Full text data of ECHDC1
ECHDC1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ethylmalonyl-CoA decarboxylase; 4.1.1.94 (Enoyl-CoA hydratase domain-containing protein 1; Methylmalonyl-CoA decarboxylase; MMCD; 4.1.1.41)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ethylmalonyl-CoA decarboxylase; 4.1.1.94 (Enoyl-CoA hydratase domain-containing protein 1; Methylmalonyl-CoA decarboxylase; MMCD; 4.1.1.41)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NTX5
ID ECHD1_HUMAN Reviewed; 307 AA.
AC Q9NTX5; A6NFJ5; B7Z8S0; E9PEN7; E9PR31; F8W851; Q5TEF6; Q5TEF7;
read moreAC Q5TEG0; Q5TEG4; Q9NZ30;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Ethylmalonyl-CoA decarboxylase;
DE EC=4.1.1.94;
DE AltName: Full=Enoyl-CoA hydratase domain-containing protein 1;
DE AltName: Full=Methylmalonyl-CoA decarboxylase;
DE Short=MMCD;
DE EC=4.1.1.41;
GN Name=ECHDC1;
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 MRNA] (ISOFORM 2).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Hypothalamus;
RA Xiao H., Song H., Gao G., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human adrenal gland.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 FUNCTION.
RX PubMed=22016388; DOI=10.1074/jbc.M111.281527;
RA Linster C.L., Noel G., Stroobant V., Vertommen D., Vincent M.F.,
RA Bommer G.T., Veiga-da-Cunha M., Van Schaftingen E.;
RT "Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
RT proofreading.";
RL J. Biol. Chem. 286:42992-43003(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Decarboxylases ethylmalonyl-CoA decarboxylase, a
CC potentially toxic metabolite, to form butyryl-CoA, suggesting it
CC might be involved in metabolite proofreading. Also has
CC methylmalonyl-CoA decarboxylase activity at lower level.
CC -!- CATALYTIC ACTIVITY: (S)-ethylmalonyl-CoA = butanoyl-CoA + CO(2).
CC -!- CATALYTIC ACTIVITY: (S)-methylmalonyl-CoA = propanoyl-CoA + CO(2).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9NTX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NTX5-2; Sequence=VSP_022498;
CC Name=3;
CC IsoId=Q9NTX5-3; Sequence=VSP_042581;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9NTX5-4; Sequence=VSP_042581, VSP_042583;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q9NTX5-5; Sequence=VSP_022498, VSP_042583;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q9NTX5-6; Sequence=VSP_022498, VSP_042582;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67657.1; Type=Frameshift; Positions=121, 123, 125;
CC Sequence=CAI20295.1; Type=Erroneous gene model prediction;
CC Sequence=CAI20297.1; Type=Erroneous gene model prediction;
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DR EMBL; AL834469; CAD39128.1; -; mRNA.
DR EMBL; AK303812; BAH14056.1; -; mRNA.
DR EMBL; AF220192; AAF67657.1; ALT_FRAME; mRNA.
DR EMBL; AL109939; CAB76256.1; -; Genomic_DNA.
DR EMBL; AL109939; CAI20295.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL109939; CAI20297.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL109939; CAI20302.1; -; Genomic_DNA.
DR EMBL; AL109939; CAI20298.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48107.1; -; Genomic_DNA.
DR EMBL; BC003549; AAH03549.1; -; mRNA.
DR RefSeq; NP_001002030.1; NM_001002030.1.
DR RefSeq; NP_001099014.1; NM_001105544.1.
DR RefSeq; NP_001099015.1; NM_001105545.1.
DR RefSeq; NP_001132982.1; NM_001139510.1.
DR RefSeq; NP_060949.2; NM_018479.3.
DR RefSeq; XP_005267104.1; XM_005267047.1.
DR RefSeq; XP_005267105.1; XM_005267048.1.
DR RefSeq; XP_005267107.1; XM_005267050.1.
