Full text data of FAHD1
FAHD1
(C16orf36, YISKL)
[Confidence: low (only semi-automatic identification from reviews)]
Acylpyruvase FAHD1, mitochondrial; 3.7.1.5 (Fumarylacetoacetate hydrolase domain-containing protein 1; YisK-like protein; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Acylpyruvase FAHD1, mitochondrial; 3.7.1.5 (Fumarylacetoacetate hydrolase domain-containing protein 1; YisK-like protein; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6P587
ID FAHD1_HUMAN Reviewed; 224 AA.
AC Q6P587; B1AK40; B1AK41; Q6FIC7; Q96RY1; Q9H0N6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2005, sequence version 2.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Acylpyruvase FAHD1, mitochondrial;
DE EC=3.7.1.5;
DE AltName: Full=Fumarylacetoacetate hydrolase domain-containing protein 1;
DE AltName: Full=YisK-like protein;
DE Flags: Precursor;
GN Name=FAHD1; Synonyms=C16orf36, YISKL;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2
RT Mb of the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Glial tumor;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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 [7]
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).
RN [8]
RP CATALYTIC ACTIVITY, KINETIC PARAMETERS, COFACTOR, MUTAGENESIS OF
RP ASP-102 AND ARG-106, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21878618; DOI=10.1074/jbc.M111.264770;
RA Pircher H., Straganz G.D., Ehehalt D., Morrow G., Tanguay R.M.,
RA Jansen-Durr P.;
RT "Identification of human fumarylacetoacetate hydrolase domain
RT containing protein 1 (FAHD1) as a novel mitochondrial acylpyruvase.";
RL J. Biol. Chem. 286:36500-36508(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM,
RP FUNCTION, AND DIMERIZATION.
RX PubMed=15551868; DOI=10.1515/BC.2004.122;
RA Manjasetty B.A., Niesen F.H., Delbrueck H., Goetz F., Sievert V.,
RA Buessow K., Behlke J., Heinemann U.;
RT "X-ray structure of fumarylacetoacetate hydrolase family member Homo
RT sapiens FLJ36880.";
RL Biol. Chem. 385:935-942(2004).
CC -!- FUNCTION: Probable mitochondrial acylpyruvase which is able to
CC hydrolyze acetylpyruvate and fumarylpyruvate in vitro.
CC -!- CATALYTIC ACTIVITY: A 3-acylpyruvate + H(2)O = a carboxylate +
CC pyruvate.
CC -!- COFACTOR: Magnesium or manganese (Probable).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 uM for acetylpyruvate;
CC Vmax=0.135 umol/min/mg enzyme toward acetylpyruvate;
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Q9NPD3:EXOSC4; NbExp=1; IntAct=EBI-597013, EBI-371823;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm, cytosol.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P587-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P587-2; Sequence=VSP_013741;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q6P587-3; Sequence=VSP_046259;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- TISSUE SPECIFICITY: Ubiquitous (at protein level).
CC -!- SIMILARITY: Belongs to the FAH family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK61295.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AE006639; AAK61295.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL136720; CAB66654.1; -; mRNA.
DR EMBL; AK094199; BAC04308.1; -; mRNA.
DR EMBL; CR533499; CAG38530.1; -; mRNA.
DR EMBL; AL031722; CAM26476.1; -; Genomic_DNA.
DR EMBL; AC012180; CAM26476.1; JOINED; Genomic_DNA.
DR EMBL; BC063017; AAH63017.1; -; mRNA.
DR RefSeq; NP_001018114.1; NM_001018104.2.
DR RefSeq; NP_001135870.1; NM_001142398.1.
DR RefSeq; NP_112485.1; NM_031208.3.
DR UniGene; Hs.513265; -.
DR PDB; 1SAW; X-ray; 2.20 A; A/B=2-224.
DR PDBsum; 1SAW; -.
DR ProteinModelPortal; Q6P587; -.
DR SMR; Q6P587; 6-224.
DR IntAct; Q6P587; 3.
DR MINT; MINT-3065811; -.
DR STRING; 9606.ENSP00000372112; -.
DR PhosphoSite; Q6P587; -.
DR DMDM; 68566321; -.
DR UCD-2DPAGE; Q6P587; -.
