ID   H6ST2_HUMAN             Reviewed;         605 AA.
AC   Q96MM7; B9WRT4; B9WRT5; E9PDY5; Q2TB13; Q4VC07; Q6PIC4; Q86SM9; Q8N3T4;
AC   Q8NBN4; Q96SJ4;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Heparan-sulfate 6-O-sulfotransferase 2 {ECO:0000305};
DE            Short=HS6ST-2;
DE            EC=2.8.2.- {ECO:0000269|PubMed:12492399};
GN   Name=HS6ST2 {ECO:0000312|HGNC:HGNC:19133}; ORFNames=PSEC0092;
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] (ISOFORMS 2 AND 3), FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RC   TISSUE=Brain;
RX   PubMed=12492399; DOI=10.1042/bj20021259;
RA   Habuchi H., Miyake G., Nogami K., Kuroiwa A., Matsuda Y.,
RA   Kusche-Gullberg M., Habuchi O., Tanaka M., Kimata K.;
RT   "Biosynthesis of heparan sulphate with diverse structures and functions:
RT   two alternatively spliced forms of human heparan sulphate 6-O-
RT   sulphotransferase-2 having different expression patterns and properties.";
RL   Biochem. J. 371:131-142(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Placenta;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 176-605 (ISOFORM 3).
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).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-605.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 465-605.
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   [7]
RP   INVOLVEMENT IN MRXSPM, FUNCTION, VARIANT MRXSPM ARG-306, AND
RP   CHARACTERIZATION OF VARIANT MRXSPM ARG-306.
RX   PubMed=30471091; DOI=10.1111/cge.13485;
RA   Paganini L., Hadi L.A., Chetta M., Rovina D., Fontana L., Colapietro P.,
RA   Bonaparte E., Pezzani L., Marchisio P., Tabano S.M., Costanza J.,
RA   Sirchia S.M., Riboni L., Milani D., Miozzo M.;
RT   "A HS6ST2 gene variant associated with X-linked intellectual disability and
RT   severe myopia in two male twins.";
RL   Clin. Genet. 95:368-374(2019).
CC   -!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate
CC       from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the
CC       N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
CC       {ECO:0000269|PubMed:12492399, ECO:0000269|PubMed:30471091}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC         sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) +
CC         adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:56604, Rhea:RHEA-
CC         COMP:9830, Rhea:RHEA-COMP:14621, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC         ChEBI:CHEBI:140604; Evidence={ECO:0000269|PubMed:12492399,
CC         ECO:0000269|PubMed:30471091};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56605;
CC         Evidence={ECO:0000269|PubMed:30471091};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q96MM7-1; Sequence=Displayed;
CC       Name=2; Synonyms=HS6ST-2S;
CC         IsoId=Q96MM7-2; Sequence=VSP_015846;
CC       Name=3; Synonyms=HS6ST-2;
CC         IsoId=Q96MM7-3; Sequence=VSP_015846, VSP_015847;
CC       Name=4;
CC         IsoId=Q96MM7-4; Sequence=VSP_015847;
CC   -!- DISEASE: Paganini-Miozzo syndrome (MRXSPM) [MIM:301025]: An X-linked,
CC       syndromic, neurodevelopmental disorder characterized by intellectual
CC       disability, global developmental delay, severe myopia, and mild facial
CC       dysmorphism. {ECO:0000269|PubMed:30471091}. Note=The disease may be
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 6 family. {ECO:0000305}.
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DR   EMBL; AB067776; BAC07183.1; -; mRNA.
DR   EMBL; AB067777; BAC07184.1; -; mRNA.
DR   EMBL; AK027720; BAB55322.1; -; mRNA.
DR   EMBL; AK056706; BAB71260.1; -; mRNA.
DR   EMBL; Z81365; CAX30811.1; -; Genomic_DNA.
DR   EMBL; Z86064; CAX30811.1; JOINED; Genomic_DNA.
DR   EMBL; Z81365; CAX30812.1; -; Genomic_DNA.
DR   EMBL; Z86064; CAX30812.1; JOINED; Genomic_DNA.
DR   EMBL; AL022309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL022159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z82205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z86064; CAI42774.1; -; Genomic_DNA.
DR   EMBL; Z81365; CAI42774.1; JOINED; Genomic_DNA.
DR   EMBL; Z86064; CAI42775.1; -; Genomic_DNA.
