CHSTA_MOUSE
ID CHSTA_MOUSE Reviewed; 356 AA.
AC Q6PGK7; Q8BKU3; Q8BL08; Q8R2Y5; Q91Y40;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Carbohydrate sulfotransferase 10;
DE EC=2.8.2.- {ECO:0000250|UniProtKB:O43529};
DE AltName: Full=HNK-1 sulfotransferase;
DE Short=HNK-1ST;
DE Short=HNK1ST;
GN Name=Chst10 {ECO:0000303|PubMed:23269668, ECO:0000312|MGI:MGI:2138283};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Melanoma;
RA Spanjaard R.A., Zhao X.;
RT "Complete sequence of murine HNK-1 sulfotransferase.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
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 [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12358771; DOI=10.1046/j.1471-4159.2002.01066.x;
RA Chou D.K.H., Schachner M., Jungalwala F.B.;
RT "HNK-1 sulfotransferase null mice express glucuronyl glycoconjugates and
RT show normal cerebellar granule neuron migration in vivo and in vitro.";
RL J. Neurochem. 82:1239-1251(2002).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12213450; DOI=10.1006/mcne.2002.1142;
RA Senn C., Kutsche M., Saghatelyan A., Boesl M.R., Loehler J., Bartsch U.,
RA Morellini F., Schachner M.;
RT "Mice deficient for the HNK-1 sulfotransferase show alterations in synaptic
RT efficacy and spatial learning and memory.";
RL Mol. Cell. Neurosci. 20:712-729(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
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:12213450, PubMed:12358771). Sulfates terminal glucuronyl
CC residue of the laminin globular (LG)-domain binding epitope on
CC DAG1/alpha-dystroglycan and prevents further polymerization by LARGE1
CC glycosyltransferase. Likely defines the chain length of LG epitope,
CC confering binding specificity to extracellular matrix components (By
CC similarity). Plays a role in down-regulating the steroid hormones.
CC Sulfates glucuronidated estrogens and androgens with an impact in
CC hormone cycle and fertility. Has a preference for glucuronyl moiety at
CC the 3-hydroxyl group of a sterol ring rather than the 17-hydroxyl
CC group, showing high catalytic efficiency for 17beta-estradiol 3-O-
CC (beta-D-glucuronate) and dehydroepiandrosterone 3-O-(beta-D-
CC glucuronate) hormones (PubMed:23269668) (By similarity).
CC {ECO:0000250|UniProtKB:O43529, ECO:0000269|PubMed:12213450,
CC ECO:0000269|PubMed:12358771, ECO:0000269|PubMed:23269668}.
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68305;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68697;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68661;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68665;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68669;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68673;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68701;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68677;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68681;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68685;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68689;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68693;
CC Evidence={ECO:0000250|UniProtKB:O43529};
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:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68705;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:O43529}.
CC -!- PATHWAY: Protein modification; carbohydrate sulfation.
CC {ECO:0000250|UniProtKB:O43529}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O54702}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PGK7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PGK7-2; Sequence=VSP_012989, VSP_012990, VSP_012991;
CC -!- DISRUPTION PHENOTYPE: Mice are viable, fertile and show normal
CC cerebellar granule neuron migration. The anatomy of all major brain
CC areas are histologically normal. However, basal synaptic transmission
CC in pyramidal cells in the CA1 region of the hippocampus are increased
CC and long-term potentiation evoked by theta-burst stimulation are
CC reduced. Mice show an impaired long-term memory and a poorer spatial
CC learning when a short inter-trial interval is used (PubMed:12213450,
CC PubMed:12358771). Mutant female mice are subfertile, have extensive
CC growth of endometrial epithelium associated with increased 17-beta-
CC estradiol levels at pro-estrus phase and dysregulated hormonal cycle
CC (PubMed:23269668). {ECO:0000269|PubMed:12213450,
CC ECO:0000269|PubMed:12358771, ECO:0000269|PubMed:23269668}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC34375.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BC056956; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF360543; AAK52908.1; -; mRNA.
DR EMBL; AK046415; BAC32718.1; -; mRNA.
