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Database: UniProt
Entry: A7DZP8
LinkDB: A7DZP8
Original site: A7DZP8 
ID   GPDM_MESAU              Reviewed;         727 AA.
AC   A7DZP8;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   10-APR-2019, entry version 61.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial;
DE            Short=GPD-M;
DE            Short=GPDH-M;
DE            EC=1.1.5.3;
DE   AltName: Full=mGPD;
DE   Flags: Precursor;
GN   Name=GPD2;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Venkatesh K., Shivaji S.;
RT   "Hamster sperm capacitation: role of FAD linked glycerol-3-phosphate
RT   dehydrogenase.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B.,
RA   Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection
RT   antigen (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:132124; EC=1.1.5.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Calcium-binding enhance the activity of the
CC       enzyme. {ECO:0000250}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (aerobic route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AM774032; CAO79918.1; -; mRNA.
DR   RefSeq; NP_001268609.1; NM_001281680.1.
DR   ProteinModelPortal; A7DZP8; -.
DR   SMR; A7DZP8; -.
DR   STRING; 10036.XP_005069035.1; -.
DR   PRIDE; A7DZP8; -.
DR   GeneID; 101825992; -.
DR   CTD; 2820; -.
DR   HOVERGEN; HBG005897; -.
DR   OrthoDB; 669193at2759; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000189706; Genome assembly.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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   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   Calcium; Complete proteome; FAD; Flavoprotein; Metal-binding;
KW   Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Repeat; Transit peptide.
FT   TRANSIT       1     42       Mitochondrion. {ECO:0000250}.
FT   CHAIN        43    727       Glycerol-3-phosphate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000355968.
FT   DOMAIN      623    658       EF-hand 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      659    694       EF-hand 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   NP_BIND      71     99       FAD. {ECO:0000255}.
FT   CA_BIND     672    683       {ECO:0000255|PROSITE-ProRule:PRU00448}.
FT   MOD_RES     601    601       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q64521}.
SQ   SEQUENCE   727 AA;  80857 MW;  89C18A4C8D0205DA CRC64;
     MAFQKAVKRT VLVCGGALAT VLGLSQCSHY RRKQVNLACL KAAGCHTEPV NREPPSREAQ
     LLTLQNTSEF DILVIGGGAT GSGCALDAVT RGLKTALVER DDFSSGTSSR STKLIHGGVR
     YLQKAIMKLD VEQYRMVKEA LHERANLLEI APHLSAPLPI MLPIYKWWQL PYYWVGIKLY
     DLVAGSNCLK SSYVLSKSRA LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG
     AATANYREVV SLLKKTDPET GKERVSGARC KDVLTGLEFD VRAKCVINAT GPFTDSVRKM
     DDNKAPAICQ PSAGVHIVMP GYYSPESMGL LDPATSDGRV IFFLPWENMT IAGTTDSPTK
     NTHHPIPSEE DINFILNEVR NYLSCDVEVR RGDVLAAWSG IRPLVIDPKS ADTQSISRNH
     VVDVSESGLI TIAGGKWTTY RSMAEDTVDT AIKVHNLKAG PCRTVGLFLQ GGKDWSPTLY
     IRLVQDYGLE SEVAQHLATT YGDKAFEVAK MAKVTGKRWP IVGVRLVSEF PYIEAEVKYG
     IKEYACTAVD MISRRTRLAF LNIQAAEEAL PRIVELMGRE LDWSEIRKQA ELETATKFLY
     YEMGSKSRSE QLTDRTEISL RPSDIERYTK RFHKFDADEK GFITIVDVQR VLENINVKID
     ENTLHEILSE VDLNKNGQVE LNEFLQLMSA IQKGRVSGSR LAILMKTAEE NLDRRVPIPV
     DRSCGGL
//
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