SIA7B_HUMAN
ID SIA7B_HUMAN Reviewed; 374 AA.
AC Q9UJ37; Q12971;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2;
DE EC=2.4.99.3 {ECO:0000269|PubMed:10742600, ECO:0000269|PubMed:29251719};
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase II;
DE AltName: Full=ST6GalNAc II {ECO:0000303|PubMed:10742600};
DE Short=ST6GalNAcII {ECO:0000303|PubMed:29251719};
DE AltName: Full=SThM;
DE AltName: Full=Sialyltransferase 7B;
DE Short=SIAT7-B;
GN Name=ST6GALNAC2; Synonyms=SIAT7B, SIATL1, STHM;
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, CATALYTIC ACTIVITY, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=10742600; DOI=10.1016/s0304-4165(00)00020-9;
RA Samyn-Petit B., Krzewinski-Recchi M.A., Steelant W.F.A., Delannoy P.,
RA Harduin-Lepers A.;
RT "Molecular cloning and functional expression of human ST6GalNAc II.
RT Molecular expression in various human cultured cells.";
RL Biochim. Biophys. Acta 1474:201-211(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RA Sotiropoulou G., Anisowicz A., Sager R.;
RT "Isolation and cloning from human mammary epithelial cells of a complete
RT cDNA sequence homologous to other known sialyltransferases.";
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [5] {ECO:0007744|PDB:6APJ, ECO:0007744|PDB:6APL}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH CMP, FUNCTION,
RP CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION
RP AT ASN-85; ASN-130 AND ASN-161, AND DISULFIDE BONDS.
RX PubMed=29251719; DOI=10.1038/nchembio.2539;
RA Moremen K.W., Ramiah A., Stuart M., Steel J., Meng L., Forouhar F.,
RA Moniz H.A., Gahlay G., Gao Z., Chapla D., Wang S., Yang J.Y.,
RA Prabhakar P.K., Johnson R., Rosa M.D., Geisler C., Nairn A.V.,
RA Seetharaman J., Wu S.C., Tong L., Gilbert H.J., LaBaer J., Jarvis D.L.;
RT "Expression system for structural and functional studies of human
RT glycosylation enzymes.";
RL Nat. Chem. Biol. 14:156-162(2018).
RN [6]
RP INVOLVEMENT IN IGA NEPHROPATHY.
RX PubMed=19357720; DOI=10.1038/ki.2009.99;
RA Zhu L., Tang W., Li G., Lv J., Ding J., Yu L., Zhao M., Li Y., Zhang X.,
RA Shen Y., Zhang H., Wang H.;
RT "Interaction between variants of two glycosyltransferase genes in IgA
RT nephropathy.";
RL Kidney Int. 76:190-198(2009).
CC -!- FUNCTION: Catalyzes the transfer of N-acetylneuraminyl groups onto
CC glycan chains in glycoproteins (PubMed:10742600, PubMed:29251719).
CC Shows a preference for N-acetylgalactosamine (GalNAc) residues already
CC modified by the addition of galactose or galactose followed by sialic
CC acid in alpha-2,3 linkage (PubMed:10742600).
CC {ECO:0000269|PubMed:10742600, ECO:0000269|PubMed:29251719}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = a beta-D-galactosyl-
CC (1->3)-[N-acetyl-alpha-neuraminyl-(2->6)]-N-acetyl-alpha-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:11136,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133470, ChEBI:CHEBI:140764; EC=2.4.99.3;
CC Evidence={ECO:0000269|PubMed:10742600, ECO:0000269|PubMed:29251719};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11137;
CC Evidence={ECO:0000269|PubMed:10742600, ECO:0000269|PubMed:29251719};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=130 uM for CMP-N-acetylneuraminate {ECO:0000269|PubMed:10742600};
CC KM=104 uM for CMP-N-acetylneuraminate {ECO:0000269|PubMed:29251719};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:10742600, ECO:0000269|PubMed:29251719}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, kidney,
CC placenta, lung and leukocytes. {ECO:0000269|PubMed:10742600}.
CC -!- MISCELLANEOUS: Aberrant O-galactosylation of IgA1 molecules plays a
CC role in the development and progression of IgA nephropathy (IgAN).
CC Genetic interactions of C1GALT1 and ST6GALNAC2 variants influence IgA1
CC O-glycosylation, disease predisposition, and disease severity, and may
CC contribute to the polygenic nature of IgAN.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6GalNAc
CC II;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_631";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ251053; CAB61434.1; -; mRNA.
DR EMBL; U14550; AAA52228.1; -; mRNA.
DR EMBL; BT019972; AAV38775.1; -; mRNA.
DR EMBL; BC040455; AAH40455.1; -; mRNA.
DR CCDS; CCDS11747.1; -.
DR RefSeq; NP_006447.2; NM_006456.2.
DR PDB; 6APJ; X-ray; 3.10 A; A/B/C/D/E/F=1-374.
DR PDB; 6APL; X-ray; 2.35 A; A/B/C/D/E/F=1-374.
DR PDBsum; 6APJ; -.
DR PDBsum; 6APL; -.
DR AlphaFoldDB; Q9UJ37; -.
DR SMR; Q9UJ37; -.
DR BioGRID; 115856; 3.
DR IntAct; Q9UJ37; 1.
