GPDM_HUMAN
ID GPDM_HUMAN Reviewed; 727 AA.
AC P43304; A8K4V0; B3KSA9; Q59FR1; Q9HAP9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial {ECO:0000305};
DE Short=GPD-M;
DE Short=GPDH-M;
DE EC=1.1.5.3 {ECO:0000269|PubMed:9070847};
DE AltName: Full=mitohondrial glycerophosphate dehydrogenase gene {ECO:0000303|PubMed:9070847};
DE Short=mGDH {ECO:0000303|PubMed:9070847};
DE AltName: Full=mtGPD;
DE Flags: Precursor;
GN Name=GPD2 {ECO:0000312|HGNC:HGNC:4456};
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] (ISOFORM 1), AND VARIANTS HIS-264 AND HIS-525.
RX PubMed=7821823; DOI=10.1016/0378-1119(94)90469-3;
RA Lehn D.A., Brown L.J., Simonson G.D., Moran S.M., McDonald M.J.;
RT "The sequence of a human mitochondrial glycerol-3-phosphate dehydrogenase-
RT encoding cDNA.";
RL Gene 150:417-418(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-264.
RX PubMed=8549872; DOI=10.2337/diab.45.2.262;
RA Ferrer J., Aoki M., Behn P., Nestorowicz A., Riggs A., Permutt M.A.;
RT "Mitochondrial glycerol-3-phosphate dehydrogenase. Cloning of an
RT alternatively spliced human islet-cell cDNA, tissue distribution, physical
RT mapping, and identification of a polymorphic genetic marker.";
RL Diabetes 45:262-266(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-264.
RX PubMed=8682323; DOI=10.1016/0378-1119(96)00019-4;
RA Brown L.J., Stoffel M., Moran S.M., Fernald A.A., Lehn D.A., LeBeau M.M.,
RA MacDonald M.J.;
RT "Structural organization and mapping of the human mitochondrial glycerol
RT phosphate dehydrogenase-encoding gene and pseudogene.";
RL Gene 172:309-312(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS HIS-264 AND HIS-525.
RC TISSUE=Testis;
RA Yin L.L., Li J.M., Sha J.H.;
RT "A novel glycerol-3-phosphate dehydrogenase 3 from adult testis.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP HIS-264.
RC TISSUE=Testis, and Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-264.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-264.
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-408, AND VARIANT HIS-264.
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [10]
RP PROTEIN SEQUENCE OF 212-227 AND 558-572, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 340-348; 410-418; 526-538; 558-572 AND 715-722, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (JAN-2006) to UniProtKB.
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP VARIANTS SER-635; PRO-649 AND CYS-650, FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX PubMed=9070847; DOI=10.1006/bbrc.1997.6147;
RA Novials A., Vidal J., Franco C., Ribera F., Sener A., Malaisse W.J.,
RA Gomis R.;
RT "Mutation in the calcium-binding domain of the mitochondrial
RT glycerophosphate dehydrogenase gene in a family of diabetic subjects.";
RL Biochem. Biophys. Res. Commun. 231:570-572(1997).
CC -!- FUNCTION: Calcium-responsive mitochondrial glycerol-3-phosphate
CC dehydrogenase which seems to be a key component of the pancreatic beta-
CC cell glucose-sensing device. {ECO:0000269|PubMed:9070847}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000269|PubMed:9070847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18978;
CC Evidence={ECO:0000305|PubMed:9070847};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- ACTIVITY REGULATION: Calcium-binding enhance the activity of the
CC enzyme. {ECO:0000269|PubMed:9070847}.
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC route): step 1/1. {ECO:0000269|PubMed:9070847}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43304-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43304-2; Sequence=VSP_017134;
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92636.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U12424; AAA65701.1; -; mRNA.
DR EMBL; U36310; AAB60403.1; -; mRNA.
DR EMBL; U40367; AAC50556.1; -; Genomic_DNA.
DR EMBL; U40353; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; U40354; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; U40355; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; U40357; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; U40358; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; U40359; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; U40360; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; U40361; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; U40362; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; U40363; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; U40364; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; U40365; AAC50556.1; JOINED; Genomic_DNA.
