H6ST2_HUMAN
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 03-AUG-2022, entry version 152.
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; 133.
DR IntAct; Q96MM7; 8.
DR STRING; 9606.ENSP00000429473; -.
DR GlyGen; Q96MM7; 9 sites, 1 O-linked glycan (1 site).
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 PeptideAtlas; Q96MM7; -.
DR PRIDE; 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; 59 antibodies from 19 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 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; 1167623at2759; -.
DR PhylomeDB; Q96MM7; -.
DR TreeFam; TF312835; -.
DR PathwayCommons; Q96MM7; -.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR SignaLink; Q96MM7; -.
DR BioGRID-ORCS; 90161; 12 hits in 695 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 160 other tissues.
DR ExpressionAtlas; Q96MM7; baseline and differential.
DR Genevisible; Q96MM7; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:Reactome.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12812; PTHR12812; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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; unknown pathological
FT significance; reduced sulfotransferase activity; no effect
FT on protein levels; 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