DR MINT; Q9UJ37; -.
DR STRING; 9606.ENSP00000225276; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q9UJ37; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UJ37; -.
DR PhosphoSitePlus; Q9UJ37; -.
DR BioMuta; ST6GALNAC2; -.
DR DMDM; 21759448; -.
DR EPD; Q9UJ37; -.
DR MassIVE; Q9UJ37; -.
DR MaxQB; Q9UJ37; -.
DR PaxDb; Q9UJ37; -.
DR PeptideAtlas; Q9UJ37; -.
DR PRIDE; Q9UJ37; -.
DR ProteomicsDB; 84582; -.
DR Antibodypedia; 32441; 106 antibodies from 19 providers.
DR DNASU; 10610; -.
DR Ensembl; ENST00000225276.10; ENSP00000225276.4; ENSG00000070731.11.
DR GeneID; 10610; -.
DR KEGG; hsa:10610; -.
DR MANE-Select; ENST00000225276.10; ENSP00000225276.4; NM_006456.3; NP_006447.2.
DR UCSC; uc002jsg.5; human.
DR CTD; 10610; -.
DR DisGeNET; 10610; -.
DR GeneCards; ST6GALNAC2; -.
DR HGNC; HGNC:10867; ST6GALNAC2.
DR HPA; ENSG00000070731; Low tissue specificity.
DR MIM; 610137; gene.
DR neXtProt; NX_Q9UJ37; -.
DR OpenTargets; ENSG00000070731; -.
DR PharmGKB; PA35769; -.
DR VEuPathDB; HostDB:ENSG00000070731; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000160433; -.
DR HOGENOM; CLU_032020_0_0_1; -.
DR InParanoid; Q9UJ37; -.
DR OMA; LHYIFIP; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q9UJ37; -.
DR TreeFam; TF354325; -.
DR BRENDA; 2.4.99.3; 2681.
DR PathwayCommons; Q9UJ37; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-9683673; Maturation of protein 3a.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-9694719; Maturation of protein 3a.
DR Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
DR SignaLink; Q9UJ37; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 10610; 7 hits in 1059 CRISPR screens.
DR ChiTaRS; ST6GALNAC2; human.
DR GeneWiki; ST6GALNAC2; -.
DR GenomeRNAi; 10610; -.
DR Pharos; Q9UJ37; Tbio.
DR PRO; PR:Q9UJ37; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UJ37; protein.
DR Bgee; ENSG00000070731; Expressed in tibial nerve and 98 other tissues.
DR ExpressionAtlas; Q9UJ37; baseline and differential.
DR Genevisible; Q9UJ37; 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:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; TAS:Reactome.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
DR GO; GO:1990743; P:protein sialylation; IDA:UniProtKB.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
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..374
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 2"
FT /id="PRO_0000149272"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..374
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000269|PubMed:29251719,
FT ECO:0007744|PDB:6APL"
FT BINDING 179
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000269|PubMed:29251719,
FT ECO:0007744|PDB:6APL"
FT BINDING 304
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000269|PubMed:29251719,
FT ECO:0007744|PDB:6APL"
FT BINDING 336
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000269|PubMed:29251719,
FT ECO:0007744|PDB:6APL"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29251719,
FT ECO:0007744|PDB:6APL"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29251719,
FT ECO:0007744|PDB:6APL"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29251719,
FT ECO:0007744|PDB:6APL"
FT DISULFID 66..148
FT /evidence="ECO:0000269|PubMed:29251719,
FT ECO:0007744|PDB:6APJ, ECO:0007744|PDB:6APL"
FT DISULFID 151..317
FT /evidence="ECO:0000269|PubMed:29251719,
FT ECO:0007744|PDB:6APJ, ECO:0007744|PDB:6APL"
FT CONFLICT 11
FT /note="L -> V (in Ref. 2; AAA52228)"
FT /evidence="ECO:0000305"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:6APL"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6APL"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:6APL"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:6APL"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:6APL"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:6APL"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:6APL"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:6APL"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:6APL"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:6APL"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 305..316
FT /evidence="ECO:0007829|PDB:6APL"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:6APL"
FT HELIX 328..332
FT /evidence="ECO:0007829|PDB:6APL"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:6APJ"
FT HELIX 353..365
FT /evidence="ECO:0007829|PDB:6APL"
SQ SEQUENCE 374 AA; 41939 MW; E0BD439E4C6BB427 CRC64;
MGLPRGSFFW LLLLLTAACS GLLFALYFSA VQRYPGPAAG ARDTTSFEAF FQSKASNSWT
GKGQACRHLL HLAIQRHPHF RGLFNLSIPV LLWGDLFTPA LWDRLSQHKA PYGWRGLSHQ
VIASTLSLLN GSESAKLFAP PRDTPPKCIR CAVVGNGGIL NGSRQGPNID AHDYVFRLNG
AVIKGFERDV GTKTSFYGFT VNTMKNSLVS YWNLGFTSVP QGQDLQYIFI PSDIRDYVML
RSAILGVPVP EGLDKGDRPH AYFGPEASAS KFKLLHPDFI SYLTERFLKS KLINTHFGDL
YMPSTGALML LTALHTCDQV SAYGFITSNY WKFSDHYFER KMKPLIFYAN HDLSLEAALW
RDLHKAGILQ LYQR