DR EMBL; AF311325; AAG33851.1; -; mRNA.
DR EMBL; AK093198; BAG52671.1; -; mRNA.
DR EMBL; AK291065; BAF83754.1; -; mRNA.
DR EMBL; AK292817; BAF85506.1; -; mRNA.
DR EMBL; AB209399; BAD92636.1; ALT_INIT; mRNA.
DR EMBL; AC011308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471058; EAX11453.1; -; Genomic_DNA.
DR EMBL; U79250; AAB50200.1; -; mRNA.
DR CCDS; CCDS2202.1; -. [P43304-1]
DR PIR; G02093; G02093.
DR RefSeq; NP_000399.3; NM_000408.4. [P43304-1]
DR RefSeq; NP_001076581.2; NM_001083112.2. [P43304-1]
DR RefSeq; XP_005246526.1; XM_005246469.2. [P43304-1]
DR RefSeq; XP_011509279.1; XM_011510977.2. [P43304-1]
DR RefSeq; XP_016859319.1; XM_017003830.1. [P43304-1]
DR AlphaFoldDB; P43304; -.
DR SMR; P43304; -.
DR BioGRID; 109081; 78.
DR IntAct; P43304; 28.
DR MINT; P43304; -.
DR STRING; 9606.ENSP00000308610; -.
DR ChEMBL; CHEMBL3391681; -.
DR SwissLipids; SLP:000000147; -.
DR GlyGen; P43304; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P43304; -.
DR PhosphoSitePlus; P43304; -.
DR SwissPalm; P43304; -.
DR BioMuta; GPD2; -.
DR DMDM; 229462943; -.
DR REPRODUCTION-2DPAGE; IPI00017895; -.
DR UCD-2DPAGE; P43304; -.
DR EPD; P43304; -.
DR jPOST; P43304; -.
DR MassIVE; P43304; -.
DR MaxQB; P43304; -.
DR PaxDb; P43304; -.
DR PeptideAtlas; P43304; -.
DR PRIDE; P43304; -.
DR ProteomicsDB; 55607; -. [P43304-1]
DR ProteomicsDB; 55608; -. [P43304-2]
DR Antibodypedia; 2370; 282 antibodies from 30 providers.
DR DNASU; 2820; -.
DR Ensembl; ENST00000310454.10; ENSP00000308610.5; ENSG00000115159.16. [P43304-1]
DR Ensembl; ENST00000409125.8; ENSP00000386484.5; ENSG00000115159.16. [P43304-2]
DR Ensembl; ENST00000409674.5; ENSP00000386425.1; ENSG00000115159.16. [P43304-1]
DR Ensembl; ENST00000409861.5; ENSP00000386626.1; ENSG00000115159.16. [P43304-1]
DR Ensembl; ENST00000438166.7; ENSP00000409708.2; ENSG00000115159.16. [P43304-1]
DR GeneID; 2820; -.
DR KEGG; hsa:2820; -.
DR MANE-Select; ENST00000438166.7; ENSP00000409708.2; NM_000408.5; NP_000399.3.
DR UCSC; uc002tzd.5; human. [P43304-1]
DR CTD; 2820; -.
DR DisGeNET; 2820; -.
DR GeneCards; GPD2; -.
DR HGNC; HGNC:4456; GPD2.
DR HPA; ENSG00000115159; Low tissue specificity.
DR MalaCards; GPD2; -.
DR MIM; 138430; gene.
DR neXtProt; NX_P43304; -.
DR OpenTargets; ENSG00000115159; -.
DR PharmGKB; PA28837; -.
DR VEuPathDB; HostDB:ENSG00000115159; -.
DR eggNOG; KOG0042; Eukaryota.
DR GeneTree; ENSGT00390000001718; -.
DR HOGENOM; CLU_015740_3_1_1; -.
DR InParanoid; P43304; -.
DR OMA; CIVNAAG; -.
DR OrthoDB; 669193at2759; -.
DR PhylomeDB; P43304; -.
DR TreeFam; TF300359; -.