DR   EMBL; Z81365; CAI42775.1; JOINED; Genomic_DNA.
DR   EMBL; BC037325; AAH37325.1; -; mRNA.
DR   EMBL; BC094718; AAH94718.1; -; mRNA.
DR   EMBL; BC110620; AAI10621.1; -; mRNA.
DR   EMBL; BC110621; AAI10622.1; -; mRNA.
DR   EMBL; AK075402; BAC11597.1; -; mRNA.
DR   EMBL; AL831923; CAD38583.1; -; mRNA.
DR   CCDS; CCDS48169.1; -. [Q96MM7-1]
DR   CCDS; CCDS48170.1; -. [Q96MM7-4]
DR   RefSeq; NP_001070656.1; NM_001077188.1. [Q96MM7-4]
DR   RefSeq; NP_671704.3; NM_147175.3. [Q96MM7-1]
DR   RefSeq; XP_005262547.1; XM_005262490.3.
DR   RefSeq; XP_011529708.1; XM_011531406.1. [Q96MM7-3]
DR   RefSeq; XP_016885433.1; XM_017029944.1.
DR   RefSeq; XP_016885434.1; XM_017029945.1. [Q96MM7-3]
DR   AlphaFoldDB; Q96MM7; -.
DR   SMR; Q96MM7; -.
DR   BioGRID; 124671; 135.
DR   IntAct; Q96MM7; 8.
DR   STRING; 9606.ENSP00000429473; -.
DR   GlyCosmos; Q96MM7; 9 sites, 1 glycan.
DR   GlyGen; Q96MM7; 12 sites, 2 O-linked glycans (4 sites).
DR   iPTMnet; Q96MM7; -.
DR   PhosphoSitePlus; Q96MM7; -.
DR   BioMuta; HS6ST2; -.
DR   DMDM; 77416506; -.
DR   EPD; Q96MM7; -.
DR   jPOST; Q96MM7; -.
DR   MassIVE; Q96MM7; -.
DR   MaxQB; Q96MM7; -.
DR   PaxDb; 9606-ENSP00000429473; -.
DR   PeptideAtlas; Q96MM7; -.
DR   ProteomicsDB; 19773; -.
DR   ProteomicsDB; 77375; -. [Q96MM7-1]
DR   ProteomicsDB; 77376; -. [Q96MM7-2]
DR   ProteomicsDB; 77377; -. [Q96MM7-3]
DR   ABCD; Q96MM7; 7 sequenced antibodies.
DR   Antibodypedia; 30253; 94 antibodies from 20 providers.
DR   DNASU; 90161; -.
DR   Ensembl; ENST00000370833.7; ENSP00000359870.3; ENSG00000171004.19. [Q96MM7-4]
DR   Ensembl; ENST00000370836.6; ENSP00000359873.2; ENSG00000171004.19. [Q96MM7-1]
DR   Ensembl; ENST00000406696.5; ENSP00000384013.5; ENSG00000171004.19. [Q96MM7-3]
DR   Ensembl; ENST00000521489.5; ENSP00000429473.1; ENSG00000171004.19. [Q96MM7-4]
DR   Ensembl; ENST00000640529.2; ENSP00000491722.2; ENSG00000171004.19. [Q96MM7-3]
DR   GeneID; 90161; -.
DR   KEGG; hsa:90161; -.
DR   MANE-Select; ENST00000370833.7; ENSP00000359870.3; NM_001394073.1; NP_001381002.1. [Q96MM7-4]
DR   UCSC; uc011mvd.2; human. [Q96MM7-1]
DR   AGR; HGNC:19133; -.
DR   CTD; 90161; -.
DR   DisGeNET; 90161; -.
DR   GeneCards; HS6ST2; -.
DR   HGNC; HGNC:19133; HS6ST2.
DR   HPA; ENSG00000171004; Tissue enhanced (brain, kidney, ovary).
DR   MalaCards; HS6ST2; -.
DR   MIM; 300545; gene.
DR   MIM; 301025; phenotype.
DR   neXtProt; NX_Q96MM7; -.
DR   OpenTargets; ENSG00000171004; -.
DR   PharmGKB; PA134950831; -.
DR   VEuPathDB; HostDB:ENSG00000171004; -.
DR   eggNOG; KOG3955; Eukaryota.
DR   GeneTree; ENSGT00950000183071; -.
DR   HOGENOM; CLU_027877_1_0_1; -.
DR   InParanoid; Q96MM7; -.
