SIA8C_HUMAN
ID SIA8C_HUMAN Reviewed; 380 AA.
AC O43173; A8K0F2; Q6B085; Q9NS41;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase;
DE EC=2.4.99.- {ECO:0000269|PubMed:26192331};
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 {ECO:0000303|PubMed:9826427};
DE Short=ST8SiaIII {ECO:0000303|PubMed:26192331};
GN Name=ST8SIA3; Synonyms=SIAT8C;
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], 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 alpha2,8-
RT Sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and 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., 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 [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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6] {ECO:0007744|PDB:5BO6, ECO:0007744|PDB:5BO7, ECO:0007744|PDB:5BO8, ECO:0007744|PDB:5BO9}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 81-380 IN COMPLEXES WITH CDP; CTP
RP AND SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF
RP HIS-354, SUBUNIT, PATHWAY, DISULFIDE BONDS, GLYCOSYLATION AT ASN-93;
RP ASN-113; ASN-160 AND ASN-206, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26192331; DOI=10.1038/nsmb.3060;
RA Volkers G., Worrall L.J., Kwan D.H., Yu C.C., Baumann L., Lameignere E.,
RA Wasney G.A., Scott N.E., Wakarchuk W., Foster L.J., Withers S.G.,
RA Strynadka N.C.;
RT "Structure of human ST8SiaIII sialyltransferase provides insight into cell-
RT surface polysialylation.";
RL Nat. Struct. Mol. Biol. 22:627-635(2015).
CC -!- FUNCTION: Catalyzes the transfer of sialic acid from a CMP-linked
CC sialic acid donor onto the terminal sialic acid of an acceptor through
CC alpha-2,8-linkages. Is active with alpha-2,3-linked, alpha-2,6-linked
CC and alpha-2,8-linked sialic acid of N-linked oligosaccharides of
CC glycoproteins and glycolipids. Displays preference for substrates with
CC alpha-2,3-linked terminal sialic acid. It can form polysialic acid in
CC vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic
CC acid. {ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:26192331,
CC ECO:0000269|PubMed:9826427}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:10766765, ECO:0000305|PubMed:26192331}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26192331}.
CC -!- INTERACTION:
CC O43173; O43173: ST8SIA3; NbExp=4; IntAct=EBI-16165155, EBI-16165155;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in fetal and adult brain and fetal liver.
CC {ECO:0000269|PubMed:9826427}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia
CC III;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_638";
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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 CCDS; CCDS32834.1; -.
DR RefSeq; NP_056963.2; NM_015879.2.
DR PDB; 5BO6; X-ray; 2.07 A; A/B=81-380.
DR PDB; 5BO7; X-ray; 1.85 A; A/B=81-380.
DR PDB; 5BO8; X-ray; 2.70 A; A/B=61-380.
DR PDB; 5BO9; X-ray; 2.30 A; A/B=81-380.
DR PDB; 5CXY; X-ray; 2.15 A; A/B=81-380.
DR PDBsum; 5BO6; -.
DR PDBsum; 5BO7; -.
DR PDBsum; 5BO8; -.
DR PDBsum; 5BO9; -.
DR PDBsum; 5CXY; -.
DR AlphaFoldDB; O43173; -.
DR SMR; O43173; -.
DR BioGRID; 119243; 34.
DR DIP; DIP-61706N; -.
DR IntAct; O43173; 11.
DR STRING; 9606.ENSP00000320431; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; O43173; 4 sites.
DR iPTMnet; O43173; -.
DR PhosphoSitePlus; O43173; -.
DR BioMuta; ST8SIA3; -.
DR MassIVE; O43173; -.
DR PaxDb; O43173; -.
DR PeptideAtlas; O43173; -.
DR PRIDE; O43173; -.
DR ProteomicsDB; 48790; -.
DR Antibodypedia; 22809; 73 antibodies from 19 providers.
DR DNASU; 51046; -.
DR Ensembl; ENST00000324000.4; ENSP00000320431.2; ENSG00000177511.6.
DR GeneID; 51046; -.
DR KEGG; hsa:51046; -.
DR MANE-Select; ENST00000324000.4; ENSP00000320431.2; NM_015879.3; NP_056963.2.
DR UCSC; uc002lgn.4; human.
DR CTD; 51046; -.
DR DisGeNET; 51046; -.
DR GeneCards; ST8SIA3; -.
DR HGNC; HGNC:14269; ST8SIA3.
DR HPA; ENSG00000177511; Tissue enhanced (brain, pituitary gland, retina).
DR MIM; 609478; gene.
DR neXtProt; NX_O43173; -.
DR OpenTargets; ENSG00000177511; -.
DR PharmGKB; PA37864; -.
DR VEuPathDB; HostDB:ENSG00000177511; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR HOGENOM; CLU_048583_0_0_1; -.
DR InParanoid; O43173; -.
DR OMA; PIHNKHY; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; O43173; -.
DR TreeFam; TF323961; -.
DR BRENDA; 2.4.99.8; 2681.
DR PathwayCommons; O43173; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR SignaLink; O43173; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 51046; 4 hits in 1064 CRISPR screens.
DR ChiTaRS; ST8SIA3; human.
DR GenomeRNAi; 51046; -.
DR Pharos; O43173; Tbio.
DR PRO; PR:O43173; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; O43173; protein.
DR Bgee; ENSG00000177511; Expressed in middle temporal gyrus and 111 other tissues.
DR ExpressionAtlas; O43173; baseline and differential.
DR Genevisible; O43173; 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0033691; F:sialic acid binding; IC:BHF-UCL.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0009100; P:glycoprotein metabolic process; IDA:BHF-UCL.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; TAS:ProtInc.
DR GO; GO:0006491; P:N-glycan processing; IDA:UniProtKB.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA:BHF-UCL.
DR GO; GO:0006486; P:protein glycosylation; IDA:BHF-UCL.
DR GO; GO:1990743; P:protein sialylation; IDA: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 3D-structure; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..380
FT /note="Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-
FT sialyltransferase"
FT /id="PRO_0000149289"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..380
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 354
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:26192331"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26192331"
FT BINDING 211..213
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26192331"
FT BINDING 300..302
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26192331"
FT BINDING 336..337
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26192331"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26192331"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26192331"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:26192331"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26192331"
FT DISULFID 162..313
FT /evidence="ECO:0000269|PubMed:26192331,
FT ECO:0007744|PDB:5BO6, ECO:0007744|PDB:5BO7,
FT ECO:0007744|PDB:5BO8, ECO:0007744|PDB:5BO9"
FT DISULFID 176..379
FT /evidence="ECO:0000269|PubMed:26192331,
FT ECO:0007744|PDB:5BO6, ECO:0007744|PDB:5BO7,
FT ECO:0007744|PDB:5BO8, ECO:0007744|PDB:5BO9"
FT VARIANT 91
FT /note="K -> T (in dbSNP:rs3745060)"
FT /id="VAR_020249"
FT MUTAGEN 354
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:26192331"
FT CONFLICT 173..174
FT /note="GS -> FI (in Ref. 1; AAB87642)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="Q -> R (in Ref. 1; AAB87642)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="T -> S (in Ref. 1; AAB87642)"
FT /evidence="ECO:0000305"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:5BO7"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:5BO7"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:5BO7"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:5BO7"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:5BO7"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:5BO7"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:5BO7"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:5BO7"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:5BO7"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:5BO7"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:5BO7"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:5BO7"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:5BO7"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:5BO6"
FT HELIX 356..368
FT /evidence="ECO:0007829|PDB:5BO7"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:5BO7"
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