DR PaxDb; Q6P587; -.
DR PRIDE; Q6P587; -.
DR DNASU; 81889; -.
DR Ensembl; ENST00000382666; ENSP00000372112; ENSG00000180185.
DR Ensembl; ENST00000382668; ENSP00000372114; ENSG00000180185.
DR Ensembl; ENST00000427358; ENSP00000398053; ENSG00000180185.
DR GeneID; 81889; -.
DR KEGG; hsa:81889; -.
DR UCSC; uc002cnd.3; human.
DR CTD; 81889; -.
DR GeneCards; GC16P001876; -.
DR HGNC; HGNC:14169; FAHD1.
DR HPA; CAB025530; -.
DR neXtProt; NX_Q6P587; -.
DR PharmGKB; PA25551; -.
DR eggNOG; COG0179; -.
DR HOGENOM; HOG000063753; -.
DR HOVERGEN; HBG057495; -.
DR KO; K01557; -.
DR OMA; PKARIPD; -.
DR OrthoDB; EOG7DFXDC; -.
DR PhylomeDB; Q6P587; -.
DR EvolutionaryTrace; Q6P587; -.
DR GeneWiki; FAHD1; -.
DR GenomeRNAi; 81889; -.
DR NextBio; 72236; -.
DR PRO; PR:Q6P587; -.
DR Bgee; Q6P587; -.
DR CleanEx; HS_FAHD1; -.
DR Genevestigator; Q6P587; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0018773; F:acetylpyruvate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0047621; F:acylpyruvate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0034545; F:fumarylpyruvate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.850.10; -; 1.
DR InterPro; IPR002529; Fumarylacetoacetase_C.
DR InterPro; IPR011234; Fumarylacetoacetase_C-rel.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR SUPFAM; SSF56529; SSF56529; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calcium;
KW Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Mitochondrion; Polymorphism; Reference proteome; Transit peptide.
FT TRANSIT 1 27 Mitochondrion (Potential).
FT CHAIN 28 224 Acylpyruvase FAHD1, mitochondrial.
FT /FTId=PRO_0000156829.
FT METAL 71 71 Divalent metal cation.
FT METAL 73 73 Divalent metal cation.
FT METAL 102 102 Divalent metal cation.
FT MOD_RES 113 113 N6-acetyllysine (By similarity).
FT VAR_SEQ 213 224 VSMTFKVEKPEY -> PKVSSATLPVRLQE (in
FT isoform 2).
FT /FTId=VSP_013741.
FT VAR_SEQ 213 224 VSMTFKVEKPEY -> RQGLTLSPKLECSSAITAHCSLELP
FT GSSNPPSASRF (in isoform 3).
FT /FTId=VSP_046259.
FT VARIANT 110 110 D -> N (in dbSNP:rs3743853).
FT /FTId=VAR_049014.
FT MUTAGEN 102 102 D->A: Loss of catalytic activity; when
FT associated with A-106.
FT MUTAGEN 106 106 R->A: Loss of catalytic activity; when
FT associated with A-102.
FT CONFLICT 177 177 S -> P (in Ref. 4; CAG38530).
FT HELIX 10 12
FT HELIX 13 16
FT STRAND 19 24
FT STRAND 44 48
FT HELIX 49 51
FT STRAND 52 54
FT STRAND 68 70
FT STRAND 72 80
FT TURN 87 89
FT HELIX 90 92
FT STRAND 93 101
FT HELIX 106 115
FT HELIX 120 123
FT STRAND 129 131
FT STRAND 147 152
FT STRAND 155 161
FT HELIX 162 164
FT STRAND 165 167
FT HELIX 169 177
FT STRAND 187 189
FT STRAND 197 199
FT STRAND 204 209
FT TURN 210 212
FT STRAND 213 220
SQ SEQUENCE 224 AA; 24843 MW; A005E4ECD613C72E CRC64;
MGIMAASRPL SRFWEWGKNI VCVGRNYADH VREMRSAVLS EPVLFLKPST AYAPEGSPIL
MPAYTRNLHH ELELGVVMGK RCRAVPEAAA MDYVGGYALC LDMTARDVQD ECKKKGLPWT
LAKSFTASCP VSAFVPKEKI PDPHKLKLWL KVNGELRQEG ETSSMIFSIP YIISYVSKII
TLEEGDIILT GTPKGVGPVK ENDEIEAGIH GLVSMTFKVE KPEY
//
ID FAHD1_HUMAN Reviewed; 224 AA.