DR   OMA; WWDLDEN; -.
DR   OrthoDB; 2896660at2759; -.
DR   PhylomeDB; Q96MM7; -.
DR   TreeFam; TF312835; -.
DR   PathwayCommons; Q96MM7; -.
DR   Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR   SignaLink; Q96MM7; -.
DR   BioGRID-ORCS; 90161; 14 hits in 767 CRISPR screens.
DR   ChiTaRS; HS6ST2; human.
DR   GenomeRNAi; 90161; -.
DR   Pharos; Q96MM7; Tbio.
DR   PRO; PR:Q96MM7; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q96MM7; Protein.
DR   Bgee; ENSG00000171004; Expressed in endothelial cell and 162 other cell types or tissues.
DR   ExpressionAtlas; Q96MM7; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IBA:GO_Central.
DR   GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005331; Sulfotransferase.
DR   PANTHER; PTHR12812; HEPARAN SULFATE 6-O-SULFOTRANSFERASE 3; 1.
DR   PANTHER; PTHR12812:SF6; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE 2; 1.
DR   Pfam; PF03567; Sulfotransfer_2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   Genevisible; Q96MM7; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disease variant; Glycoprotein;
KW   Intellectual disability; Membrane; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..605
FT                   /note="Heparan-sulfate 6-O-sulfotransferase 2"
FT                   /id="PRO_0000190805"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..605
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        290
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   BINDING         233..241
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   BINDING         263..264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   BINDING         280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   BINDING         325
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   BINDING         333
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   BINDING         337
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   BINDING         457..459
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   BINDING         463..464
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        460
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        544
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        556
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        564
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        589
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..146
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12492399,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015846"
FT   VAR_SEQ         315..316
FT                   /note="SR -> SRWRIFQILDAASKDKRGSPNTNAGANSPSSTKTRNTSKSGK (in
FT                   isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12492399,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015847"
FT   VARIANT         127
FT                   /note="K -> N (in dbSNP:rs7053397)"
FT                   /id="VAR_061828"
FT   VARIANT         306
FT                   /note="G -> R (in MRXSPM; uncertain significance; reduced
FT                   sulfotransferase activity; no effect on protein levels;
FT                   dbSNP:rs866919041)"
FT                   /evidence="ECO:0000269|PubMed:30471091"
FT                   /id="VAR_082055"
FT   CONFLICT        192
FT                   /note="D -> G (in Ref. 2; BAB71260)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        299
FT                   /note="C -> Y (in Ref. 4; AAH37325)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        426
FT                   /note="K -> R (in Ref. 5; BAC11597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        568
FT                   /note="S -> N (in Ref. 2; BAB71260)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        580
FT                   /note="Q -> R (in Ref. 5; BAC11597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        585
FT                   /note="E -> G (in Ref. 5; BAC11597)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   605 AA;  69130 MW;  10528AC424935B13 CRC64;
     MALPACAVRE FEPPRQPERG APVRTTCPRR HSRVEAELAA SRPGSVAASV RAGPPRGVSH
     GFHTRPLLDK PRKASSSLAG AACAPLFALL SRGRRRRMHV LRRRWDLGSL CRALLTRGLA
     ALGHSLKHVL GAIFSKIFGP MASVGNMDEK SNKLLLALVM LFLFAVIVLQ YVCPGTECQL
     LRLQAFSSPV PDPYRSEDES SARFVPRYNF TRGDLLRKVD FDIKGDDLIV FLHIQKTGGT
     TFGRHLVRNI QLEQPCECRV GQKKCTCHRP GKRETWLFSR FSTGWSCGLH ADWTELTSCV
     PSVVDGKRDA RLRPSRNFHY ITILRDPVSR YLSEWRHVQR GATWKASLHV CDGRPPTSEE
     LPSCYTGDDW SGCPLKEFMD CPYNLANNRQ VRMLSDLTLV GCYNLSVMPE KQRNKVLLES
     AKSNLKHMAF FGLTEFQRKT QYLFEKTFNM NFISPFTQYN TTRASSVEIN EEIQKRIEGL
     NFLDMELYSY AKDLFLQRYQ FMRQKEHQEA RRKRQEQRKF LKGRLLQTHF QSQGQGQSQN
     PNQNQSQNPN PNANQNLTQN LMQNLTQSLS QKENRESPKQ NSGKEQNDNT SNGTNDYIGS
     VEKWR
//