ID G3ST4_HUMAN Reviewed; 486 AA. AC Q96RP7; A4D2A8; B4DWL8; D6W5U5; Q8N3P7; Q8WZ17; Q96E33; Q9HA78; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 160. DE RecName: Full=Galactose-3-O-sulfotransferase 4; DE Short=Gal3ST-4; DE EC=2.8.2.-; DE AltName: Full=Beta-galactose-3-O-sulfotransferase 4; DE AltName: Full=Gal-beta-1,3-GalNAc 3'-sulfotransferase; GN Name=GAL3ST4; ORFNames=PP6968; 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, AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=11333265; DOI=10.1074/jbc.m101558200; RA Seko A., Hara-Kuge S., Yamashita K.; RT "Molecular cloning and characterization of a novel human galactose 3-O- RT sulfotransferase that transfers sulfate to Galbeta1->3GalNAc residue in O- RT glycans."; RL J. Biol. Chem. 276:25697-25704(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-467. RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Mammary gland; 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 MRNA] (ISOFORM 1). RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-467. 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). CC -!- FUNCTION: Catalyzes the transfer of sulfate to beta-1,3-linked CC galactose residues in O-linked glycoproteins. Good substrates include CC asialofetuin, Gal-beta-1,3-GalNAc and Gal-beta-1,3 (GlcNAc- CC beta-1,6)GalNAc. {ECO:0000269|PubMed:11333265}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6-7.; CC -!- PATHWAY: Protein modification; carbohydrate sulfation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane CC {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96RP7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96RP7-2; Sequence=VSP_057006, VSP_057007; CC -!- TISSUE SPECIFICITY: Expressed mainly in placenta, thymus, testis, CC ovary, spinal cord, trachea and adrenal gland and at low levels in CC brain, lung, spleen, prostate, small intestine, colon, stomach thyroid CC and lymph node. {ECO:0000269|PubMed:11333265}. CC -!- SIMILARITY: Belongs to the galactose-3-O-sulfotransferase family. CC {ECO:0000305}. 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; AF316113; AAK73365.1; -; mRNA. DR EMBL; AF289575; AAL55759.1; -; mRNA. DR EMBL; AK022178; BAB13977.1; -; mRNA. DR EMBL; AK301591; BAG63080.1; -; mRNA. DR EMBL; AL833824; CAD38686.2; -; mRNA. DR EMBL; AC073842; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236956; EAL23847.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76575.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76577.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76579.1; -; Genomic_DNA. DR EMBL; BC012976; AAH12976.1; -; mRNA. DR CCDS; CCDS5688.1; -. [Q96RP7-1] DR RefSeq; NP_078913.3; NM_024637.4. [Q96RP7-1] DR AlphaFoldDB; Q96RP7; -. DR BioGRID; 122811; 3. DR IntAct; Q96RP7; 1. DR STRING; 9606.ENSP00000353142; -. DR GlyCosmos; Q96RP7; 1 site, No reported glycans. DR GlyGen; Q96RP7; 1 site. DR iPTMnet; Q96RP7; -. DR PhosphoSitePlus; Q96RP7; -. DR BioMuta; GAL3ST4; -. DR DMDM; 47116570; -. DR EPD; Q96RP7; -. DR jPOST; Q96RP7; -. DR MassIVE; Q96RP7; -. DR PaxDb; 9606-ENSP00000353142; -. DR PeptideAtlas; Q96RP7; -. DR ProteomicsDB; 5356; -. DR ProteomicsDB; 77998; -. [Q96RP7-1] DR Antibodypedia; 30607; 217 antibodies from 24 providers. DR DNASU; 79690; -. DR Ensembl; ENST00000360039.9; ENSP00000353142.4; ENSG00000197093.11. [Q96RP7-1] DR Ensembl; ENST00000413800.5; ENSP00000400451.1; ENSG00000197093.11. [Q96RP7-1] DR GeneID; 79690; -. DR KEGG; hsa:79690; -. DR MANE-Select; ENST00000360039.9; ENSP00000353142.4; NM_024637.5; NP_078913.3. DR UCSC; uc003utt.4; human. [Q96RP7-1] DR AGR; HGNC:24145; -. DR CTD; 79690; -. DR DisGeNET; 79690; -. DR GeneCards; GAL3ST4; -. DR HGNC; HGNC:24145; GAL3ST4. DR HPA; ENSG00000197093; Tissue