AC Q6P587; B1AK40; B1AK41; Q6FIC7; Q96RY1; Q9H0N6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2005, sequence version 2.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Acylpyruvase FAHD1, mitochondrial;
DE EC=3.7.1.5;
DE AltName: Full=Fumarylacetoacetate hydrolase domain-containing protein 1;
DE AltName: Full=YisK-like protein;
DE Flags: Precursor;
GN Name=FAHD1; Synonyms=C16orf36, YISKL;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2
RT Mb of the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Glial tumor;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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 [7]
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).
RN [8]
RP CATALYTIC ACTIVITY, KINETIC PARAMETERS, COFACTOR, MUTAGENESIS OF
RP ASP-102 AND ARG-106, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21878618; DOI=10.1074/jbc.M111.264770;
RA Pircher H., Straganz G.D., Ehehalt D., Morrow G., Tanguay R.M.,
RA Jansen-Durr P.;
RT "Identification of human fumarylacetoacetate hydrolase domain
RT containing protein 1 (FAHD1) as a novel mitochondrial acylpyruvase.";
RL J. Biol. Chem. 286:36500-36508(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM,
RP FUNCTION, AND DIMERIZATION.
RX PubMed=15551868; DOI=10.1515/BC.2004.122;
RA Manjasetty B.A., Niesen F.H., Delbrueck H., Goetz F., Sievert V.,
RA Buessow K., Behlke J., Heinemann U.;
RT "X-ray structure of fumarylacetoacetate hydrolase family member Homo
RT sapiens FLJ36880.";
RL Biol. Chem. 385:935-942(2004).
CC -!- FUNCTION: Probable mitochondrial acylpyruvase which is able to
CC hydrolyze acetylpyruvate and fumarylpyruvate in vitro.
CC -!- CATALYTIC ACTIVITY: A 3-acylpyruvate + H(2)O = a carboxylate +
CC pyruvate.
CC -!- COFACTOR: Magnesium or manganese (Probable).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 uM for acetylpyruvate;
CC Vmax=0.135 umol/min/mg enzyme toward acetylpyruvate;
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Q9NPD3:EXOSC4; NbExp=1; IntAct=EBI-597013, EBI-371823;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm, cytosol.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P587-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P587-2; Sequence=VSP_013741;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q6P587-3; Sequence=VSP_046259;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- TISSUE SPECIFICITY: Ubiquitous (at protein level).
CC -!- SIMILARITY: Belongs to the FAH family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK61295.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AE006639; AAK61295.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL136720; CAB66654.1; -; mRNA.
DR EMBL; AK094199; BAC04308.1; -; mRNA.
DR EMBL; CR533499; CAG38530.1; -; mRNA.
DR EMBL; AL031722; CAM26476.1; -; Genomic_DNA.
DR EMBL; AC012180; CAM26476.1; JOINED; Genomic_DNA.
DR EMBL; BC063017; AAH63017.1; -; mRNA.
DR RefSeq; NP_001018114.1; NM_001018104.2.
DR RefSeq; NP_001135870.1; NM_001142398.1.
DR RefSeq; NP_112485.1; NM_031208.3.
DR UniGene; Hs.513265; -.
DR PDB; 1SAW; X-ray; 2.20 A; A/B=2-224.
DR PDBsum; 1SAW; -.
DR ProteinModelPortal; Q6P587; -.
DR SMR; Q6P587; 6-224.
DR IntAct; Q6P587; 3.
DR MINT; MINT-3065811; -.
DR STRING; 9606.ENSP00000372112; -.
DR PhosphoSite; Q6P587; -.
DR DMDM; 68566321; -.
DR UCD-2DPAGE; Q6P587; -.
DR PaxDb; Q6P587; -.
DR PRIDE; Q6P587; -.
DR DNASU; 81889; -.
DR Ensembl; ENST00000382666; ENSP00000372112; ENSG00000180185.