DR UniGene; Hs.486410; -.
DR ProteinModelPortal; Q9NTX5; -.
DR SMR; Q9NTX5; 57-285.
DR IntAct; Q9NTX5; 2.
DR STRING; 9606.ENSP00000357278; -.
DR PhosphoSite; Q9NTX5; -.
DR DMDM; 124007138; -.
DR PaxDb; Q9NTX5; -.
DR PRIDE; Q9NTX5; -.
DR DNASU; 55862; -.
DR Ensembl; ENST00000309620; ENSP00000311115; ENSG00000093144.
DR Ensembl; ENST00000368289; ENSP00000357272; ENSG00000093144.
DR Ensembl; ENST00000368291; ENSP00000357274; ENSG00000093144.
DR Ensembl; ENST00000430841; ENSP00000402492; ENSG00000093144.
DR Ensembl; ENST00000454591; ENSP00000404866; ENSG00000093144.
DR Ensembl; ENST00000454859; ENSP00000401751; ENSG00000093144.
DR Ensembl; ENST00000474289; ENSP00000434908; ENSG00000093144.
DR Ensembl; ENST00000528402; ENSP00000436109; ENSG00000093144.
DR Ensembl; ENST00000531967; ENSP00000436585; ENSG00000093144.
DR GeneID; 55862; -.
DR KEGG; hsa:55862; -.
DR UCSC; uc003qax.3; human.
DR CTD; 55862; -.
DR GeneCards; GC06M127609; -.
DR H-InvDB; HIX0006203; -.
DR HGNC; HGNC:21489; ECHDC1.
DR HPA; HPA035445; -.
DR MIM; 612136; gene.
DR neXtProt; NX_Q9NTX5; -.
DR PharmGKB; PA134871524; -.
DR eggNOG; COG1024; -.
DR HOGENOM; HOG000007808; -.
DR HOVERGEN; HBG054783; -.
DR OMA; HKHMGLV; -.
DR OrthoDB; EOG79W95T; -.
DR ChiTaRS; ECHDC1; human.
DR GenomeRNAi; 55862; -.
DR NextBio; 61169; -.
DR PRO; PR:Q9NTX5; -.
DR ArrayExpress; Q9NTX5; -.
DR Bgee; Q9NTX5; -.
DR CleanEx; HS_ECHDC1; -.
DR Genevestigator; Q9NTX5; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016831; F:carboxy-lyase activity; ISS:UniProtKB.
DR GO; GO:0004492; F:methylmalonyl-CoA decarboxylase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001753; Crotonase_core_superfam.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR Pfam; PF00378; ECH; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Lyase; Reference proteome.
FT CHAIN 1 307 Ethylmalonyl-CoA decarboxylase.
FT /FTId=PRO_0000273246.
FT MOD_RES 217 217 N6-acetyllysine (By similarity).
FT VAR_SEQ 1 81 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_042581.
FT VAR_SEQ 1 6 Missing (in isoform 2, isoform 5 and
FT isoform 6).
FT /FTId=VSP_022498.
FT VAR_SEQ 125 144 TPEDGMAVCMFMQNTLTRFM -> LQR (in isoform
FT 6).
FT /FTId=VSP_042582.
FT VAR_SEQ 128 307 DGMAVCMFMQNTLTRFMRLPLISVALVQGWALGGGAEFTTA
FT CDFRLMTPESKIRFVHKEMGIIPSWGGTTRLVEIIGSRQAL
FT KVLSGALKLDSKNALNIGMVEEVLQSSDETKSLEEAQEWLK
FT QFIQGPPEVIRALKKSVCSGRELYLEEALQNERDLLGTVWG
FT GPANLEAIAKKGKFNK -> TSFNKCCAGSRLGIGWRSRIY
FT YSM (in isoform 4 and isoform 5).
FT /FTId=VSP_042583.
FT CONFLICT 243 243 E -> G (in Ref. 2; BAH14056).