enhanced (skin). DR MIM; 608235; gene. DR neXtProt; NX_Q96RP7; -. DR NIAGADS; ENSG00000197093; -. DR OpenTargets; ENSG00000197093; -. DR PharmGKB; PA134921067; -. DR VEuPathDB; HostDB:ENSG00000197093; -. DR eggNOG; ENOG502QSHR; Eukaryota. DR GeneTree; ENSGT00950000182923; -. DR HOGENOM; CLU_040616_1_2_1; -. DR InParanoid; Q96RP7; -. DR OMA; RNNQYAR; -. DR OrthoDB; 3032344at2759; -. DR PhylomeDB; Q96RP7; -. DR TreeFam; TF314802; -. DR PathwayCommons; Q96RP7; -. DR SignaLink; Q96RP7; -. DR UniPathway; UPA00353; -. DR BioGRID-ORCS; 79690; 18 hits in 1147 CRISPR screens. DR GeneWiki; GAL3ST4; -. DR GenomeRNAi; 79690; -. DR Pharos; Q96RP7; Tdark. DR PRO; PR:Q96RP7; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q96RP7; Protein. DR Bgee; ENSG00000197093; Expressed in parotid gland and 154 other cell types or tissues. DR ExpressionAtlas; Q96RP7; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; NAS:UniProtKB. DR GO; GO:0050694; F:galactose 3-O-sulfotransferase activity; IDA:UniProtKB. DR GO; GO:0001733; F:galactosylceramide sulfotransferase activity; IEA:InterPro. DR GO; GO:0050698; F:proteoglycan sulfotransferase activity; NAS:UniProtKB. DR GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB. DR GO; GO:0009247; P:glycolipid biosynthetic process; IEA:InterPro. DR GO; GO:0009101; P:glycoprotein biosynthetic process; IDA:MGI. DR GO; GO:0009100; P:glycoprotein metabolic process; NAS:UniProtKB. DR GO; GO:0009311; P:oligosaccharide metabolic process; NAS:UniProtKB. DR GO; GO:0030166; P:proteoglycan biosynthetic process; NAS:UniProtKB. DR GO; GO:0006790; P:sulfur compound metabolic process; NAS:UniProtKB. 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:SF57; GALACTOSE-3-O-SULFOTRANSFERASE 4; 1. DR Pfam; PF06990; Gal-3-0_sulfotr; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; Q96RP7; HS. PE 1: Evidence at protein level; KW Alternative splicing; Glycoprotein; Golgi apparatus; Membrane; KW Reference proteome; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..486 FT /note="Galactose-3-O-sulfotransferase 4" FT /id="PRO_0000085209" FT TOPO_DOM 1..18 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 19..39 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 40..486 FT /note="Lumenal" FT /evidence="ECO:0000255" FT CARBOHYD 374 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..80 FT /note="MGPLSPARTLRLWGPRSLGVALGVFMTIGFALQLLGGPFQRRLPGLQLRQPS FT APSLRPALPSCPPRQRLVFLKTHKSGSS -> MTPRSPTSAFRSCTAVSSCLCPSSWPW FT LHLSVTSPFPVPHGPSLSCQDAAALGTSEPGGGSGSLHDHWLCTPALGRALPE (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057006" FT VAR_SEQ 81..142 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057007" FT VARIANT 353 FT /note="R -> Q (in dbSNP:rs3800952)" FT /id="VAR_021989" FT VARIANT 467 FT /note="A -> V (in dbSNP:rs3823646)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:15498874" FT /id="VAR_033736" FT CONFLICT 137 FT /note="M -> L (in Ref. 3; BAB13977)" FT /evidence="ECO:0000305" FT CONFLICT 201..204 FT /note="RGDH -> VGTT (in Ref. 2; AAL55759)" FT /evidence="ECO:0000305" FT CONFLICT 441 FT /note="S -> R (in Ref. 3; BAB13977)" FT /evidence="ECO:0000305" SQ SEQUENCE 486 AA; 54166 MW; 2D731D16B191CC3C CRC64; MGPLSPARTL RLWGPRSLGV ALGVFMTIGF ALQLLGGPFQ RRLPGLQLRQ PSAPSLRPAL PSCPPRQRLV FLKTHKSGSS SVLSLLHRYG DQHGLRFALP ARYQFGYPKL FQASRVKGYR PQGGGTQLPF HILCHHMRFN LKEVLQVMPS DSFFFSIVRD PAALARSAFS YYKSTSSAFR KSPSLAAFLA NPRGFYRPGA RGDHYARNLL WFDFGLPFPP EKRAKRGNIH PPRDPNPPQL QVLPSGAGPR AQTLNPNALI HPVSTVTDHR SQISSPASFD LGSSSFIQWG LAWLDSVFDL VMVAEYFDES LVLLADALCW GLDDVVGFMH NAQAGHKQGL STVSNSGLTA EDRQLTARAR AWNNLDWALY VHFNRSLWAR IEKYGQGRLQ TAVAELRARR EALAKHCLVG GEASDPKYIT DRRFRPFQFG SAKVLGYILR SGLSPQDQEE CERLATPELQ YKDKLDAKQF PPTVSLPLKT SRPLSP //