G3ST2_HUMAN
ID G3ST2_HUMAN Reviewed; 398 AA.
AC Q9H3Q3; Q17RK0; Q57Z52;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Galactose-3-O-sulfotransferase 2;
DE Short=Gal3ST-2;
DE EC=2.8.2.-;
DE AltName: Full=Beta-galactose-3-O-sulfotransferase 2;
DE AltName: Full=Gal-beta-1, 3-GalNAc 3'-sulfotransferase 2;
DE AltName: Full=Glycoprotein beta-Gal 3'-sulfotransferase 2;
GN Name=GAL3ST2; Synonyms=GP3ST;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP ACTIVITY REGULATION, AND VARIANT LEU-4.
RC TISSUE=Colon;
RX PubMed=11029462; DOI=10.1074/jbc.m005666200;
RA Honke K., Tsuda M., Koyota S., Wada Y., Iida-Tanaka N., Ishizuka I.,
RA Nakayama J., Taniguchi N.;
RT "Molecular cloning and characterization of a human beta-Gal-3'-
RT sulfotransferase that acts on both type 1 and type 2 (Galbeta 1-3/1-
RT 4GlcNAc-R) oligosaccharides.";
RL J. Biol. Chem. 276:267-274(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-4.
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: Transfers a sulfate group to the hydroxyl group at C3 of non-
CC reducing beta-galactosyl residues. Acts both on type 1 (Gal-beta-1,3-
CC GlcNAc) and type 2 (Gal-beta-1,4-GlcNAc) chains with similar
CC efficiency.
CC -!- ACTIVITY REGULATION: Strongly inhibited by Cu(2+) and Zn(2+).
CC {ECO:0000269|PubMed:11029462}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-6.5.;
CC -!- PATHWAY: Protein modification; carbohydrate sulfation.
CC -!- INTERACTION:
CC Q9H3Q3; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-10306373, EBI-742948;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305|PubMed:11029462}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:11029462}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, stomach, colon,
CC liver and spleen, in epithelial cells lining the lower to middle layer
CC of the crypts in colonic mucosa, hepatocytes surrounding the central
CC vein of the liver, extravillous cytotrophoblasts in the basal plate of
CC the septum of the placenta, renal tubules of the kidney, and neuronal
CC cells of the cerebral cortex. {ECO:0000269|PubMed:11029462}.
CC -!- SIMILARITY: Belongs to the galactose-3-O-sulfotransferase family.
CC {ECO:0000305}.
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DR EMBL; AB040610; BAB16844.1; -; mRNA.
DR EMBL; AC114730; AAX82021.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71293.1; -; Genomic_DNA.
DR EMBL; BC117293; AAI17294.1; -; mRNA.
DR EMBL; BC117295; AAI17296.1; -; mRNA.
DR CCDS; CCDS33427.1; -.
DR RefSeq; NP_071417.2; NM_022134.2.
DR AlphaFoldDB; Q9H3Q3; -.
DR BioGRID; 122052; 141.
DR IntAct; Q9H3Q3; 1.
DR STRING; 9606.ENSP00000192314; -.
DR GlyGen; Q9H3Q3; 6 sites.
DR iPTMnet; Q9H3Q3; -.
DR PhosphoSitePlus; Q9H3Q3; -.
DR BioMuta; GAL3ST2; -.
DR DMDM; 212276434; -.
DR jPOST; Q9H3Q3; -.
DR MassIVE; Q9H3Q3; -.
DR PaxDb; Q9H3Q3; -.
DR PeptideAtlas; Q9H3Q3; -.
DR PRIDE; Q9H3Q3; -.
DR ProteomicsDB; 80740; -.
DR Antibodypedia; 53483; 11 antibodies from 7 providers.
DR DNASU; 64090; -.
DR Ensembl; ENST00000192314.7; ENSP00000192314.6; ENSG00000154252.12.
DR GeneID; 64090; -.
DR KEGG; hsa:64090; -.
DR MANE-Select; ENST00000192314.7; ENSP00000192314.6; NM_022134.3; NP_071417.2.
DR UCSC; uc002wcj.2; human.
DR CTD; 64090; -.
DR DisGeNET; 64090; -.
DR GeneCards; GAL3ST2; -.
DR HGNC; HGNC:24869; GAL3ST2.
DR HPA; ENSG00000154252; Tissue enriched (intestine).
DR MIM; 608237; gene.
DR neXtProt; NX_Q9H3Q3; -.
DR OpenTargets; ENSG00000154252; -.
DR PharmGKB; PA134913637; -.
DR VEuPathDB; HostDB:ENSG00000154252; -.
DR eggNOG; ENOG502QSHR; Eukaryota.
DR GeneTree; ENSGT00950000182923; -.
DR HOGENOM; CLU_040616_1_1_1; -.
DR InParanoid; Q9H3Q3; -.
DR OMA; ELQYMSY; -.
DR OrthoDB; 1385827at2759; -.
DR PhylomeDB; Q9H3Q3; -.
DR TreeFam; TF314802; -.
DR PathwayCommons; Q9H3Q3; -.
DR SignaLink; Q9H3Q3; -.
DR UniPathway; UPA00353; -.
DR BioGRID-ORCS; 64090; 10 hits in 1067 CRISPR screens.
DR ChiTaRS; GAL3ST2; human.
DR GeneWiki; GAL3ST2; -.
DR GenomeRNAi; 64090; -.
DR Pharos; Q9H3Q3; Tdark.
DR PRO; PR:Q9H3Q3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H3Q3; protein.
DR Bgee; ENSG00000154252; Expressed in olfactory segment of nasal mucosa and 69 other tissues.
DR Genevisible; Q9H3Q3; HS.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR GO; GO:0050694; F:galactose 3-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0001733; F:galactosylceramide sulfotransferase activity; IEA:InterPro.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IEA:InterPro.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR009729; Gal-3-0_sulfotransfrase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR14647; PTHR14647; 1.
DR Pfam; PF06990; Gal-3-0_sulfotr; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..398
FT /note="Galactose-3-O-sulfotransferase 2"
FT /id="PRO_0000085203"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 4
FT /note="M -> L (in dbSNP:rs12469459)"
FT /evidence="ECO:0000269|PubMed:11029462,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_047060"
SQ SEQUENCE 398 AA; 46110 MW; 900FF26B515E82D5 CRC64;
MMSMLGGLQR YFRVILLLLL ALTLLLLAGF LHSDLELDTP LFGGQAEGPP VTNIMFLKTH
KTASSTVLNI LYRFAETHNL SVALPAGSRV HLGYPWLFLA RYVEGVGSQQ RFNIMCNHLR
FNLPQVQKVM PNDTFYFSIL RNPVFQLESS FIYYKTYAPA FRGAPSLDAF LASPRTFYND
SRHLRNVYAK NNMWFDFGFD PNAQCEEGYV RARIAEVERR FRLVLIAEHL DESLVLLRRR
LRWALDDVVA FRLNSRSARS VARLSPETRE RARSWCALDW RLYEHFNRTL WAQLRAELGP
RRLRGEVERL RARRRELASL CLQDGGALKN HTQIRDPRLR PYQSGKADIL GYNLRPGLDN
QTLGVCQRLV MPELQYMARL YALQFPEKPL KNIPFLGA
