ID   HS2ST_HUMAN             Reviewed;         356 AA.
AC   Q7LGA3; D3DT22; O75036; Q32NB5; Q8TAC5; Q9H441; Q9NUJ9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 171.
DE   RecName: Full=Heparan sulfate 2-O-sulfotransferase 1 {ECO:0000305};
DE            EC=2.8.2.- {ECO:0000250|UniProtKB:Q8R3H7};
DE   AltName: Full=2-O-sulfotransferase {ECO:0000250|UniProtKB:Q8R3H7};
DE            Short=2-OST {ECO:0000250|UniProtKB:Q8R3H7};
DE            Short=2OST {ECO:0000250|UniProtKB:Q76KB1};
DE   AltName: Full=HS 2-O-sulfotransferase {ECO:0000250|UniProtKB:Q8R3H7};
DE   AltName: Full=Heparan sulfate 2-sulfotransferase {ECO:0000250|UniProtKB:Q8R3H7};
GN   Name=HS2ST1 {ECO:0000312|HGNC:HGNC:5193}; Synonyms=HS2ST, KIAA0448;
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 {ECO:0000312|Proteomes:UP000005640};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Habuchi H.;
RT   "Human heparan sulfate 2-O-sulfotransferase.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA   Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA   Nomura N., Ohara O.;
RT   "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT   human brain.";
RL   DNA Res. 4:345-349(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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] (ISOFORM 3).
RC   TISSUE=Brain, Ovary, and Testis;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   INVOLVEMENT IN NFSRA, AND VARIANTS NFSRA TYR-165; SER-176 AND SER-189.
RX   PubMed=33159882; DOI=10.1016/j.ajhg.2020.10.007;
RA   Schneeberger P.E., von Elsner L., Barker E.L., Meinecke P., Marquardt I.,
RA   Alawi M., Steindl K., Joset P., Rauch A., Zwijnenburg P.J.G., Weiss M.M.,
RA   Merry C.L.R., Kutsche K.;
RT   "Bi-allelic pathogenic variants in HS2ST1 cause a syndrome characterized by
RT   developmental delay and corpus callosum, skeletal, and renal
RT   abnormalities.";
RL   Am. J. Hum. Genet. 107:1044-1061(2020).
CC   -!- FUNCTION: Catalyzes the transfer of a sulfo group from 3'-phospho-5'-
CC       adenylyl sulfate (PAPS) to the 2-OH position of iduronic acid (IdoA) or
CC       glucuronic acid (GlcA) within the heparan sulfate (HS) chain and
CC       participates in HS biosynthesis (By similarity). Required for
CC       metanephric development of kidney formation, suggesting that 2-O-
CC       sulfation within HS is essential for signaling between ureteric bud and
CC       metanephric mesenchyme (By similarity). {ECO:0000250|UniProtKB:Q76KB1,
CC       ECO:0000250|UniProtKB:Q8R3H7}.
CC   -!- SUBUNIT: Homotrimer (By similarity). Interacts with the C5-epimerase
CC       GLCE (By similarity). {ECO:0000250|UniProtKB:Q76KB1,
CC       ECO:0000250|UniProtKB:Q8R3H7}.
CC   -!- INTERACTION:
CC       Q7LGA3-3; O14908-2: GIPC1; NbExp=3; IntAct=EBI-25887463, EBI-25913156;
CC       Q7LGA3-3; Q92876: KLK6; NbExp=3; IntAct=EBI-25887463, EBI-2432309;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q8R3H7}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q8R3H7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q7LGA3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7LGA3-2; Sequence=VSP_014062, VSP_014064;
CC       Name=3;
CC         IsoId=Q7LGA3-3; Sequence=VSP_014063;
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O08889}.
CC   -!- DISEASE: Neurofacioskeletal syndrome with or without renal agenesis
CC       (NFSRA) [MIM:619194]: An autosomal recessive syndrome characterized by
CC       developmental delay and/or intellectual disability, corpus callosum
CC       agenesis or hypoplasia, flexion contractures, brachydactyly of hands
CC       and feet with broad fingertips and toes, and dysmorphic features such
CC       as coarse face, upslanted palpebral fissures, broad nasal tip and wide
CC       mouth. Some patients manifest unilateral or bilateral renal agenesis.
CC       {ECO:0000269|PubMed:33159882}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA32293.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB024568; BAA89250.1; -; mRNA.