DR BioCyc; MetaCyc:HS03841-MON; -.
DR BRENDA; 1.1.5.3; 2681.
DR PathwayCommons; P43304; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR SignaLink; P43304; -.
DR UniPathway; UPA00618; UER00673.
DR BioGRID-ORCS; 2820; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; GPD2; human.
DR GenomeRNAi; 2820; -.
DR Pharos; P43304; Tbio.
DR PRO; PR:P43304; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P43304; protein.
DR Bgee; ENSG00000115159; Expressed in secondary oocyte and 185 other tissues.
DR ExpressionAtlas; P43304; baseline and differential.
DR Genevisible; P43304; HS.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; TAS:Reactome.
DR GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0006127; P:glycerophosphate shuttle; TAS:Reactome.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.8.870; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985; PTHR11985; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Direct protein sequencing; FAD;
KW Flavoprotein; Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 43..727
FT /note="Glycerol-3-phosphate dehydrogenase, mitochondrial"
FT /id="PRO_0000010429"
FT DOMAIN 623..658
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 659..694
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 71..99
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 672
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 674
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 676
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 678
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 683
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 601
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q64521"
FT VAR_SEQ 1..126
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_017134"
FT VARIANT 264
FT /note="R -> H (in dbSNP:rs2116665)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:7821823, ECO:0000269|PubMed:8549872,
FT ECO:0000269|PubMed:8682323, ECO:0000269|PubMed:9110174,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.6, ECO:0000269|Ref.8"
FT /id="VAR_049113"
FT VARIANT 453
FT /note="K -> Q (in dbSNP:rs35096779)"
FT /id="VAR_049114"
FT VARIANT 525
FT /note="R -> H (in dbSNP:rs1051916)"
FT /evidence="ECO:0000269|PubMed:7821823, ECO:0000269|Ref.4"
FT /id="VAR_025215"
FT VARIANT 635
FT /note="F -> S (found in patients with type 2 diabetes;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:9070847"
FT /id="VAR_083484"
FT VARIANT 649
FT /note="Q -> P (found in patients with type 2 diabetes;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:9070847"
FT /id="VAR_083485"
FT VARIANT 650
FT /note="R -> C (found in patients with type 2 diabetes;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:9070847"
FT /id="VAR_083486"
SQ SEQUENCE 727 AA; 80853 MW; 70D8B4E5CB4F2EFD CRC64;
MAFQKAVKGT ILVGGGALAT VLGLSQFAHY RRKQMNLAYV KAADCISEPV NREPPSREAQ
LLTLQNTSEF DILVIGGGAT GSGCALDAVT RGLKTALVER DDFSSGTSSR STKLIHGGVR
YLQKAIMKLD IEQYRMVKEA LHERANLLEI APHLSAPLPI MLPVYKWWQL PYYWVGIKLY
DLVAGSNCLK SSYVLSKSRA LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG
AATANYMEVV SLLKKTDPQT GKVRVSGARC KDVLTGQEFD VRAKCVINAT GPFTDSVRKM
DDKDAAAICQ PSAGVHIVMP GYYSPESMGL LDPATSDGRV IFFLPWQKMT IAGTTDTPTD
VTHHPIPSEE DINFILNEVR NYLSCDVEVR RGDVLAAWSG IRPLVTDPKS ADTQSISRNH
VVDISESGLI TIAGGKWTTY RSMAEDTINA AVKTHNLKAG PSRTVGLFLQ GGKDWSPTLY
IRLVQDYGLE SEVAQHLAAT YGDKAFEVAK MASVTGKRWP IVGVRLVSEF PYIEAEVKYG
IKEYACTAVD MISRRTRLAF LNVQAAEEAL PRIVELMGRE LNWDDYKKQE QLETARKFLY
YEMGYKSRSE QLTDRSEISL LPSDIDRYKK RFHKFDADQK GFITIVDVQR VLESINVQMD
ENTLHEILNE VDLNKNGQVE LNEFLQLMSA IQKGRVSGSR LAILMKTAEE NLDRRVPIPV
DRSCGGL
