SIA8E_HUMAN
ID SIA8E_HUMAN Reviewed; 376 AA.
AC O15466; B7Z1K9; Q6IAW7;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Alpha-2,8-sialyltransferase 8E {ECO:0000305};
DE EC=2.4.99.- {ECO:0000269|PubMed:9199191};
DE AltName: Full=Sialyltransferase 8E;
DE Short=SIAT8-E;
DE AltName: Full=Sialyltransferase St8Sia V;
DE Short=ST8SiaV;
GN Name=ST8SIA5 {ECO:0000312|HGNC:HGNC:17827}; Synonyms=SIAT8E;
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), FUNCTION, TISSUE SPECIFICITY,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RC TISSUE=Brain;
RX PubMed=9199191; DOI=10.1006/bbrc.1997.6725;
RA Kim Y.-J., Kim K.-S., Do S.-I., Kim C.-H., Kim S.-K., Lee Y.-C.;
RT "Molecular cloning and expression of human alpha2,8-sialyltransferase
RT (hST8Sia V).";
RL Biochem. Biophys. Res. Commun. 235:327-330(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Teratocarcinoma;
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 MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
CC -!- FUNCTION: Involved in the synthesis of gangliosides GD1c, GT1a, GQ1b,
CC GP1c and GT3 from GD1a, GT1b, GM1b and GD3 respectively.
CC {ECO:0000269|PubMed:9199191}.
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GT1b (d18:1(4E)) =
CC CMP + ganglioside GQ1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41772,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78452, ChEBI:CHEBI:78455;
CC Evidence={ECO:0000269|PubMed:9199191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41773;
CC Evidence={ECO:0000269|PubMed:9199191};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD3 (d18:1(4E)) =
CC CMP + ganglioside GT3 (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41764,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78436, ChEBI:CHEBI:78438;
CC Evidence={ECO:0000269|PubMed:9199191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41765;
CC Evidence={ECO:0000269|PubMed:9199191};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1a (d18:1(4E)) =
CC CMP + ganglioside GT1a (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41768,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78445, ChEBI:CHEBI:78447;
CC Evidence={ECO:0000269|PubMed:9199191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41769;
CC Evidence={ECO:0000269|PubMed:9199191};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) =
CC CMP + ganglioside GD1c (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47576,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78568, ChEBI:CHEBI:87787;
CC Evidence={ECO:0000269|PubMed:9199191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47577;
CC Evidence={ECO:0000269|PubMed:9199191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GQ1c (d18:1(4E)) =
CC CMP + ganglioside GP1c (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47592,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:87791, ChEBI:CHEBI:87792;
CC Evidence={ECO:0000250|UniProtKB:Q6ZXC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47593;
CC Evidence={ECO:0000250|UniProtKB:Q6ZXC8};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:9199191}.
CC -!- INTERACTION:
CC O15466; Q92624: APPBP2; NbExp=3; IntAct=EBI-10182857, EBI-743771;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q6ZXC8}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15466-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15466-2; Sequence=VSP_056664;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in fetal and adult brain,
CC adult heart and skeletal muscle. {ECO:0000269|PubMed:9199191}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in fetal and adult brain,
CC not detected in adult heart and skeletal muscle.
CC {ECO:0000269|PubMed:9199191}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia V;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_640";
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DR EMBL; U91641; AAC51727.1; -; mRNA.
DR EMBL; AK056270; BAG51661.1; -; mRNA.
DR EMBL; AK293608; BAH11545.1; -; mRNA.
DR EMBL; CR457037; CAG33318.1; -; mRNA.
DR EMBL; AC064800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471088; EAX01483.1; -; Genomic_DNA.
DR EMBL; BC108910; AAI08911.1; -; mRNA.
DR EMBL; BC108911; AAI08912.1; -; mRNA.
DR CCDS; CCDS11930.1; -. [O15466-1]
DR CCDS; CCDS77184.1; -. [O15466-2]
DR PIR; JC5600; JC5600.
DR RefSeq; NP_001294915.1; NM_001307986.1. [O15466-2]
DR RefSeq; NP_001294916.1; NM_001307987.1.
