SIA8D_HUMAN
ID SIA8D_HUMAN Reviewed; 359 AA.
AC Q92187; A8KA07; G3V104; Q8N1F4; Q92693;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 178.
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=PST, PST1, SIAT8D;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=7624364; DOI=10.1073/pnas.92.15.7031;
RA Nakayama J., Fukuda M.N., Fredette B., Ranscht B., Fukuda M.;
RT "Expression cloning of a human polysialyltransferase that forms the
RT polysialylated neural cell adhesion molecule present in embryonic brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7031-7035(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP LYS-7.
RC TISSUE=Brain, and Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-74.
RX PubMed=11279095; DOI=10.1074/jbc.m100576200;
RA Angata K., Yen T.Y., El-Battari A., Macher B.A., Fukuda M.;
RT "Unique disulfide bond structures found in ST8Sia IV polysialyltransferase
RT are required for its activity.";
RL J. Biol. Chem. 276:15369-15377(2001).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-92.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92187-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92187-2; Sequence=VSP_044867;
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal brain, lung and kidney
CC and in adult heart, spleen and thymus. Present to a lesser extent in
CC adult brain, placenta, lung, large and small intestine and peripheral
CC blood leukocytes.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia
CC IV;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_639";
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DR EMBL; L41680; AAC41775.1; -; mRNA.
DR EMBL; AK292872; BAF85561.1; -; mRNA.
DR EMBL; AC010411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW49104.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW49105.1; -; Genomic_DNA.
DR EMBL; BC027866; AAH27866.1; -; mRNA.
DR EMBL; BC053657; AAH53657.1; -; mRNA.
DR CCDS; CCDS4091.1; -. [Q92187-1]
DR CCDS; CCDS47252.1; -. [Q92187-2]
DR PIR; I59403; I59403.
DR RefSeq; NP_005659.1; NM_005668.5. [Q92187-1]
DR RefSeq; NP_778222.1; NM_175052.2. [Q92187-2]
DR PDB; 5Y22; NMR; -; A=258-279.
DR PDB; 5Y3U; NMR; -; A=258-279.
DR PDB; 6AHZ; NMR; -; A=245-279.
DR PDBsum; 5Y22; -.
DR PDBsum; 5Y3U; -.
DR PDBsum; 6AHZ; -.
DR AlphaFoldDB; Q92187; -.
DR SMR; Q92187; -.
DR BioGRID; 113636; 84.
DR IntAct; Q92187; 66.
DR STRING; 9606.ENSP00000231461; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q92187; 5 sites.
DR iPTMnet; Q92187; -.
DR PhosphoSitePlus; Q92187; -.
DR BioMuta; ST8SIA4; -.
DR DMDM; 2494834; -.
DR EPD; Q92187; -.
DR MassIVE; Q92187; -.
DR PaxDb; Q92187; -.
DR PeptideAtlas; Q92187; -.
DR PRIDE; Q92187; -.
DR ProteomicsDB; 32217; -.
DR ProteomicsDB; 75254; -. [Q92187-1]
DR ABCD; Q92187; 1 sequenced antibody.
DR Antibodypedia; 25167; 182 antibodies from 24 providers.
DR DNASU; 7903; -.
DR Ensembl; ENST00000231461.10; ENSP00000231461.4; ENSG00000113532.13. [Q92187-1]
DR Ensembl; ENST00000451528.2; ENSP00000428914.1; ENSG00000113532.13. [Q92187-2]
DR GeneID; 7903; -.
DR KEGG; hsa:7903; -.
DR MANE-Select; ENST00000231461.10; ENSP00000231461.4; NM_005668.6; NP_005659.1.
DR UCSC; uc003knk.5; human. [Q92187-1]
DR CTD; 7903; -.
DR DisGeNET; 7903; -.
DR GeneCards; ST8SIA4; -.
DR HGNC; HGNC:10871; ST8SIA4.
DR HPA; ENSG00000113532; Tissue enhanced (lymphoid).
DR MIM; 602547; gene.
DR neXtProt; NX_Q92187; -.
DR OpenTargets; ENSG00000113532; -.
DR PharmGKB; PA35772; -.
DR VEuPathDB; HostDB:ENSG00000113532; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR HOGENOM; CLU_048583_3_0_1; -.
DR InParanoid; Q92187; -.
DR OMA; HAAEGWK; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; Q92187; -.
DR TreeFam; TF352820; -.
DR BRENDA; 2.4.99.8; 2681.
DR PathwayCommons; Q92187; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR SignaLink; Q92187; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 7903; 8 hits in 1063 CRISPR screens.
DR ChiTaRS; ST8SIA4; human.
DR GeneWiki; ST8SIA4; -.
DR GenomeRNAi; 7903; -.
DR Pharos; Q92187; Tbio.
DR PRO; PR:Q92187; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q92187; protein.
DR Bgee; ENSG00000113532; Expressed in bronchial epithelial cell and 163 other tissues.
DR ExpressionAtlas; Q92187; baseline and differential.
DR Genevisible; Q92187; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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; 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:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA:BHF-UCL.
DR GO; GO:0006486; P:protein glycosylation; IDA:BHF-UCL.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
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; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="CMP-N-acetylneuraminate-poly-alpha-2,8-
FT sialyltransferase"
FT /id="PRO_0000149293"
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:0000269|PubMed:11279095"
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:0000269|PubMed:11279095"
FT DISULFID 156..356
FT /evidence="ECO:0000269|PubMed:11279095"
FT VAR_SEQ 169..359
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044867"
FT VARIANT 7
FT /note="R -> K (in dbSNP:rs199768560)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_068976"
FT VARIANT 92
FT /note="E -> G (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036169"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:6AHZ"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:5Y22"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:6AHZ"
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
