Full text data of SQRDL
SQRDL
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Sulfide:quinone oxidoreductase, mitochondrial; 1.-.-.-; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Sulfide:quinone oxidoreductase, mitochondrial; 1.-.-.-; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y6N5
ID SQRD_HUMAN Reviewed; 450 AA.
AC Q9Y6N5; Q9UQM8;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Sulfide:quinone oxidoreductase, mitochondrial;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=SQRDL; ORFNames=CGI-44;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10224084; DOI=10.1074/jbc.274.19.13250;
RA Vande Weghe J.G., Ow D.W.;
RT "A fission yeast gene for mitochondrial sulfide oxidation.";
RL J. Biol. Chem. 274:13250-13257(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-264.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the oxidation of hydrogen sulfide, with the
CC help of a quinone (By similarity).
CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion (Probable).
CC -!- SIMILARITY: Belongs to the SQRD family.
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DR EMBL; AF042284; AAD41160.1; -; mRNA.
DR EMBL; AF151802; AAD34039.1; -; mRNA.
DR EMBL; BC016836; AAH16836.1; -; mRNA.
DR RefSeq; NP_001258142.1; NM_001271213.1.
DR RefSeq; NP_067022.1; NM_021199.3.
DR RefSeq; XP_005254628.1; XM_005254571.1.
DR RefSeq; XP_005254629.1; XM_005254572.1.
DR UniGene; Hs.511251; -.
DR UniGene; Hs.743355; -.
DR ProteinModelPortal; Q9Y6N5; -.
DR SMR; Q9Y6N5; 41-398.
DR IntAct; Q9Y6N5; 6.
DR MINT; MINT-4657978; -.
DR STRING; 9606.ENSP00000260324; -.
DR PhosphoSite; Q9Y6N5; -.
DR DMDM; 27151704; -.
DR PaxDb; Q9Y6N5; -.
DR PeptideAtlas; Q9Y6N5; -.
DR PRIDE; Q9Y6N5; -.
DR DNASU; 58472; -.
DR Ensembl; ENST00000260324; ENSP00000260324; ENSG00000137767.
DR Ensembl; ENST00000568606; ENSP00000456019; ENSG00000137767.
DR GeneID; 58472; -.
DR KEGG; hsa:58472; -.
DR UCSC; uc001zvu.4; human.
DR CTD; 58472; -.
DR GeneCards; GC15P045927; -.
DR HGNC; HGNC:20390; SQRDL.
DR HPA; HPA017079; -.
DR HPA; HPA041589; -.
DR neXtProt; NX_Q9Y6N5; -.
DR PharmGKB; PA134894920; -.
DR eggNOG; COG0446; -.
DR HOGENOM; HOG000249874; -.
DR HOVERGEN; HBG029110; -.
DR InParanoid; Q9Y6N5; -.
DR KO; K17218; -.
DR OMA; DKHYYQP; -.
DR PhylomeDB; Q9Y6N5; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; SQRDL; human.
DR GenomeRNAi; 58472; -.
DR NextBio; 64896; -.
DR PRO; PR:Q9Y6N5; -.
DR ArrayExpress; Q9Y6N5; -.
DR Bgee; Q9Y6N5; -.
DR CleanEx; HS_SQRDL; -.
DR Genevestigator; Q9Y6N5; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0070224; F:sulfide:quinone oxidoreductase activity; TAS:Reactome.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0070221; P:sulfide oxidation, using sulfide:quinone oxidoreductase; TAS:Reactome.
DR GO; GO:0000098; P:sulfur amino acid catabolic process; TAS:Reactome.
DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR InterPro; IPR015904; Sulphide_quinone_reductase.
DR PANTHER; PTHR10632; PTHR10632; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion;
KW NADP; Oxidoreductase; Polymorphism; Reference proteome;
KW Transit peptide.
FT TRANSIT 1 ? Mitochondrion (Potential).
FT CHAIN ? 450 Sulfide:quinone oxidoreductase,
FT mitochondrial.
FT /FTId=PRO_0000022408.
FT MOD_RES 173 173 N6-acetyllysine (By similarity).
FT VARIANT 264 264 I -> T (in dbSNP:rs1044032).
FT /FTId=VAR_014959.
SQ SEQUENCE 450 AA; 49961 MW; 943ABD4049E3634D CRC64;
MVPLVAVVSG PRAQLFACLL RLGTQQVGPL QLHTGASHAA RNHYEVLVLG GGSGGITMAA
RMKRKVGAEN VAIVEPSERH FYQPIWTLVG AGAKQLSSSG RPTASVIPSG VEWIKARVTE
LNPDKNCIHT DDDEKISYRY LIIALGIQLD YEKIKGLPEG FAHPKIGSNY SVKTVEKTWK
ALQDFKEGNA IFTFPNTPVK CAGAPQKIMY LSEAYFRKTG KRSKANIIFN TSLGAIFGVK
KYADALQEII QERNLTVNYK KNLIEVRADK QEAVFENLDK PGETQVISYE MLHVTPPMSP
PDVLKTSPVA DAAGWVDVDK ETLQHRRYPN VFGIGDCTNL PTSKTAAAVA AQSGILDRTI
SVIMKNQTPT KKYDGYTSCP LVTGYNRVIL AEFDYKAEPL ETFPFDQSKE RLSMYLMKAD
LMPFLYWNMM LRGYWGGPAF LRKLFHLGMS
//
ID SQRD_HUMAN Reviewed; 450 AA.
