ID CHSTA_HUMAN Reviewed; 356 AA. AC O43529; Q53T18; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Carbohydrate sulfotransferase 10; DE EC=2.8.2.- {ECO:0000269|PubMed:23269668, ECO:0000269|PubMed:32149355}; DE AltName: Full=HNK-1 sulfotransferase; DE Short=HNK-1ST; DE Short=HNK1ST {ECO:0000303|PubMed:32149355}; DE Short=HuHNK-1ST; GN Name=CHST10 {ECO:0000303|PubMed:23269668, GN ECO:0000312|HGNC:HGNC:19650}; 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, ENZYME ACTIVITY, AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=9478973; DOI=10.1074/jbc.273.9.5190; RA Ong E., Yeh J.-C., Ding Y., Hindsgaul O., Fukuda M.; RT "Expression cloning of a human sulfotransferase that directs the synthesis RT of the HNK-1 glycan on the neural cell adhesion molecule and glycolipids."; RL J. Biol. Chem. 273:5190-5195(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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=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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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]. RC TISSUE=Brain; 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 MUTAGENESIS OF LYS-128; ARG-189; ASP-190; PRO-191 AND SER-197. RX PubMed=10464296; DOI=10.1074/jbc.274.36.25608; RA Ong E., Yeh J.-C., Ding Y., Hindsgaul O., Pedersen L.C., Negishi M., RA Fukuda M.; RT "Structure and function of HNK-1 sulfotransferase. Identification of donor RT and acceptor binding sites by site-directed mutagenesis."; RL J. Biol. Chem. 274:25608-25612(1999). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RX PubMed=23269668; DOI=10.1074/jbc.m112.433474; RA Suzuki-Anekoji M., Suzuki A., Wu S.W., Angata K., Murai K.K., Sugihara K., RA Akama T.O., Khoo K.H., Nakayama J., Fukuda M.N., Fukuda M.; RT "In vivo regulation of steroid hormones by the Chst10 sulfotransferase in RT mouse."; RL J. Biol. Chem. 288:5007-5016(2013). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY. RX PubMed=32149355; DOI=10.1093/glycob/cwaa024; RA Sheikh M.O., Venzke D., Anderson M.E., Yoshida-Moriguchi T., Glushka J.N., RA Nairn A.V., Galizzi M., Moremen K.W., Campbell K.P., Wells L.; RT "HNK-1 sulfotransferase modulates alpha-dystroglycan glycosylation by 3-O- RT sulfation of glucuronic acid on matriglycan."; RL Glycobiology 30:817-829(2020). CC -!- FUNCTION: Catalyzes the transfer of sulfate from 3'-phosphoadenylyl CC sulfate (PAPS) to position 3 of terminal glucuronic acid of both CC protein- and lipid-linked oligosaccharides. Participates in CC biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA- CC (1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-lactosaminyl CC residue carried by many neural recognition molecules, which is involved CC in cell interactions during ontogenetic development and in synaptic CC plasticity in the adult. May be indirectly involved in synapse CC plasticity of the hippocampus, via its role in HNK-1 biosynthesis CC (PubMed:9478973). Sulfates terminal glucuronyl residue of the laminin CC globular (LG)-domain binding epitope on DAG1/alpha-dystroglycan and CC prevents further polymerization by LARGE1 glycosyltransferase. Likely CC defines the chain length of LG epitope, conferring binding specificity CC to extracellular matrix components (PubMed:32149355). Plays a role in CC down-regulating the steroid hormones. Sulfates glucuronidated estrogens CC and androgens with an impact in hormone cycle and fertility. Has a CC preference for glucuronyl moiety at the 3-hydroxyl group of a sterol CC ring rather than the 17-hydroxyl group, showing high catalytic CC efficiency for 17beta-estradiol 3-O-(beta-D-glucuronate) and CC dehydroepiandrosterone 3-O-(beta-D-glucuronate) hormones CC (PubMed:23269668). {ECO:0000269|PubMed:23269668, CC ECO:0000269|PubMed:32149355, ECO:0000269|PubMed:9478973}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-GlcA-(1->[3)-alpha-D- CC Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol- CC P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L- CC Thr-[protein] = 3-O-{O-3-S-beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)- CC beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D- CC GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] CC + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68304, CC Rhea:RHEA-COMP:17486, Rhea:RHEA-COMP:17487, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:177355, CC ChEBI:CHEBI:177363; Evidence={ECO:0000269|PubMed:32149355}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68305; CC Evidence={ECO:0000305|PubMed:32149355}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17beta-estradiol 3-O-(beta-D-glucuronate) + 3'-phosphoadenylyl CC sulfate = 17beta-estradiol 3-O-(3-sulfo-beta-D-glucuronate) + CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68696, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, CC ChEBI:CHEBI:136641, ChEBI:CHEBI:178093; CC Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68697; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17beta-estradiol 3-O-(beta-D-glucuronate) 17-sulfate + 3'- CC phosphoadenylyl sulfate = 17beta-estradiol 3-O-(3-sulfo-beta-D- CC glucuronate) 17-sulfate + adenosine 3',5'-bisphosphate + H(+); CC Xref=Rhea:RHEA:68660, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:178094, ChEBI:CHEBI:178095; CC Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68661; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17beta-estradiol 17-O-(beta-D-glucuronate) + 3'- CC phosphoadenylyl sulfate = 17beta-estradiol 17-O-(3-sulfo-beta-D- CC glucuronate) + adenosine 3',5'-bisphosphate + H(+); CC Xref=Rhea:RHEA:68664, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:82961, ChEBI:CHEBI:178096; CC Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68665; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- CATALYTIC ACTIVITY: CC Reaction=16alpha,17beta-estriol 3-O-(beta-D-glucuronate) + 3'- CC phosphoadenylyl sulfate = 16alpha,17beta-estriol 3-O-(3-sulfo-beta-D- CC glucuronate) + adenosine 3',5'-bisphosphate + H(+); CC Xref=Rhea:RHEA:68668, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:136649, ChEBI:CHEBI:178097; CC Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68669; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- CATALYTIC ACTIVITY: CC Reaction=16alpha,17beta-estriol 16-O-(beta-D-glucuronate) + 3'- CC phosphoadenylyl sulfate = 16alpha,17beta-estriol 16-O-(3-sulfo-beta- CC D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); CC Xref=Rhea:RHEA:68672, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:136650, ChEBI:CHEBI:178098; CC Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68673; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- CATALYTIC ACTIVITY: CC Reaction=16alpha,17beta-estriol 17-O-(beta-D-glucuronate) + 3'- CC phosphoadenylyl sulfate = 16alpha,17beta-estriol 17-O-(3-sulfo-beta- CC D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); CC Xref=Rhea:RHEA:68700, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:178099, ChEBI:CHEBI:178100; CC Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68701; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + estrone 3-O-(beta-D-glucuronate) CC = adenosine 3',5'-bisphosphate + estrone 3-O-(3-sulfo-beta-D- CC glucuronate) + H(+); Xref=Rhea:RHEA:68676, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136634, CC ChEBI:CHEBI:178101; Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68677; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + 3alpha,20alpha-dihydroxy-5beta- CC pregnane 3-O-(beta-D-glucuronate) = 3alpha,20alpha-dihydroxy-5beta- CC pregnane 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'- CC bisphosphate + H(+); Xref=Rhea:RHEA:68680, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178102, CC ChEBI:CHEBI:178103; Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68681; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + testosterone 17-O-(beta-D- CC glucuronate) = adenosine 3',5'-bisphosphate + H(+) + testosterone 17- CC O-(3-sulfo-beta-D-glucuronate); Xref=Rhea:RHEA:68684, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, CC ChEBI:CHEBI:136639, ChEBI:CHEBI:178104; CC Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68685; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + 3beta-androst-5-en-17-one 3-O- CC (beta-D-glucuronate) = 3beta-androst-5-en-17-one 3-O-(3-sulfo-beta-D- CC