FT CONFLICT 263 263 L -> M (in Ref. 2; BAH14056).
SQ SEQUENCE 307 AA; 33698 MW; 77A09FDE065FE0A4 CRC64;
MALKQEMAKS LLKTASLSGR TKLLHQTGLS LYSTSHGFYE EEVKKTLQQF PGGSIDLQKE
DNGIGILTLN NPSRMNAFSG VMMLQLLEKV IELENWTEGK GLIVRGAKNT FSSGSDLNAV
KSLGTPEDGM AVCMFMQNTL TRFMRLPLIS VALVQGWALG GGAEFTTACD FRLMTPESKI
RFVHKEMGII PSWGGTTRLV EIIGSRQALK VLSGALKLDS KNALNIGMVE EVLQSSDETK
SLEEAQEWLK QFIQGPPEVI RALKKSVCSG RELYLEEALQ NERDLLGTVW GGPANLEAIA
KKGKFNK
//
ID ECHD1_HUMAN Reviewed; 307 AA.
AC Q9NTX5; A6NFJ5; B7Z8S0; E9PEN7; E9PR31; F8W851; Q5TEF6; Q5TEF7;
read moreAC Q5TEG0; Q5TEG4; Q9NZ30;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Ethylmalonyl-CoA decarboxylase;
DE EC=4.1.1.94;
DE AltName: Full=Enoyl-CoA hydratase domain-containing protein 1;
DE AltName: Full=Methylmalonyl-CoA decarboxylase;
DE Short=MMCD;
DE EC=4.1.1.41;
GN Name=ECHDC1;
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 MRNA] (ISOFORM 2).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Hypothalamus;
RA Xiao H., Song H., Gao G., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human adrenal gland.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 FUNCTION.
RX PubMed=22016388; DOI=10.1074/jbc.M111.281527;
RA Linster C.L., Noel G., Stroobant V., Vertommen D., Vincent M.F.,
RA Bommer G.T., Veiga-da-Cunha M., Van Schaftingen E.;
RT "Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
RT proofreading.";
RL J. Biol. Chem. 286:42992-43003(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Decarboxylases ethylmalonyl-CoA decarboxylase, a
CC potentially toxic metabolite, to form butyryl-CoA, suggesting it
CC might be involved in metabolite proofreading. Also has
CC methylmalonyl-CoA decarboxylase activity at lower level.
CC -!- CATALYTIC ACTIVITY: (S)-ethylmalonyl-CoA = butanoyl-CoA + CO(2).
CC -!- CATALYTIC ACTIVITY: (S)-methylmalonyl-CoA = propanoyl-CoA + CO(2).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9NTX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NTX5-2; Sequence=VSP_022498;
CC Name=3;
CC IsoId=Q9NTX5-3; Sequence=VSP_042581;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9NTX5-4; Sequence=VSP_042581, VSP_042583;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q9NTX5-5; Sequence=VSP_022498, VSP_042583;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q9NTX5-6; Sequence=VSP_022498, VSP_042582;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67657.1; Type=Frameshift; Positions=121, 123, 125;
CC Sequence=CAI20295.1; Type=Erroneous gene model prediction;
CC Sequence=CAI20297.1; Type=Erroneous gene model prediction;
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DR EMBL; AL834469; CAD39128.1; -; mRNA.
DR EMBL; AK303812; BAH14056.1; -; mRNA.
DR EMBL; AF220192; AAF67657.1; ALT_FRAME; mRNA.
DR EMBL; AL109939; CAB76256.1; -; Genomic_DNA.
DR EMBL; AL109939; CAI20295.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL109939; CAI20297.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL109939; CAI20302.1; -; Genomic_DNA.
DR EMBL; AL109939; CAI20298.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48107.1; -; Genomic_DNA.
DR EMBL; BC003549; AAH03549.1; -; mRNA.
DR RefSeq; NP_001002030.1; NM_001002030.1.