AC Q9Y6N5; Q9UQM8;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Sulfide:quinone oxidoreductase, mitochondrial;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=SQRDL; ORFNames=CGI-44;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10224084; DOI=10.1074/jbc.274.19.13250;
RA Vande Weghe J.G., Ow D.W.;
RT "A fission yeast gene for mitochondrial sulfide oxidation.";
RL J. Biol. Chem. 274:13250-13257(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-264.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the oxidation of hydrogen sulfide, with the
CC help of a quinone (By similarity).
CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion (Probable).
CC -!- SIMILARITY: Belongs to the SQRD family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF042284; AAD41160.1; -; mRNA.
DR EMBL; AF151802; AAD34039.1; -; mRNA.
DR EMBL; BC016836; AAH16836.1; -; mRNA.
DR RefSeq; NP_001258142.1; NM_001271213.1.
DR RefSeq; NP_067022.1; NM_021199.3.
DR RefSeq; XP_005254628.1; XM_005254571.1.
DR RefSeq; XP_005254629.1; XM_005254572.1.
DR UniGene; Hs.511251; -.
DR UniGene; Hs.743355; -.
DR ProteinModelPortal; Q9Y6N5; -.
DR SMR; Q9Y6N5; 41-398.
DR IntAct; Q9Y6N5; 6.
DR MINT; MINT-4657978; -.
DR STRING; 9606.ENSP00000260324; -.
DR PhosphoSite; Q9Y6N5; -.
DR DMDM; 27151704; -.
DR PaxDb; Q9Y6N5; -.
DR PeptideAtlas; Q9Y6N5; -.
DR PRIDE; Q9Y6N5; -.
DR DNASU; 58472; -.
DR Ensembl; ENST00000260324; ENSP00000260324; ENSG00000137767.
DR Ensembl; ENST00000568606; ENSP00000456019; ENSG00000137767.
DR GeneID; 58472; -.
DR KEGG; hsa:58472; -.
DR UCSC; uc001zvu.4; human.
DR CTD; 58472; -.
DR GeneCards; GC15P045927; -.
DR HGNC; HGNC:20390; SQRDL.
DR HPA; HPA017079; -.
DR HPA; HPA041589; -.
DR neXtProt; NX_Q9Y6N5; -.
DR PharmGKB; PA134894920; -.
DR eggNOG; COG0446; -.
DR HOGENOM; HOG000249874; -.
DR HOVERGEN; HBG029110; -.
DR InParanoid; Q9Y6N5; -.
DR KO; K17218; -.
DR OMA; DKHYYQP; -.
DR PhylomeDB; Q9Y6N5; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; SQRDL; human.
DR GenomeRNAi; 58472; -.
DR NextBio; 64896; -.
DR PRO; PR:Q9Y6N5; -.
DR ArrayExpress; Q9Y6N5; -.
DR Bgee; Q9Y6N5; -.
DR CleanEx; HS_SQRDL; -.
DR Genevestigator; Q9Y6N5; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0070224; F:sulfide:quinone oxidoreductase activity; TAS:Reactome.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0070221; P:sulfide oxidation, using sulfide:quinone oxidoreductase; TAS:Reactome.
DR GO; GO:0000098; P:sulfur amino acid catabolic process; TAS:Reactome.
DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR InterPro; IPR015904; Sulphide_quinone_reductase.
DR PANTHER; PTHR10632; PTHR10632; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion;
KW NADP; Oxidoreductase; Polymorphism; Reference proteome;
KW Transit peptide.
FT TRANSIT 1 ? Mitochondrion (Potential).
FT CHAIN ? 450 Sulfide:quinone oxidoreductase,
FT mitochondrial.
FT /FTId=PRO_0000022408.
FT MOD_RES 173 173 N6-acetyllysine (By similarity).
FT VARIANT 264 264 I -> T (in dbSNP:rs1044032).
FT /FTId=VAR_014959.
SQ SEQUENCE 450 AA; 49961 MW; 943ABD4049E3634D CRC64;
MVPLVAVVSG PRAQLFACLL RLGTQQVGPL QLHTGASHAA RNHYEVLVLG GGSGGITMAA
RMKRKVGAEN VAIVEPSERH FYQPIWTLVG AGAKQLSSSG RPTASVIPSG VEWIKARVTE
LNPDKNCIHT DDDEKISYRY LIIALGIQLD YEKIKGLPEG FAHPKIGSNY SVKTVEKTWK
ALQDFKEGNA IFTFPNTPVK CAGAPQKIMY LSEAYFRKTG KRSKANIIFN TSLGAIFGVK
KYADALQEII QERNLTVNYK KNLIEVRADK QEAVFENLDK PGETQVISYE MLHVTPPMSP
PDVLKTSPVA DAAGWVDVDK ETLQHRRYPN VFGIGDCTNL PTSKTAAAVA AQSGILDRTI
SVIMKNQTPT KKYDGYTSCP LVTGYNRVIL AEFDYKAEPL ETFPFDQSKE RLSMYLMKAD
LMPFLYWNMM LRGYWGGPAF LRKLFHLGMS
//