DR EMBL; AK047378; BAC33040.1; -; mRNA.
DR EMBL; AK050676; BAC34375.1; ALT_INIT; mRNA.
DR EMBL; BC026960; AAH26960.1; -; mRNA.
DR EMBL; BC056956; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS14901.1; -. [Q6PGK7-1]
DR RefSeq; NP_660124.2; NM_145142.2. [Q6PGK7-1]
DR RefSeq; XP_006496428.1; XM_006496365.3.
DR AlphaFoldDB; Q6PGK7; -.
DR STRING; 10090.ENSMUSP00000027249; -.
DR GlyGen; Q6PGK7; 3 sites.
DR PhosphoSitePlus; Q6PGK7; -.
DR MaxQB; Q6PGK7; -.
DR PaxDb; Q6PGK7; -.
DR PRIDE; Q6PGK7; -.
DR ProteomicsDB; 281677; -. [Q6PGK7-1]
DR ProteomicsDB; 281678; -. [Q6PGK7-2]
DR DNASU; 98388; -.
DR Ensembl; ENSMUST00000027249; ENSMUSP00000027249; ENSMUSG00000026080. [Q6PGK7-1]
DR Ensembl; ENSMUST00000194361; ENSMUSP00000141295; ENSMUSG00000026080. [Q6PGK7-1]
DR GeneID; 98388; -.
DR KEGG; mmu:98388; -.
DR UCSC; uc007ata.1; mouse. [Q6PGK7-2]
DR UCSC; uc011wjt.1; mouse. [Q6PGK7-1]
DR CTD; 9486; -.
DR MGI; MGI:2138283; Chst10.
DR eggNOG; KOG4651; Eukaryota.
DR GeneTree; ENSGT00940000157128; -.
DR InParanoid; Q6PGK7; -.
DR Reactome; R-MMU-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR UniPathway; UPA00353; -.
DR BioGRID-ORCS; 98388; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Chst10; mouse.
DR PRO; PR:Q6PGK7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6PGK7; protein.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016232; F:HNK-1 sulfotransferase activity; ISO:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; IMP:MGI.
DR GO; GO:0008209; P:androgen metabolic process; ISO:MGI.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0007616; P:long-term memory; IMP:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; Carbohydrate metabolism; Glycoprotein;
KW Golgi apparatus; Lipid metabolism; Membrane; Reference proteome;
KW Signal-anchor; Steroid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..356
FT /note="Carbohydrate sulfotransferase 10"
FT /id="PRO_0000189658"
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:0000250"
FT BINDING 189..197
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
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 VAR_SEQ 1..33
FT /note="MHHQWLLLAACFWVIFMFMVASKFITLTFKDPD -> MAKTLRDIK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012989"
FT VAR_SEQ 144..188
FT /note="AFSSIEEIPENVVHDHEKNGLPRLSSFSKIGIQKRLKTYFKFFIV -> MCG
FT VGGGGTSVMGEGLRLALKDGVASSEKTHNLSEGSLCCFPHSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012990"
FT VAR_SEQ 189..356
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012991"
FT CONFLICT 238
FT /note="E -> A (in Ref. 2; BAC34375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 42055 MW; 72A4D0BA9A93F879 CRC64;
MHHQWLLLAA CFWVIFMFMV ASKFITLTFK DPDGYSAKQE FVFLTTMPEA EKLRGEKHFP
EVPKPTGKML SDSRPDQPPV YLERLELIRN TCKEEALRNL SHTEVSKFVL DRIFVCDKHK
ILFCQTPKVG NTQWKKVLIV LNGAFSSIEE IPENVVHDHE KNGLPRLSSF SKIGIQKRLK
TYFKFFIVRD PFERLISAFK DKFVHNPRFE PWYRHEIAPG IIRKYRKNRT ETRGIQFEDF
VRYLGDPNRR WLDLQFGDHI IHWVTYVELC APCEIKYSVV GHHETLEADA PYILKEAGID
HLVSYPTIPP GITMYNRTKV EQYFLGISKR DIRRLYARFE GDFKLFGYQK PDFLLN