DR RefSeq; NP_001099014.1; NM_001105544.1.
DR RefSeq; NP_001099015.1; NM_001105545.1.
DR RefSeq; NP_001132982.1; NM_001139510.1.
DR RefSeq; NP_060949.2; NM_018479.3.
DR RefSeq; XP_005267104.1; XM_005267047.1.
DR RefSeq; XP_005267105.1; XM_005267048.1.
DR RefSeq; XP_005267107.1; XM_005267050.1.
DR UniGene; Hs.486410; -.
DR ProteinModelPortal; Q9NTX5; -.
DR SMR; Q9NTX5; 57-285.
DR IntAct; Q9NTX5; 2.
DR STRING; 9606.ENSP00000357278; -.
DR PhosphoSite; Q9NTX5; -.
DR DMDM; 124007138; -.
DR PaxDb; Q9NTX5; -.
DR PRIDE; Q9NTX5; -.
DR DNASU; 55862; -.
DR Ensembl; ENST00000309620; ENSP00000311115; ENSG00000093144.
DR Ensembl; ENST00000368289; ENSP00000357272; ENSG00000093144.
DR Ensembl; ENST00000368291; ENSP00000357274; ENSG00000093144.
DR Ensembl; ENST00000430841; ENSP00000402492; ENSG00000093144.
DR Ensembl; ENST00000454591; ENSP00000404866; ENSG00000093144.
DR Ensembl; ENST00000454859; ENSP00000401751; ENSG00000093144.
DR Ensembl; ENST00000474289; ENSP00000434908; ENSG00000093144.
DR Ensembl; ENST00000528402; ENSP00000436109; ENSG00000093144.
DR Ensembl; ENST00000531967; ENSP00000436585; ENSG00000093144.
DR GeneID; 55862; -.
DR KEGG; hsa:55862; -.
DR UCSC; uc003qax.3; human.
DR CTD; 55862; -.
DR GeneCards; GC06M127609; -.
DR H-InvDB; HIX0006203; -.
DR HGNC; HGNC:21489; ECHDC1.
DR HPA; HPA035445; -.
DR MIM; 612136; gene.
DR neXtProt; NX_Q9NTX5; -.
DR PharmGKB; PA134871524; -.
DR eggNOG; COG1024; -.
DR HOGENOM; HOG000007808; -.
DR HOVERGEN; HBG054783; -.
DR OMA; HKHMGLV; -.
DR OrthoDB; EOG79W95T; -.
DR ChiTaRS; ECHDC1; human.
DR GenomeRNAi; 55862; -.
DR NextBio; 61169; -.
DR PRO; PR:Q9NTX5; -.
DR ArrayExpress; Q9NTX5; -.
DR Bgee; Q9NTX5; -.
DR CleanEx; HS_ECHDC1; -.
DR Genevestigator; Q9NTX5; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016831; F:carboxy-lyase activity; ISS:UniProtKB.
DR GO; GO:0004492; F:methylmalonyl-CoA decarboxylase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001753; Crotonase_core_superfam.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR Pfam; PF00378; ECH; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Lyase; Reference proteome.
FT CHAIN 1 307 Ethylmalonyl-CoA decarboxylase.
FT /FTId=PRO_0000273246.
FT MOD_RES 217 217 N6-acetyllysine (By similarity).
FT VAR_SEQ 1 81 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_042581.
FT VAR_SEQ 1 6 Missing (in isoform 2, isoform 5 and
FT isoform 6).
FT /FTId=VSP_022498.
FT VAR_SEQ 125 144 TPEDGMAVCMFMQNTLTRFM -> LQR (in isoform
FT 6).
FT /FTId=VSP_042582.
