SIA10_HUMAN
ID SIA10_HUMAN Reviewed; 331 AA.
AC Q9Y274; B2RCH2; B3KMI1; D3DN39; F8W6U0;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Type 2 lactosamine alpha-2,3-sialyltransferase;
DE EC=2.4.99.-;
DE AltName: Full=CMP-NeuAc:beta-galactoside alpha-2,3-sialyltransferase VI;
DE AltName: Full=ST3Gal VI;
DE Short=ST3GalVI;
DE AltName: Full=Sialyltransferase 10;
GN Name=ST3GAL6; Synonyms=SIAT10;
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), AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=10206952; DOI=10.1074/jbc.274.17.11479;
RA Okajima T., Fukumoto S., Miyazaki H., Ishida H., Kiso M., Furukawa K.,
RA Urano T., Furukawa K.;
RT "Molecular cloning of a novel alpha2,3-sialyltransferase (ST3Gal VI) that
RT sialylates type II lactosamine structures on glycoproteins and
RT glycolipids.";
RL J. Biol. Chem. 274:11479-11486(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Kapitonov D., Yu R.K.;
RT "Sialyltransferases.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: Involved in the synthesis of sialyl-paragloboside, a
CC precursor of sialyl-Lewis X determinant. Has a alpha-2,3-
CC sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on
CC glycoproteins and glycolipids. Has a restricted substrate specificity,
CC it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and
CC neolactotetraosylceramide and neolactohexaosylceramide, but not
CC lactotetraosylceramide, lactosylceramide or asialo-GM1.
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=Q9Y274-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y274-2; Sequence=VSP_047009, VSP_047010;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST3Gal
CC VI;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_627";
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DR EMBL; AB022918; BAA77609.1; -; mRNA.
DR EMBL; AF119391; AAD39131.1; -; mRNA.
DR EMBL; AK315111; BAG37569.1; -; mRNA.
DR EMBL; AK001922; BAG50993.1; -; mRNA.
DR EMBL; AC106728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79849.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79850.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79852.1; -; Genomic_DNA.
DR EMBL; BC023312; AAH23312.1; -; mRNA.
DR CCDS; CCDS2933.1; -. [Q9Y274-1]
DR CCDS; CCDS59452.1; -. [Q9Y274-2]
DR RefSeq; NP_001258074.1; NM_001271145.1.
DR RefSeq; NP_001258075.1; NM_001271146.1. [Q9Y274-1]
DR RefSeq; NP_001258076.1; NM_001271147.1. [Q9Y274-2]
DR RefSeq; NP_001310281.1; NM_001323352.1. [Q9Y274-1]
DR RefSeq; NP_001310294.1; NM_001323365.1. [Q9Y274-1]
DR RefSeq; NP_001310296.1; NM_001323367.1. [Q9Y274-1]
DR RefSeq; NP_001310297.1; NM_001323368.1. [Q9Y274-1]
DR RefSeq; NP_006091.1; NM_006100.3. [Q9Y274-1]
DR AlphaFoldDB; Q9Y274; -.
DR SMR; Q9Y274; -.
DR BioGRID; 115674; 28.
DR CORUM; Q9Y274; -.
DR IntAct; Q9Y274; 5.
DR STRING; 9606.ENSP00000480884; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyConnect; 1868; 11 N-Linked glycans (1 site).
DR GlyGen; Q9Y274; 7 sites, 11 N-linked glycans (1 site).
DR iPTMnet; Q9Y274; -.
DR PhosphoSitePlus; Q9Y274; -.
DR BioMuta; ST3GAL6; -.
DR DMDM; 54039605; -.
DR EPD; Q9Y274; -.
DR MassIVE; Q9Y274; -.
DR PaxDb; Q9Y274; -.
DR PeptideAtlas; Q9Y274; -.
DR PRIDE; Q9Y274; -.
DR ProteomicsDB; 29837; -.
DR ProteomicsDB; 85676; -. [Q9Y274-1]
DR Antibodypedia; 35151; 60 antibodies from 23 providers.