DR RefSeq; NP_037437.2; NM_013305.5. [O15466-1]
DR AlphaFoldDB; O15466; -.
DR SMR; O15466; -.
DR BioGRID; 118954; 62.
DR IntAct; O15466; 2.
DR STRING; 9606.ENSP00000321343; -.
DR SwissLipids; SLP:000001361; -. [O15466-1]
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; O15466; 4 sites.
DR iPTMnet; O15466; -.
DR PhosphoSitePlus; O15466; -.
DR BioMuta; ST8SIA5; -.
DR MassIVE; O15466; -.
DR PaxDb; O15466; -.
DR PeptideAtlas; O15466; -.
DR PRIDE; O15466; -.
DR ProteomicsDB; 48682; -. [O15466-1]
DR ProteomicsDB; 6343; -.
DR Antibodypedia; 54885; 39 antibodies from 10 providers.
DR DNASU; 29906; -.
DR Ensembl; ENST00000315087.12; ENSP00000321343.6; ENSG00000101638.14. [O15466-1]
DR Ensembl; ENST00000538168.5; ENSP00000445492.1; ENSG00000101638.14. [O15466-2]
DR GeneID; 29906; -.
DR KEGG; hsa:29906; -.
DR MANE-Select; ENST00000315087.12; ENSP00000321343.6; NM_013305.6; NP_037437.2.
DR UCSC; uc002lcj.2; human. [O15466-1]
DR CTD; 29906; -.
DR DisGeNET; 29906; -.
DR GeneCards; ST8SIA5; -.
DR HGNC; HGNC:17827; ST8SIA5.
DR HPA; ENSG00000101638; Tissue enhanced (adrenal gland, brain, parathyroid gland).
DR MIM; 607162; gene.
DR neXtProt; NX_O15466; -.
DR OpenTargets; ENSG00000101638; -.
DR PharmGKB; PA38249; -.
DR VEuPathDB; HostDB:ENSG00000101638; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR InParanoid; O15466; -.
DR OMA; FEFNSTA; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; O15466; -.
DR TreeFam; TF323961; -.
DR BRENDA; 2.4.99.8; 2681.
DR PathwayCommons; O15466; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR SignaLink; O15466; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 29906; 12 hits in 1066 CRISPR screens.
DR ChiTaRS; ST8SIA5; human.
DR GenomeRNAi; 29906; -.
DR Pharos; O15466; Tdark.
DR PRO; PR:O15466; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; O15466; protein.
DR Bgee; ENSG00000101638; Expressed in endothelial cell and 134 other tissues.
DR ExpressionAtlas; O15466; baseline and differential.
DR Genevisible; O15466; HS.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
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:0008373; F:sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lipid metabolism; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..376
FT /note="Alpha-2,8-sialyltransferase 8E"
FT /id="PRO_0000149296"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 348
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 214..216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 300..302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 164..313
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 178..373
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT VAR_SEQ 43
FT /note="K -> KRGLQFGWQSGDQLTNWTGLFNVTDDPAVQSGSDSSS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056664"
FT CONFLICT 8
FT /note="A -> P (in Ref. 1; AAC51727)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="F -> G (in Ref. 1; AAC51727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 43895 MW; 15B57F3E06080236 CRC64;
MRYADPSANR DLLGSRTLLF IFICAFALVT LLQQILYGRN YIKRYFEFYE GPFEYNSTRC
LELRHEILEV KVLSMVKQSE LFDRWKSLQM CKWAMNISEA NQFKSTLSRC CNAPAFLFTT
QKNTPLGTKL KYEVDTSGIY HINQEIFRMF PKDMPYYRSQ FKKCAVVGNG GILKNSRCGR
EINSADFVFR CNLPPISEKY TMDVGVKTDV VTVNPSIITE RFHKLEKWRR PFYRVLQVYE
NASVLLPAFY NTRNTDVSIR VKYVLDDFES PQAVYYFHPQ YLVNVSRYWL SLGVRAKRIS
TGLILVTAAL ELCEEVHLFG FWAFPMNPSG LYITHHYYDN VKPRPGFHAM PSEIFNFLHL
HSRGILRVHT GTCSCC
