ASPH_MOUSE
ID ASPH_MOUSE Reviewed; 741 AA.
AC Q8BSY0; Q6P8S1; Q9EPA6; Q9EQ64;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Aspartyl/asparaginyl beta-hydroxylase;
DE EC=1.14.11.16 {ECO:0000269|PubMed:11773073};
DE AltName: Full=Aspartate beta-hydroxylase;
DE Short=ASP beta-hydroxylase;
DE AltName: Full=Peptide-aspartate beta-dioxygenase;
GN Name=Asph; Synonyms=Bah;
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 2), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Heart muscle;
RX PubMed=8530521; DOI=10.1074/jbc.270.51.30787;
RA Jones L.R., Zhang L., Sanborn K., Jorgensen A.O., Kelley J.;
RT "Purification, primary structure, and immunological characterization of the
RT 26-kDa calsequestrin binding protein (junctin) from cardiac junctional
RT sarcoplasmic reticulum.";
RL J. Biol. Chem. 270:30787-30796(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=10956665; DOI=10.1074/jbc.m006753200;
RA Dinchuk J.E., Henderson N.L., Burn T.C., Huber R., Ho S.P., Link J.,
RA O'Neil K.T., Focht R.J., Scully M.S., Hollis J.M., Hollis G.F.,
RA Friedman P.A.;
RT "Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform
RT of Asph missing the catalytic domain share exons with junctin.";
RL J. Biol. Chem. 275:39543-39554(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Heart;
RA Hong C., Kim D.H.;
RT "Mouse junctin-1 mRNA.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=11773073; DOI=10.1074/jbc.m110389200;
RA Dinchuk J.E., Focht R.J., Kelley J.A., Henderson N.L., Zolotarjova N.I.,
RA Wynn R., Neff N.T., Link J., Huber R.M., Burn T.C., Rupar M.J.,
RA Cunningham M.R., Selling B.H., Ma J., Stern A.A., Hollis G.F., Stein R.B.,
RA Friedman P.A.;
RT "Absence of post-translational aspartyl beta-hydroxylation of epidermal
RT growth factor domains in mice leads to developmental defects and an
RT increased incidence of intestinal neoplasia.";
RL J. Biol. Chem. 277:12970-12977(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=22768324; DOI=10.1371/journal.pone.0039962;
RA Boncompagni S., Thomas M., Lopez J.R., Allen P.D., Yuan Q., Kranias E.G.,
RA Franzini-Armstrong C., Perez C.F.;
RT "Triadin/junctin double null mouse reveals a differential role for triadin
RT and junctin in anchoring CASQ to the jSR and regulating Ca(2+)
RT homeostasis.";
RL PLoS ONE 7:E39962-E39962(2012).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=24768550; DOI=10.1016/j.ajhg.2014.04.002;
RA Patel N., Khan A.O., Mansour A., Mohamed J.Y., Al-Assiri A., Haddad R.,
RA Jia X., Xiong Y., Megarbane A., Traboulsi E.I., Alkuraya F.S.;
RT "Mutations in ASPH cause facial dysmorphism, lens dislocation, anterior-
RT segment abnormalities, and spontaneous filtering blebs, or Traboulsi
RT syndrome.";
RL Am. J. Hum. Genet. 94:755-759(2014).
CC -!- FUNCTION: [Isoform 1]: Specifically hydroxylates an Asp or Asn residue
CC in certain epidermal growth factor-like (EGF) domains of a number of
CC proteins. {ECO:0000269|PubMed:11773073}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartyl-[protein] + O2 = 3-hydroxy-L-
CC aspartyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:11508,
CC Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:14951, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17427,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:30031; EC=1.14.11.16;
CC Evidence={ECO:0000269|PubMed:11773073};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q12797};
CC -!- SUBUNIT: Monomer. Isoform 2 interacts with CASQ2.
CC {ECO:0000250|UniProtKB:Q12797, ECO:0000250|UniProtKB:Q28056}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q28056}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q28056}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8530521}; Single-pass type II membrane protein
CC {ECO:0000303|PubMed:8530521}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BSY0-1; Sequence=Displayed;
CC Name=2; Synonyms=Junctin;
CC IsoId=Q8BSY0-2; Sequence=VSP_056792, VSP_056793, VSP_056794;
CC Name=3;
CC IsoId=Q8BSY0-3; Sequence=VSP_060973, VSP_060974, VSP_060975;
CC -!- TISSUE SPECIFICITY: Isoform 1 is detected in heart, liver and ovary (at
CC protein level). Detected in heart ventricle. Isoform 1 is widely
CC expressed. Isoform 2 is detected in heart and skeletal muscle.
CC {ECO:0000269|PubMed:10956665, ECO:0000269|PubMed:11773073,
CC ECO:0000269|PubMed:8530521}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in the snout, limbs and eye of
CC 11.5 dpc and 12 dpc. Strong localization of the protein in the lens of
CC the developing eye at all three stages. {ECO:0000269|PubMed:24768550}.