FT VAR_SEQ 128 307 DGMAVCMFMQNTLTRFMRLPLISVALVQGWALGGGAEFTTA
FT CDFRLMTPESKIRFVHKEMGIIPSWGGTTRLVEIIGSRQAL
FT KVLSGALKLDSKNALNIGMVEEVLQSSDETKSLEEAQEWLK
FT QFIQGPPEVIRALKKSVCSGRELYLEEALQNERDLLGTVWG
FT GPANLEAIAKKGKFNK -> TSFNKCCAGSRLGIGWRSRIY
FT YSM (in isoform 4 and isoform 5).
FT /FTId=VSP_042583.
FT CONFLICT 243 243 E -> G (in Ref. 2; BAH14056).
FT CONFLICT 263 263 L -> M (in Ref. 2; BAH14056).
SQ SEQUENCE 307 AA; 33698 MW; 77A09FDE065FE0A4 CRC64;
MALKQEMAKS LLKTASLSGR TKLLHQTGLS LYSTSHGFYE EEVKKTLQQF PGGSIDLQKE
DNGIGILTLN NPSRMNAFSG VMMLQLLEKV IELENWTEGK GLIVRGAKNT FSSGSDLNAV
KSLGTPEDGM AVCMFMQNTL TRFMRLPLIS VALVQGWALG GGAEFTTACD FRLMTPESKI
RFVHKEMGII PSWGGTTRLV EIIGSRQALK VLSGALKLDS KNALNIGMVE EVLQSSDETK
SLEEAQEWLK QFIQGPPEVI RALKKSVCSG RELYLEEALQ NERDLLGTVW GGPANLEAIA
KKGKFNK
//
MIM
612136
*RECORD*
*FIELD* NO
612136
*FIELD* TI
*612136 ENOYL COENZYME A HYDRATASE DOMAIN-CONTAINING PROTEIN 1; ECHDC1
*FIELD* TX
read moreCLONING
Gold et al. (2008) stated that the ECHDC1 protein shares characteristics
with proteins involved in mitochondrial fatty acid oxidation.
MAPPING
Gold et al. (2008) reported that the ECHDC1 gene maps to chromosome
6q22.33.
*FIELD* RF
1. Gold, B.; Kirchhoff, T.; Stefanov, S.; Lautenberger, J.; Viale,
A.; Garber, J.; Friedman, E.; Narod, S.; Olshen, A. B.; Gregersen,
P.; Kosarin, K.; Olsh, A.; Bergeron, J.; Ellis, N. A.; Klein, R. J.;
Clark, A. G.; Norton, L.; Dean, M.; Boyd, J.; Offit, K.: Genome-wide
association study provides evidence for a breast cancer risk locus
at 6q22.33. Proc. Nat. Acad. Sci. 105: 4340-4345, 2008.
*FIELD* CD
Patricia A. Hartz: 6/27/2008
*FIELD* ED
mgross: 06/27/2008
*RECORD*
*FIELD* NO
612136
*FIELD* TI
*612136 ENOYL COENZYME A HYDRATASE DOMAIN-CONTAINING PROTEIN 1; ECHDC1
*FIELD* TX
read moreCLONING
Gold et al. (2008) stated that the ECHDC1 protein shares characteristics
with proteins involved in mitochondrial fatty acid oxidation.
MAPPING
Gold et al. (2008) reported that the ECHDC1 gene maps to chromosome
6q22.33.
*FIELD* RF
1. Gold, B.; Kirchhoff, T.; Stefanov, S.; Lautenberger, J.; Viale,
A.; Garber, J.; Friedman, E.; Narod, S.; Olshen, A. B.; Gregersen,
P.; Kosarin, K.; Olsh, A.; Bergeron, J.; Ellis, N. A.; Klein, R. J.;
Clark, A. G.; Norton, L.; Dean, M.; Boyd, J.; Offit, K.: Genome-wide
association study provides evidence for a breast cancer risk locus
at 6q22.33. Proc. Nat. Acad. Sci. 105: 4340-4345, 2008.
*FIELD* CD
Patricia A. Hartz: 6/27/2008
*FIELD* ED
mgross: 06/27/2008