DR   EMBL; AB007917; BAA32293.2; ALT_INIT; mRNA.
DR   EMBL; AK002179; BAA92125.1; -; mRNA.
DR   EMBL; AC093155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL121989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471097; EAW73171.1; -; Genomic_DNA.
DR   EMBL; CH471097; EAW73172.1; -; Genomic_DNA.
DR   EMBL; BC025384; AAH25384.1; -; mRNA.
DR   EMBL; BC025990; AAH25990.1; -; mRNA.
DR   EMBL; BC108735; AAI08736.1; -; mRNA.
DR   CCDS; CCDS44171.1; -. [Q7LGA3-3]
DR   CCDS; CCDS711.1; -. [Q7LGA3-1]
DR   RefSeq; NP_001127964.1; NM_001134492.2. [Q7LGA3-3]
DR   RefSeq; NP_036394.1; NM_012262.4. [Q7LGA3-1]
DR   AlphaFoldDB; Q7LGA3; -.
DR   SMR; Q7LGA3; -.
DR   BioGRID; 115011; 203.
DR   FunCoup; Q7LGA3; 2062.
DR   IntAct; Q7LGA3; 133.
DR   MINT; Q7LGA3; -.
DR   NDEx; IQUERY-CP-HS2ST1; 5 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000359581; -.
DR   GlyConnect; Q7LGA3; 3 N-Linked glycans (1 site).
DR   GlyCosmos; Q7LGA3; 2 sites, 3 glycans.
DR   GlyGen; Q7LGA3; 3 sites, 32 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q7LGA3; -.
DR   PhosphoSitePlus; Q7LGA3; -.
DR   SwissPalm; Q7LGA3; -.
DR   BioMuta; HS2ST1; -.
DR   DMDM; 68052326; -.
DR   jPOST; Q7LGA3; -.
DR   MassIVE; Q7LGA3; -.
DR   PaxDb; 9606-ENSP00000359581; -.
DR   PeptideAtlas; Q7LGA3; -.
DR   ProteomicsDB; 68865; -. [Q7LGA3-1]
DR   ProteomicsDB; 68866; -. [Q7LGA3-2]
DR   ProteomicsDB; 68867; -. [Q7LGA3-3]
DR   Pumba; Q7LGA3; -.
DR   Antibodypedia; 33591; 228 antibodies from 27 providers.
DR   DNASU; 9653; -.
DR   Ensembl; ENST00000370548.3; ENSP00000359579.1; ENSG00000267561.2. [Q7LGA3-2]
DR   Ensembl; ENST00000370550.10; ENSP00000359581.4; ENSG00000153936.18. [Q7LGA3-1]
DR   Ensembl; ENST00000370551.8; ENSP00000359582.3; ENSG00000153936.18. [Q7LGA3-3]
DR   GeneID; 9653; -.
DR   KEGG; hsa:9653; -.
DR   MANE-Select; ENST00000370550.10; ENSP00000359581.4; NM_012262.4; NP_036394.1.
DR   UCSC; uc001dmc.5; human. [Q7LGA3-1]
DR   AGR; HGNC:5193; -.
DR   ClinPGx; PA29466; -.
DR   CTD; 9653; -.
DR   DisGeNET; 9653; -.
DR   GeneCards; HS2ST1; -.
DR   HGNC; HGNC:5193; HS2ST1.
DR   HPA; ENSG00000153936; Low tissue specificity.
DR   MalaCards; HS2ST1; -.
DR   MIM; 604844; gene.
DR   MIM; 619194; phenotype.
DR   OpenTargets; ENSG00000153936; -.
DR   OpenTargets; ENSG00000267561; -.
DR   Orphanet; 528084; Non-specific syndromic intellectual disability.
DR   VEuPathDB; HostDB:ENSG00000153936; -.
DR   eggNOG; KOG3922; Eukaryota.
DR   GeneTree; ENSGT00530000063408; -.
DR   HOGENOM; CLU_045310_1_1_1; -.
DR   InParanoid; Q7LGA3; -.
DR   OMA; MALWRMM; -.
DR   OrthoDB; 10019582at2759; -.
DR   PAN-GO; Q7LGA3; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q7LGA3; -.
DR   BioCyc; MetaCyc:ENSG00000153936-MONOMER; -.
DR   BRENDA; 2.8.2.B6; 2681.
DR   PathwayCommons; Q7LGA3; -.
DR   Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR   SignaLink; Q7LGA3; -.