DR Ensembl; ENST00000382668; ENSP00000372114; ENSG00000180185.
DR Ensembl; ENST00000427358; ENSP00000398053; ENSG00000180185.
DR GeneID; 81889; -.
DR KEGG; hsa:81889; -.
DR UCSC; uc002cnd.3; human.
DR CTD; 81889; -.
DR GeneCards; GC16P001876; -.
DR HGNC; HGNC:14169; FAHD1.
DR HPA; CAB025530; -.
DR neXtProt; NX_Q6P587; -.
DR PharmGKB; PA25551; -.
DR eggNOG; COG0179; -.
DR HOGENOM; HOG000063753; -.
DR HOVERGEN; HBG057495; -.
DR KO; K01557; -.
DR OMA; PKARIPD; -.
DR OrthoDB; EOG7DFXDC; -.
DR PhylomeDB; Q6P587; -.
DR EvolutionaryTrace; Q6P587; -.
DR GeneWiki; FAHD1; -.
DR GenomeRNAi; 81889; -.
DR NextBio; 72236; -.
DR PRO; PR:Q6P587; -.
DR Bgee; Q6P587; -.
DR CleanEx; HS_FAHD1; -.
DR Genevestigator; Q6P587; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0018773; F:acetylpyruvate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0047621; F:acylpyruvate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0034545; F:fumarylpyruvate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.850.10; -; 1.
DR InterPro; IPR002529; Fumarylacetoacetase_C.
DR InterPro; IPR011234; Fumarylacetoacetase_C-rel.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR SUPFAM; SSF56529; SSF56529; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calcium;
KW Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Mitochondrion; Polymorphism; Reference proteome; Transit peptide.
FT TRANSIT 1 27 Mitochondrion (Potential).
FT CHAIN 28 224 Acylpyruvase FAHD1, mitochondrial.
FT /FTId=PRO_0000156829.
FT METAL 71 71 Divalent metal cation.
FT METAL 73 73 Divalent metal cation.
FT METAL 102 102 Divalent metal cation.
FT MOD_RES 113 113 N6-acetyllysine (By similarity).
FT VAR_SEQ 213 224 VSMTFKVEKPEY -> PKVSSATLPVRLQE (in
FT isoform 2).
FT /FTId=VSP_013741.
FT VAR_SEQ 213 224 VSMTFKVEKPEY -> RQGLTLSPKLECSSAITAHCSLELP
FT GSSNPPSASRF (in isoform 3).
FT /FTId=VSP_046259.
FT VARIANT 110 110 D -> N (in dbSNP:rs3743853).
FT /FTId=VAR_049014.
FT MUTAGEN 102 102 D->A: Loss of catalytic activity; when
FT associated with A-106.
FT MUTAGEN 106 106 R->A: Loss of catalytic activity; when
FT associated with A-102.
FT CONFLICT 177 177 S -> P (in Ref. 4; CAG38530).
FT HELIX 10 12
FT HELIX 13 16
FT STRAND 19 24
FT STRAND 44 48
FT HELIX 49 51
FT STRAND 52 54
FT STRAND 68 70
FT STRAND 72 80
FT TURN 87 89
FT HELIX 90 92
FT STRAND 93 101
FT HELIX 106 115
FT HELIX 120 123
FT STRAND 129 131
FT STRAND 147 152
FT STRAND 155 161
FT HELIX 162 164
FT STRAND 165 167
FT HELIX 169 177
FT STRAND 187 189
FT STRAND 197 199
FT STRAND 204 209
FT TURN 210 212
FT STRAND 213 220
SQ SEQUENCE 224 AA; 24843 MW; A005E4ECD613C72E CRC64;
MGIMAASRPL SRFWEWGKNI VCVGRNYADH VREMRSAVLS EPVLFLKPST AYAPEGSPIL
MPAYTRNLHH ELELGVVMGK RCRAVPEAAA MDYVGGYALC LDMTARDVQD ECKKKGLPWT
LAKSFTASCP VSAFVPKEKI PDPHKLKLWL KVNGELRQEG ETSSMIFSIP YIISYVSKII
TLEEGDIILT GTPKGVGPVK ENDEIEAGIH GLVSMTFKVE KPEY
//