glucuronate) + adenosine 3',5'-bisphosphate + H(+); CC Xref=Rhea:RHEA:68688, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:178105, ChEBI:CHEBI:178106; CC Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68689; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + 3alpha,17alpha-dihydroxy-5beta- CC androstane-11-one-17beta-carboxylate 3-O-(beta-D-glucuronate) = CC 3alpha,17alpha-dihydroxy-5beta-androstane-11-one-17beta-carboxylate CC 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + CC H(+); Xref=Rhea:RHEA:68692, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:178107, ChEBI:CHEBI:178108; CC Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68693; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + 3alpha-hydroxyetiocholan-17-one CC 3-O-(beta-D-glucuronate) = 3alpha-hydroxyetiocholan-17-one 3-O-(3- CC sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); CC Xref=Rhea:RHEA:68704, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:178197, ChEBI:CHEBI:178198; CC Evidence={ECO:0000269|PubMed:23269668}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68705; CC Evidence={ECO:0000305|PubMed:23269668}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.21 mM for dehydroepiandrosterone 3-O-(beta-D-glucuronate) CC (GlcUA-3-DHEA) {ECO:0000269|PubMed:23269668}; CC KM=0.321 mM for 17beta-estradiol 3-O-(beta-D-glucuronate) CC (GlcUA-3-E2) {ECO:0000269|PubMed:23269668}; CC KM=1.518 mM for N-acetyllactosamine 3-O-(beta-D-glucuronate) CC (GlcUA-3-LacNAc) {ECO:0000269|PubMed:23269668}; CC Vmax=3194 pmol/min/mg enzyme toward dehydroepiandrosterone CC 3-O-(beta-D-glucuronate) (GlcUA-3-DHEA) CC {ECO:0000269|PubMed:23269668}; CC Vmax=3858 pmol/min/mg enzyme toward 17beta-estradiol CC 3-O-(beta-D-glucuronate) (GlcUA-3-E2) {ECO:0000269|PubMed:23269668}; CC Vmax=1723 pmol/min/mg enzyme toward N-acetyllactosamine CC 3-O-(beta-D-glucuronate) (GlcUA-3-LacNAc) CC {ECO:0000269|PubMed:23269668}; CC -!- PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:23269668}. CC -!- PATHWAY: Protein modification; carbohydrate sulfation. CC {ECO:0000269|PubMed:32149355}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000250|UniProtKB:O54702}; Single-pass type II membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: In fetal tissues, it is predominantly expressed in CC brain, and weakly expressed in lung, kidney and liver. In adult, it is CC highly expressed in brain, testis, ovary, expressed at intermediate CC level in heart, pancreas, skeletal muscle, spleen and thymus, and CC weakly expressed in other tissues. In brain, it is expressed at higher CC level in the frontal lobe. {ECO:0000269|PubMed:32149355, CC ECO:0000269|PubMed:9478973}. CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {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; AF033827; AAC04707.1; -; mRNA. DR EMBL; AF070594; AAC28651.1; -; mRNA. DR EMBL; AK313241; BAG36052.1; -; mRNA. DR EMBL; AC012493; AAX93044.1; -; Genomic_DNA. DR EMBL; CH471127; EAX01841.1; -; Genomic_DNA. DR EMBL; CH471127; EAX01842.1; -; Genomic_DNA. DR EMBL; CH471127; EAX01843.1; -; Genomic_DNA. DR EMBL; CH471127; EAX01844.1; -; Genomic_DNA. DR EMBL; BC010441; AAH10441.1; -; mRNA. DR CCDS; CCDS2047.1; -. DR RefSeq; NP_004845.1; NM_004854.4. DR RefSeq; XP_011510509.1; XM_011512207.1. DR RefSeq; XP_011510510.1; XM_011512208.1. DR RefSeq; XP_011510512.1; XM_011512210.1. DR RefSeq; XP_011510513.1; XM_011512211.1. DR RefSeq; XP_011510514.1; XM_011512212.1. DR RefSeq; XP_016860869.1; XM_017005380.1. DR RefSeq; XP_016860870.1; XM_017005381.1. DR RefSeq; XP_016860871.1; XM_017005382.1. DR RefSeq; XP_016860872.1; XM_017005383.1. DR AlphaFoldDB; O43529; -. DR BioGRID; 114868; 55. DR IntAct; O43529; 16. DR STRING; 9606.ENSP00000264249; -. DR GlyCosmos; O43529; 3 sites, No reported glycans. DR GlyGen; O43529; 5 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O43529; -. DR PhosphoSitePlus; O43529; -. DR BioMuta; CHST10; -. DR EPD; O43529; -. DR MassIVE; O43529; -. DR PaxDb; 9606-ENSP00000264249; -. DR PeptideAtlas; O43529; -. DR ProteomicsDB; 49037; -. DR Antibodypedia; 2360; 221 antibodies from 28 providers. DR DNASU; 9486; -. DR Ensembl; ENST00000264249.8; ENSP00000264249.3; ENSG00000115526.11. DR