ID A0A452F334_CAPHI Unreviewed; 727 AA.
AC A0A452F334;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:ENSCHIP00000018752.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000018752.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000018752.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000018752.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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; LWLT01000002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017918736.1; XM_018063247.1.
DR AlphaFoldDB; A0A452F334; -.
DR Ensembl; ENSCHIT00000026567.1; ENSCHIP00000018752.1; ENSCHIG00000018054.1.
DR GeneID; 102176370; -.
DR CTD; 2820; -.
DR GeneTree; ENSGT00390000001718; -.
DR OrthoDB; 989271at2759; -.
DR Proteomes; UP000291000; Chromosome 2.
DR Bgee; ENSCHIG00000018054; Expressed in longissimus thoracis muscle and 17 other cell types or tissues.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 623..658
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 659..694
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 727 AA; 80812 MW; B580F28D9ADF6E01 CRC64;
MAFQKAVKGT VLVGGGALAT VLGLSHFAHY KRKQVNLAFV EAADCVSEPV NREPPSREAQ
ILTLKNTSEF DVLVIGGGAT GSGCALDAVT RGLKTALVER DDFSSGTSSR STKLIHGGVR
YLQKAIMKLD IEQYRMVKEA LHERANLLEI APHLSAPLPI MLPVYKWWQL PYYWVGIKLY
DLVAGSNCLK SSYVLSKSRA LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG
AATANYMEVM SLLKKTDPQT GKERVSGARC KDVLTGEEFD VRAKCVINAT GPFTDTVRKM
DDKDTTAICQ PSAGVHIVMP GYYSPESMGL LDPATSDGRV IFFLPWQKMT IAGTTDTPTD
VTHHPIPSEE DINFILNEVR NYLSCDVEVR RGDVLAAWSG IRPLVTDPKS ADTKSISRNH
VVDISESGLI TIAGGKWTTY RSMAEDTINA AVKAHNLKAG PSRTVGLFLQ GGKDWSPTLY
IRLVQDYGLE SEVAQHLAAT YGDKAFEVAK MASVTGKRWP IVGVRLVSEF PYIEAEVKYG
IKEYACTAVD MISRRTRLAF LNVQAAEEAL PRIVELMGRE LNWDDSKKEE ELETARKFLY
YEMGYKSRSE QLTDRSEISL LPSDIDRYKK RFHKFDADQK GFITIVDVQR VLESINVQMD
ENTLHEILNE VDLNKNGQVE LNEFLQLMSA IQKGRVSGSR LAILMKTAEE NLDRRVPIPV
DRSCGGF
//
