ID F1NCA2_CHICK Unreviewed; 727 AA.
AC F1NCA2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=GPD2 {ECO:0000313|Ensembl:ENSGALP00010014255.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010014255.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010014255.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010014255.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003074}.
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:0000256|ARBA:ARBA00001590};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18978;
CC Evidence={ECO:0000256|ARBA:ARBA00001590};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation.
CC {ECO:0000256|ARBA:ARBA00004745}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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DR RefSeq; XP_015145680.1; XM_015290194.1.
DR RefSeq; XP_015145681.1; XM_015290195.1.
DR RefSeq; XP_015145683.1; XM_015290197.1.
DR RefSeq; XP_015145684.1; XM_015290198.1.
DR RefSeq; XP_015145685.1; XM_015290199.1.
DR AlphaFoldDB; F1NCA2; -.
DR SMR; F1NCA2; -.
DR STRING; 9031.ENSGALP00000067954; -.
DR PaxDb; 9031-ENSGALP00000020459; -.
DR Ensembl; ENSGALT00010025108.1; ENSGALP00010014255.1; ENSGALG00010010528.1.
DR GeneID; 424321; -.
DR KEGG; gga:424321; -.
DR CTD; 2820; -.
DR VEuPathDB; HostDB:geneid_424321; -.
DR GeneTree; ENSGT00390000001718; -.
DR InParanoid; F1NCA2; -.
DR OMA; PHIVKPM; -.
DR OrthoDB; 989271at2759; -.
DR Reactome; R-GGA-1483166; Synthesis of PA.
DR Reactome; R-GGA-163560; Triglyceride catabolism.
DR Proteomes; UP000000539; Chromosome 7.
DR Bgee; ENSGALG00000012543; Expressed in brain and 14 other cell types or tissues.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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.
PE 1: Evidence at protein level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1NCA2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
SQ SEQUENCE 727 AA; 80752 MW; 0DF69F2DAC3281D0 CRC64;
MAFQKAVKGT VLIGGGAIAT VFGLSQFSQY RNKHGSLVNV QAAEAVTVPI KNDFPTREEQ
ISTLKSTPEF DVLIIGGGAT GCGCALDAVT RGLKTALLER DDFSSGTSSR STKLIHGGVR
YLQKAIMKLD FEQYKMVKEA LQERANLLEI APHLSAPLPI MLPVYKWWQL PYYWIGIKLY
DLVAGSQCLK RSYVLSKSRA LEHFPMLRKD KLVGAIVYYD GQHNDARMNL AIALTAARYG
AATANYTEVL RLLKRTEPGS GKQRVCGARC RDVLTGQEFD VKAKCVINAT GPFTDSVRKM
DDQEVPNICQ PSAGVHIVMP GYYSPDNMGL LDPATSDGRV IFFLPWEKMT IAGTTDSPTD
VTSHPIPTEE DINFILSEVR NYLSVDVEVR RGDVLAAWSG IRPLVTDPNS KDTQSICRNH
VVAVSDSGLV TIAGGKWTTY RAMAQDTIDA AIQAHNLPAG SSKTIGLLLQ GAEDWSPTLY
IRLVQDYGLE SEVAQHLAST YGDKAFEVAK IAQVTGKRWP IVGKRLVSEF PYIEAEVIYG
VKEYARTAVD IISRRTRLAF LNVQAAEEAL PRIVDIMGKE LNWNEQKKKE ELEAARKFLY
YEMGYKVKSD QLTDSSEITL MPSDIERYKK RFHMFDKDKK GFITILDVQR VLESISVQID
EKTLHDILNE VDLNKNGQVE LIEFLQLMSA IQKGHVSGSR LAVLMKTAEE NLRQRVVIPV
DRSGGGL
//