Ensembl; ENST00000409701.5; ENSP00000387309.1; ENSG00000115526.11. DR GeneID; 9486; -. DR KEGG; hsa:9486; -. DR MANE-Select; ENST00000264249.8; ENSP00000264249.3; NM_004854.5; NP_004845.1. DR UCSC; uc002tam.4; human. DR AGR; HGNC:19650; -. DR CTD; 9486; -. DR DisGeNET; 9486; -. DR GeneCards; CHST10; -. DR HGNC; HGNC:19650; CHST10. DR HPA; ENSG00000115526; Low tissue specificity. DR MIM; 606376; gene. DR neXtProt; NX_O43529; -. DR OpenTargets; ENSG00000115526; -. DR PharmGKB; PA134920179; -. DR VEuPathDB; HostDB:ENSG00000115526; -. DR eggNOG; KOG4651; Eukaryota. DR GeneTree; ENSGT00940000157128; -. DR HOGENOM; CLU_043398_2_0_1; -. DR InParanoid; O43529; -. DR OMA; HWPEEFQ; -. DR OrthoDB; 2907043at2759; -. DR PhylomeDB; O43529; -. DR TreeFam; TF325581; -. DR PathwayCommons; O43529; -. DR Reactome; R-HSA-975578; Reactions specific to the complex N-glycan synthesis pathway. DR SignaLink; O43529; -. DR UniPathway; UPA00353; -. DR BioGRID-ORCS; 9486; 11 hits in 1150 CRISPR screens. DR ChiTaRS; CHST10; human. DR GeneWiki; CHST10; -. DR GenomeRNAi; 9486; -. DR Pharos; O43529; Tbio. DR PRO; PR:O43529; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; O43529; Protein. DR Bgee; ENSG00000115526; Expressed in ventricular zone and 154 other cell types or tissues. DR ExpressionAtlas; O43529; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0016232; F:HNK-1 sulfotransferase activity; TAS:Reactome. DR GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB. DR GO; GO:0008209; P:androgen metabolic process; IDA:UniProtKB. DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB. DR GO; GO:0007612; P:learning; IEA:Ensembl. DR GO; GO:0007616; P:long-term memory; IEA:Ensembl. DR GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central. DR InterPro; IPR018011; Carb_sulfotrans_8-10. DR InterPro; IPR005331; Sulfotransferase. DR PANTHER; PTHR12137; CARBOHYDRATE SULFOTRANSFERASE; 1. DR PANTHER; PTHR12137:SF2; CARBOHYDRATE SULFOTRANSFERASE 10; 1. DR Pfam; PF03567; Sulfotransfer_2; 1. DR Genevisible; O43529; HS. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Glycoprotein; Golgi apparatus; Lipid metabolism; KW Membrane; Reference proteome; Signal-anchor; Steroid metabolism; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..356 FT /note="Carbohydrate sulfotransferase 10" FT /id="PRO_0000189657" FT TOPO_DOM 1..6 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 7..27 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 28..356 FT /note="Lumenal" FT /evidence="ECO:0000255" FT BINDING 127..133 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000305" FT BINDING 189..197 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000305" FT CARBOHYD 99 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 228 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 316 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 20 FT /note="V -> L (in dbSNP:rs35177621)" FT /id="VAR_033737" FT VARIANT 258 FT /note="D -> N (in dbSNP:rs3748932)" FT /id="VAR_021470" FT MUTAGEN 128 FT /note="K->A: Loss of function." FT /evidence="ECO:0000269|PubMed:10464296" FT MUTAGEN 128 FT /note="K->R: Induces a reduction in enzyme activity." FT /evidence="ECO:0000269|PubMed:10464296" FT MUTAGEN 189 FT /note="R->A,K: Loss of function." FT /evidence="ECO:0000269|PubMed:10464296" FT MUTAGEN 190 FT /note="D->A: Loss of function." FT /evidence="ECO:0000269|PubMed:10464296" FT MUTAGEN 190 FT /note="D->E: Induces a mild reduction in enzyme activity." FT /evidence="ECO:0000269|PubMed:10464296" FT MUTAGEN 191 FT /note="P->A,G: Loss of function." FT /evidence="ECO:0000269|PubMed:10464296" FT MUTAGEN 197 FT /note="S->A,T: Loss of function." FT /evidence="ECO:0000269|PubMed:10464296" SQ SEQUENCE 356 AA; 42207 MW; 0AE82883CCD8291A CRC64; MHHQWLLLAA CFWVIFMFMV ASKFITLTFK DPDVYSAKQE FLFLTTMPEV RKLPEEKHIP EELKPTGKEL PDSQLVQPLV YMERLELIRN VCRDDALKNL SHTPVSKFVL DRIFVCDKHK ILFCQTPKVG NTQWKKVLIV LNGAFSSIEE IPENVVHDHE KNGLPRLSSF SDAEIQKRLK TYFKFFIVRD PFERLISAFK DKFVHNPRFE PWYRHEIAPG IIRKYRRNRT ETRGIQFEDF VRYLGDPNHR WLDLQFGDHI IHWVTYVELC APCEIMYSVI GHHETLEDDA PYILKEAGID HLVSYPTIPP GITVYNRTKV EHYFLGISKR DIRRLYARFE GDFKLFGYQK PDFLLN //