CC -!- DISRUPTION PHENOTYPE: Selective disruption of isoform 1 abolishes liver
CC aspartyl beta-hydroxylase activity, but does not affect the expression
CC of isoform 2. Mice lacking isoform 1 have normal blood chemistry, do
CC not present blood coagulation defects and appear more or less normal,
CC except for shorter snouts, mild defects of the palate ridges,
CC syndactily due to fusion of soft tissues and reduced litter size from
CC mutant females, while male fertility appears normal. Mice lacking
CC isoform 2 show no visible phenotype. {ECO:0000269|PubMed:11773073,
CC ECO:0000269|PubMed:22768324}.
CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC family. {ECO:0000305}.
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DR EMBL; AF221854; AAK00614.1; -; mRNA.
DR EMBL; AF289486; AAG40808.1; -; mRNA.
DR EMBL; AF289487; AAG40809.1; -; mRNA.
DR EMBL; AF289490; AAG40812.1; -; mRNA.
DR EMBL; AF223413; AAN87549.1; -; mRNA.
DR EMBL; AK030293; BAC26882.1; -; mRNA.
DR EMBL; AL671970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL773548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC061098; AAH61098.1; -; mRNA.
DR EMBL; BC128299; AAI28300.1; -; mRNA.
DR EMBL; BC152365; AAI52366.1; -; mRNA.
DR CCDS; CCDS17959.1; -. [Q8BSY0-2]
DR CCDS; CCDS38690.1; -. [Q8BSY0-1]
DR CCDS; CCDS51118.1; -. [Q8BSY0-3]
DR RefSeq; NP_001171321.1; NM_001177850.1.
DR RefSeq; NP_001171323.1; NM_001177852.1.
DR RefSeq; NP_001171324.1; NM_001177853.1.
DR RefSeq; NP_001171325.1; NM_001177854.1.
DR RefSeq; NP_001171326.1; NM_001177855.1.
DR RefSeq; NP_001171327.1; NM_001177856.1. [Q8BSY0-3]
DR RefSeq; NP_001277296.1; NM_001290367.1.
DR RefSeq; NP_075553.2; NM_023066.3. [Q8BSY0-1]
DR AlphaFoldDB; Q8BSY0; -.
DR SMR; Q8BSY0; -.
DR BioGRID; 211167; 10.
DR IntAct; Q8BSY0; 5.
DR STRING; 10090.ENSMUSP00000077273; -.
DR GlyConnect; 2136; 6 N-Linked glycans (2 sites). [Q8BSY0-3]
DR GlyGen; Q8BSY0; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8BSY0; -.
DR PhosphoSitePlus; Q8BSY0; -.
DR SwissPalm; Q8BSY0; -.
DR EPD; Q8BSY0; -.
DR jPOST; Q8BSY0; -.
DR MaxQB; Q8BSY0; -.
DR PaxDb; Q8BSY0; -.
DR PRIDE; Q8BSY0; -.
DR ProteomicsDB; 283188; -. [Q8BSY0-1]
DR ProteomicsDB; 283189; -. [Q8BSY0-2]
DR ProteomicsDB; 308643; -.
DR Antibodypedia; 24707; 325 antibodies from 30 providers.
DR DNASU; 65973; -.
DR Ensembl; ENSMUST00000078139; ENSMUSP00000077273; ENSMUSG00000028207. [Q8BSY0-1]
DR Ensembl; ENSMUST00000146441; ENSMUSP00000116899; ENSMUSG00000028207. [Q8BSY0-3]
DR GeneID; 65973; -.
DR KEGG; mmu:65973; -.
DR UCSC; uc008ryf.2; mouse. [Q8BSY0-1]
DR UCSC; uc008ryo.3; mouse.
DR CTD; 444; -.
DR MGI; MGI:1914186; Asph.
DR VEuPathDB; HostDB:ENSMUSG00000028207; -.
DR eggNOG; KOG3696; Eukaryota.
DR GeneTree; ENSGT00940000156304; -.
DR HOGENOM; CLU_106984_2_0_1; -.
DR InParanoid; Q8BSY0; -.
DR OMA; YTELVKX; -.
DR OrthoDB; 1324479at2759; -.
DR PhylomeDB; Q8BSY0; -.
DR TreeFam; TF312799; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR BioGRID-ORCS; 65973; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Asph; mouse.
DR PRO; PR:Q8BSY0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BSY0; protein.
DR Bgee; ENSMUSG00000028207; Expressed in vastus lateralis and 248 other tissues.
DR ExpressionAtlas; Q8BSY0; baseline and differential.
DR Genevisible; Q8BSY0; MM.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0062101; F:peptidyl-aspartic acid 3-dioxygenase activity; ISS:MGI.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0032237; P:activation of store-operated calcium channel activity; ISO:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0042264; P:peptidyl-aspartic acid hydroxylation; IDA:MGI.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISO:MGI.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0031585; P:regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISO:MGI.
