CHSTA_HUMAN
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 03-AUG-2022, entry version 152.
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, 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, confering 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=0.210 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) (GlcUA-3-
CC E2) {ECO:0000269|PubMed:23269668};
CC KM=1.518 mM for N-acetyllactosamine 3-O-(beta-D-glucuronate) (GlcUA-
CC 3-LacNAc) {ECO:0000269|PubMed:23269668};
CC Vmax=3194 pmol/min/mg enzyme toward dehydroepiandrosterone 3-O-(beta-
CC D-glucuronate) (GlcUA-3-DHEA) {ECO:0000269|PubMed:23269668};
CC Vmax=3858 pmol/min/mg enzyme toward 17beta-estradiol 3-O-(beta-D-
CC glucuronate) (GlcUA-3-E2) {ECO:0000269|PubMed:23269668};
CC Vmax=1723 pmol/min/mg enzyme toward N-acetyllactosamine 3-O-(beta-D-
CC glucuronate) (GlcUA-3-LacNAc) {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}.
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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 GlyGen; O43529; 3 sites.
DR iPTMnet; O43529; -.
DR PhosphoSitePlus; O43529; -.
DR BioMuta; CHST10; -.
DR EPD; O43529; -.
DR MassIVE; O43529; -.
DR PaxDb; O43529; -.
DR PeptideAtlas; O43529; -.
DR PRIDE; O43529; -.
DR ProteomicsDB; 49037; -.
DR Antibodypedia; 2360; 204 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 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; NVCREDT; -.
DR OrthoDB; 1330889at2759; -.
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 1074 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 153 other tissues.
DR ExpressionAtlas; O43529; baseline and differential.
DR Genevisible; O43529; HS.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR12137; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
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
