from mouse
St8sia3, followed by library screening and 5-prime RACE of brain mRNA,
Lee et al. (1998) cloned human ST8SIA3. The deduced 380-amino acid
protein has a type II transmembrane topology and 3 potential
N-glycosylation sites. ST8SIA3 shares 96% amino acid identity with mouse
St8sia3. Northern blot analysis of adult and fetal tissues detected an
11-kb transcript mainly expressed in fetal and adult brain. A 5.5-kb
transcript was also expressed in fetal liver. The pattern of human
ST8SIA3 expression was distinct from that found for mouse St8sia3.
Angata et al. (2000) cloned ST8SIA3 by RT-PCR and 5-prime RACE of brain
mRNA. ST8SIA3 contains an N-terminal signal/membrane-anchoring domain,
followed by a central sialyl L motif and a sialyl S motif.
GENE FUNCTION
Lee et al. (1998) assayed the sialyltransferase activity of a
recombinant soluble form of ST8SIA3 following expression in COS-7 cells.
ST8SIA3 had strong catalytic activity in transferring sialic acid
through alpha-2,8-linkage to intact fetuin glycoprotein. Activity was
undetectable toward alpha-2,6-sialylated glycoprotein, desialylated
glycoprotein acceptors, and other glycan residues.
Angata et al. (2000) compared the sialyltransferase activities of
ST8SIA2 (602546), ST8SIA3, and ST8SIA4 (602547). All 3 enzymes could add
oligosialic and polysialic acid on various sialylated
N-acetyllactosaminyl oligosaccharides, including NCAM (116930)
N-glycans, fetuin N-glycans, synthetic sialylated N-acetyllactosamines,
and alpha-2-Heremans Schmid glycoprotein. The 3 enzymes could also use
themselves as substrates in autopolysialylation reactions. The enzymes
differed in the efficiency of adding polysialic acid on NCAM, and
ST8SIA3 did not use NCAM as substrate. Upon transfection and
overexpression in HeLa cells, ST8SIA2 and ST8SIA4 formed polysialic acid
on glycoproteins in the perinuclear Golgi compartment and on
glycoproteins on the cell surface. ST8SIA3 only formed polysialic acid
on Golgi glycoproteins, confirming that it does not use cell-surface
NCAM as substrate.
GENE STRUCTURE
Angata et al. (2000) determined that the ST8SIA3 gene contains 4 coding
exons.
MAPPING
By genomic sequence analysis and FISH, Angata et al. (2000) mapped the
ST8SIA3 gene to chromosome 18q21.2.
*FIELD* RF
1. Angata, K.; Suzuki, M.; McAuliffe, J.; Ding, Y.; Hindsgaul, O.;
Fukuda, M.: Differential biosynthesis of polysialic acid on neural
cell adhesion molecule (NCAM) and oligosaccharide acceptors by three
distinct alpha-2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II
(STX), and ST8Sia III. J. Biol. Chem. 275: 18594-18601, 2000.
2. Lee, Y.-C.; Kim, Y.-J.; Lee, K.-Y.; Kim, K.-S.; Kim, B.-U.; Kim,
H.-N.; Kim, C.-H.; Do, S.-I.: Cloning and expression of cDNA for
a human Sia-alpha-2,3-Gal-beta-1,4-GlcNA:alpha-2,8-sialyltransferase
(hST8Sia III). Arch. Biochem. Biophys. 360: 41-46, 1998.
*FIELD* CD
Patricia A. Hartz: 7/18/2005
*FIELD* ED
mgross: 07/20/2005
mgross: 7/18/2005
*RECORD*
*FIELD* NO
609478
*FIELD* TI
*609478 ST8 ALPHA-N-ACETYL-NEURAMINIDE ALPHA-2,8-SIALYLTRANSFERASE 3; ST8SIA3
;;ALPHA-2,8-SIALYLTRANSFERASE III;;
read moreST8SIA III
*FIELD* TX
DESCRIPTION
ST8SIA3 belongs to a family of sialyltransferases that form
sialyl-alpha-2,8-sialyl-R linkages at the nonreducing termini of
glycoconjugates (Lee et al., 1998).