DR GO; GO:1901879; P:regulation of protein depolymerization; IDA:BHF-UCL.
DR GO; GO:0031647; P:regulation of protein stability; IDA:BHF-UCL.
DR GO; GO:0033198; P:response to ATP; ISO:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR007943; Asp-B-hydro/Triadin_dom.
DR InterPro; IPR007803; Asp/Arg/Pro-Hydrxlase.
DR InterPro; IPR039038; ASPH.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12366; PTHR12366; 1.
DR Pfam; PF05279; Asp-B-Hydro_N; 1.
DR Pfam; PF05118; Asp_Arg_Hydrox; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Dioxygenase; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat;
KW Sarcoplasmic reticulum; Signal-anchor; TPR repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..741
FT /note="Aspartyl/asparaginyl beta-hydroxylase"
FT /id="PRO_0000254161"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..741
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 324..357
FT /note="TPR 1"
FT REPEAT 365..398
FT /note="TPR 2"
FT REPEAT 437..470
FT /note="TPR 3"
FT REPEAT 472..504
FT /note="TPR 4"
FT REPEAT 508..540
FT /note="TPR 5"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 608
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 651
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 662
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 671..673
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 708
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 718
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 624..631
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT VAR_SEQ 1..43
FT /note="MAPRKNAKGGGGNSSSSGSGSGSGSGSPSTGSSGSSSSPGARR -> MAEDK
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056792"
FT VAR_SEQ 93
FT /note="L -> LAKAKDFRYNLSEVLQ (in isoform 3)"
FT /id="VSP_060973"
FT VAR_SEQ 117..245
FT /note="GLKERSPSERTFPPEEEAETHAELEEQAPEGADIQNVEDEVKEQIQSLLQES
FT VHTDHDLEADGLAGEPQPEVEDFLTVTDSDDRFEDLEPGTVHEEIEDTYHVEDTASQNH
FT PNDMEEMTNEQENSDPSE -> EGPGGLAKRKTKAKAKEPIKEELKKERGKAVPSKNEE
FT RRQGKKEQEDRGKGRKKPDSDTSQKASAAGKRDRDKEKASSDKSSKSKESWKKAVETKA
FT VSSKVAARDKDRRGRSSSGHAHVSKENGQKRKN (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056793"
FT VAR_SEQ 119..197
FT /note="KERSPSERTFPPEEEAETHAELEEQAPEGADIQNVEDEVKEQIQSLLQESVH
FT TDHDLEADGLAGEPQPEVEDFLTVTDS -> TKDGSNENIDSLEEVLTILAEESSDWFY
FT GFLSFLYDIMTPFEMLEEEEEESETADGVDGTSQNEGVQGKTCVILDLHNQ (in
FT isoform 3)"
FT /id="VSP_060974"
FT VAR_SEQ 198..741
FT /note="Missing (in isoform 3)"
FT /id="VSP_060975"
FT VAR_SEQ 246..741
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056794"
FT CONFLICT 131..132
FT /note="Missing (in Ref. 2; AAG40808/AAG40809)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="A -> E (in Ref. 2; AAG40808/AAG40809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 83042 MW; 0660A6A5E34418C8 CRC64;
MAPRKNAKGG GGNSSSSGSG SGSGSGSPST GSSGSSSSPG ARREAKHGGH KNGRRGGISG
GSFFTWFMVI ALLGVWTSVA VVWFDLVDYE EVLGKLGVYD ADGDGDFDVD DAKVLLGLKE
RSPSERTFPP EEEAETHAEL EEQAPEGADI QNVEDEVKEQ IQSLLQESVH TDHDLEADGL
AGEPQPEVED FLTVTDSDDR FEDLEPGTVH EEIEDTYHVE DTASQNHPND MEEMTNEQEN
SDPSEAVTDA GVLLPHAEEV RHQDYDEPVY EPSEHEGVAI SDNTIDDSSI ISEEINVASV
EEQQDTPPVK KKKPKLLNKF DKTIKAELDA AEKLRKRGKI EEAVNAFEEL VRKYPQSPRA
RYGKAQCEDD LAEKQRSNEV LRRAIETYQE AADLPDAPTD LVKLSLKRRS ERQQFLGHMR
GSLLTLQRLV QLFPSDTTLK NDLGVGYLLL GDNDSAKKVY EEVLNVTPND GFAKVHYGFI
LKAQNKISES IPYLKEGIES GDPGTDDGRF YFHLGDAMQR VGNKEAYKWY ELGHKRGHFA
SVWQRSLYNV NGLKAQPWWT PRETGYTELV KSLERNWKLI RDEGLMVMDK AKGLFLPEDE
NLREKGDWSQ FTLWQQGRKN ENACKGAPKT CALLEKFSET TGCRRGQIKY SIMHPGTHVW
PHTGPTNCRL RMHLGLVIPK EGCKIRCANE TRTWEEGKVL IFDDSFEHEV WQDASSFRLI
FIVDVWHPEL TPQQRRSLPA I
