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 27-MAR-2024, entry version 211. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 90. DR IntAct; P43304; 30. DR MINT; P43304; -. DR STRING; 9606.ENSP00000308610; -. DR ChEMBL; CHEMBL3391681; -. DR SwissLipids; SLP:000000147; -. DR GlyCosmos; P43304; 2 sites, 1 glycan. 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 EPD; P43304; -. DR jPOST; P43304; -. DR MassIVE; P43304; -. DR MaxQB; P43304; -. DR PaxDb; 9606-ENSP00000308610; -. DR PeptideAtlas; P43304; -. DR ProteomicsDB; 55607; -. [P43304-1] DR ProteomicsDB; 55608; -. [P43304-2] DR Pumba; P43304; -. DR Antibodypedia; 2370; 321 antibodies from 30 providers. DR DNASU; 2820; -. DR Ensembl; ENST00000310454.10; ENSP00000308610.5; ENSG00000115159.17. [P43304-1] DR Ensembl; ENST00000409674.5; ENSP00000386425.1; ENSG00000115159.17. [P43304-1] DR Ensembl; ENST00000409861.5; ENSP00000386626.1; ENSG00000115159.17. [P43304-1] DR Ensembl; ENST00000438166.7; ENSP00000409708.2; ENSG00000115159.17. [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 AGR; HGNC:4456; -. 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; PHIVKPM; -. DR OrthoDB; 989271at2759; -. DR PhylomeDB; P43304; -. DR TreeFam; TF300359; -. DR BioCyc; MetaCyc:HS03841-MONOMER; -. 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 1165 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 187 other cell types or tissues. DR ExpressionAtlas; P43304; baseline and differential. 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; IEA:InterPro. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IDA:UniProtKB. 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; Alpha-glycerophosphate oxidase, cap domain; 1. DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 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; EF-hand; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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. DR UCD-2DPAGE; P43304; -. DR Genevisible; P43304; HS. 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 uncertain 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 uncertain 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 uncertain 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 //