CLONING
By PCR of a brain cDNA library using primers designed from mouse
St8sia3, followed by library screening and 5-prime RACE of brain mRNA,
Lee et al. (1998) cloned human ST8SIA3. The deduced 380-amino acid
protein has a type II transmembrane topology and 3 potential
N-glycosylation sites. ST8SIA3 shares 96% amino acid identity with mouse
St8sia3. Northern blot analysis of adult and fetal tissues detected an
11-kb transcript mainly expressed in fetal and adult brain. A 5.5-kb
transcript was also expressed in fetal liver. The pattern of human
ST8SIA3 expression was distinct from that found for mouse St8sia3.
Angata et al. (2000) cloned ST8SIA3 by RT-PCR and 5-prime RACE of brain
mRNA. ST8SIA3 contains an N-terminal signal/membrane-anchoring domain,
followed by a central sialyl L motif and a sialyl S motif.
GENE FUNCTION
Lee et al. (1998) assayed the sialyltransferase activity of a
recombinant soluble form of ST8SIA3 following expression in COS-7 cells.
ST8SIA3 had strong catalytic activity in transferring sialic acid
through alpha-2,8-linkage to intact fetuin glycoprotein. Activity was
undetectable toward alpha-2,6-sialylated glycoprotein, desialylated
glycoprotein acceptors, and other glycan residues.
Angata et al. (2000) compared the sialyltransferase activities of
ST8SIA2 (602546), ST8SIA3, and ST8SIA4 (602547). All 3 enzymes could add
oligosialic and polysialic acid on various sialylated
N-acetyllactosaminyl oligosaccharides, including NCAM (116930)
N-glycans, fetuin N-glycans, synthetic sialylated N-acetyllactosamines,
and alpha-2-Heremans Schmid glycoprotein. The 3 enzymes could also use
themselves as substrates in autopolysialylation reactions. The enzymes
differed in the efficiency of adding polysialic acid on NCAM, and
ST8SIA3 did not use NCAM as substrate. Upon transfection and
overexpression in HeLa cells, ST8SIA2 and ST8SIA4 formed polysialic acid
on glycoproteins in the perinuclear Golgi compartment and on
glycoproteins on the cell surface. ST8SIA3 only formed polysialic acid
on Golgi glycoproteins, confirming that it does not use cell-surface
NCAM as substrate.
GENE STRUCTURE
Angata et al. (2000) determined that the ST8SIA3 gene contains 4 coding
exons.
MAPPING
By genomic sequence analysis and FISH, Angata et al. (2000) mapped the
ST8SIA3 gene to chromosome 18q21.2.
*FIELD* RF
1. Angata, K.; Suzuki, M.; McAuliffe, J.; Ding, Y.; Hindsgaul, O.;
Fukuda, M.: Differential biosynthesis of polysialic acid on neural
cell adhesion molecule (NCAM) and oligosaccharide acceptors by three
distinct alpha-2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II
(STX), and ST8Sia III. J. Biol. Chem. 275: 18594-18601, 2000.
2. Lee, Y.-C.; Kim, Y.-J.; Lee, K.-Y.; Kim, K.-S.; Kim, B.-U.; Kim,
H.-N.; Kim, C.-H.; Do, S.-I.: Cloning and expression of cDNA for
a human Sia-alpha-2,3-Gal-beta-1,4-GlcNA:alpha-2,8-sialyltransferase
(hST8Sia III). Arch. Biochem. Biophys. 360: 41-46, 1998.
*FIELD* CD
Patricia A. Hartz: 7/18/2005
*FIELD* ED
mgross: 07/20/2005
mgross: 7/18/2005