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   27-MAR-2024, entry version 148.
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   GlyCosmos; Q9H3Q3; 6 sites, No reported glycans.
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; 9606-ENSP00000192314; -.
DR   PeptideAtlas; Q9H3Q3; -.
DR   ProteomicsDB; 80740; -.
DR   Antibodypedia; 53483; 23 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   AGR; HGNC:24869; -.
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; MFRFAER; -.
DR   OrthoDB; 3032344at2759; -.
DR   PhylomeDB; Q9H3Q3; -.
DR   TreeFam; TF314802; -.
DR   PathwayCommons; Q9H3Q3; -.
DR   SignaLink; Q9H3Q3; -.
DR   UniPathway; UPA00353; -.
DR   BioGRID-ORCS; 64090; 13 hits in 1146 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 cell types or tissues.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR009729; Gal-3-0_sulfotransfrase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR14647; GALACTOSE-3-O-SULFOTRANSFERASE; 1.
DR   PANTHER; PTHR14647:SF55; GALACTOSE-3-O-SULFOTRANSFERASE 2; 1.
DR   Pfam; PF06990; Gal-3-0_sulfotr; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   Genevisible; Q9H3Q3; HS.
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
//