DR DNASU; 10402; -.
DR Ensembl; ENST00000265261.11; ENSP00000265261.7; ENSG00000064225.13. [Q9Y274-1]
DR Ensembl; ENST00000394162.5; ENSP00000377717.1; ENSG00000064225.13. [Q9Y274-1]
DR Ensembl; ENST00000483910.6; ENSP00000417376.1; ENSG00000064225.13. [Q9Y274-1]
DR Ensembl; ENST00000613264.5; ENSP00000480884.2; ENSG00000064225.13. [Q9Y274-1]
DR GeneID; 10402; -.
DR KEGG; hsa:10402; -.
DR MANE-Select; ENST00000483910.6; ENSP00000417376.1; NM_001323368.2; NP_001310297.1.
DR UCSC; uc003dsz.5; human. [Q9Y274-1]
DR CTD; 10402; -.
DR DisGeNET; 10402; -.
DR GeneCards; ST3GAL6; -.
DR HGNC; HGNC:18080; ST3GAL6.
DR HPA; ENSG00000064225; Tissue enhanced (liver).
DR MIM; 607156; gene.
DR neXtProt; NX_Q9Y274; -.
DR OpenTargets; ENSG00000064225; -.
DR PharmGKB; PA134958548; -.
DR VEuPathDB; HostDB:ENSG00000064225; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000161415; -.
DR HOGENOM; CLU_032020_1_2_1; -.
DR InParanoid; Q9Y274; -.
DR OMA; LYWISFY; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q9Y274; -.
DR TreeFam; TF354325; -.
DR BioCyc; MetaCyc:ENSG00000064225-MON; -.
DR PathwayCommons; Q9Y274; -.
DR Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR SignaLink; Q9Y274; -.
DR BioGRID-ORCS; 10402; 38 hits in 1070 CRISPR screens.
DR ChiTaRS; ST3GAL6; human.
DR GenomeRNAi; 10402; -.
DR Pharos; Q9Y274; Tbio.
DR PRO; PR:Q9Y274; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y274; protein.
DR Bgee; ENSG00000064225; Expressed in adrenal tissue and 189 other tissues.
DR ExpressionAtlas; Q9Y274; baseline and differential.
DR Genevisible; Q9Y274; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; TAS:Reactome.
DR GO; GO:0052798; F:beta-galactoside alpha-2,3-sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0071354; P:cellular response to interleukin-6; IEP:UniProtKB.
DR GO; GO:0006664; P:glycolipid metabolic process; IDA:UniProtKB.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; TAS:Reactome.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0036211; P:protein modification process; 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 Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..331
FT /note="Type 2 lactosamine alpha-2,3-sialyltransferase"
FT /id="PRO_0000149305"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..331
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047009"
FT VAR_SEQ 112..144
FT /note="NIPCKKCVVVGNGGVLKNKTLGEKIDSYDVIIR -> K (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047010"
FT VARIANT 311
FT /note="A -> T (in dbSNP:rs28489284)"
FT /id="VAR_049227"
FT CONFLICT 271
FT /note="C -> S (in Ref. 3; BAG50993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 38214 MW; DD2B3D88D3D0A055 CRC64;
MRGYLVAIFL SAVFLYYVLH CILWGTNVYW VAPVEMKRRN KIQPCLSKPA FASLLRFHQF
HPFLCAADFR KIASLYGSDK FDLPYGMRTS AEYFRLALSK LQSCDLFDEF DNIPCKKCVV
VGNGGVLKNK TLGEKIDSYD VIIRMNNGPV LGHEEEVGRR TTFRLFYPES VFSDPIHNDP
NTTVILTAFK PHDLRWLLEL LMGDKINTNG FWKKPALNLI YKPYQIRILD PFIIRTAAYE
LLHFPKVFPK NQKPKHPTTG IIAITLAFYI CHEVHLAGFK YNFSDLKSPL HYYGNATMSL
MNKNAYHNVT AEQLFLKDII EKNLVINLTQ D