DR   Agora; ENSG00000153936; -.
DR   BioGRID-ORCS; 9653; 22 hits in 1170 CRISPR screens.
DR   ChiTaRS; HS2ST1; human.
DR   GeneWiki; HS2ST1; -.
DR   GenomeRNAi; 9653; -.
DR   Pharos; Q7LGA3; Tbio.
DR   PRO; PR:Q7LGA3; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q7LGA3; protein.
DR   Bgee; ENSG00000153936; Expressed in adrenal tissue and 194 other cell types or tissues.
DR   ExpressionAtlas; Q7LGA3; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0004394; F:heparan sulfate 2-sulfotransferase activity; ISS:UniProtKB.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IBA:GO_Central.
DR   FunFam; 3.40.50.300:FF:000534; Heparan sulfate 2-O-sulfotransferase 1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR007734; Heparan_SO4_2-O-STrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005331; Sulfotransferase.
DR   PANTHER; PTHR12129; HEPARAN SULFATE 2-O-SULFOTRANSFERASE; 1.
DR   PANTHER; PTHR12129:SF17; HEPARAN SULFATE 2-O-SULFOTRANSFERASE 1; 1.
DR   Pfam; PF03567; Sulfotransfer_2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Disease variant; Disulfide bond;
KW   Glycoprotein; Golgi apparatus; Intellectual disability; Membrane;
KW   Proteomics identification; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..356
FT                   /note="Heparan sulfate 2-O-sulfotransferase 1"
FT                   /id="PRO_0000207674"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..356
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   COILED          24..51
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000250|UniProtKB:A0A8C2LVE3"
FT   BINDING         83
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   BINDING         84
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   BINDING         85
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   BINDING         86
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   BINDING         87
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   BINDING         88
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   BINDING         164
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   BINDING         172
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   BINDING         279
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   BINDING         285
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   BINDING         290
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   BINDING         293
FT                   /ligand="adenosine 3',5'-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58343"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        201..209
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   DISULFID        222..228
FT                   /evidence="ECO:0000250|UniProtKB:Q76KB1"
FT   VAR_SEQ         1..41
FT                   /note="MGLLRIMMPPKLQLLAVVAFAVAMLFLENQIQKLEESRSKL -> MLFIKFI
FT                   HLEVFSMP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_014062"
FT   VAR_SEQ         230..356
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014063"
FT   VAR_SEQ         282..356
FT                   /note="GKKSHLRKTTEKKLPTKQTIAKLQQSDIWKMENEFYEFALEQFQFIRAHAVR
FT                   EKDGDLYILAQNFFYEKIYPKSN -> APDTATPSHRHGPICGSKSISSLLVKVSPVCK
FT                   DSHCLGKCSRNGLSAV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_014064"
FT   VARIANT         165
FT                   /note="D -> Y (in NFSRA; dbSNP:rs758990524)"
FT                   /evidence="ECO:0000269|PubMed:33159882"
FT                   /id="VAR_085252"
FT   VARIANT         176
FT                   /note="F -> S (in NFSRA; dbSNP:rs1651972168)"
FT                   /evidence="ECO:0000269|PubMed:33159882"
FT                   /id="VAR_085253"
FT   VARIANT         189
FT                   /note="R -> S (in NFSRA; dbSNP:rs1651973144)"
FT                   /evidence="ECO:0000269|PubMed:33159882"
FT                   /id="VAR_085254"
SQ   SEQUENCE   356 AA;  41881 MW;  2F5BBDFC7DF50F78 CRC64;
     MGLLRIMMPP KLQLLAVVAF AVAMLFLENQ IQKLEESRSK LERAIARHEV REIEQRHTMD
     GPRQDATLDE EEDMVIIYNR VPKTASTSFT NIAYDLCAKN KYHVLHINTT KNNPVMSLQD
     QVRFVKNITS WKEMKPGFYH GHVSYLDFAK FGVKKKPIYI NVIRDPIERL VSYYYFLRFG
     DDYRPGLRRR KQGDKKTFDE CVAEGGSDCA PEKLWLQIPF FCGHSSECWN VGSRWAMDQA
     KYNLINEYFL VGVTEELEDF IMLLEAALPR FFRGATELYR TGKKSHLRKT TEKKLPTKQT
     IAKLQQSDIW KMENEFYEFA LEQFQFIRAH AVREKDGDLY ILAQNFFYEK IYPKSN
//