ECHD1_HUMAN
ID ECHD1_HUMAN Reviewed; 307 AA.
AC Q9NTX5; A6NFJ5; B7Z8S0; E9PEN7; E9PR31; F8W851; Q5TEF6; Q5TEF7; Q5TEG0;
AC Q5TEG4; Q9NZ30; V9HW18;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Ethylmalonyl-CoA decarboxylase;
DE EC=4.1.1.94 {ECO:0000269|PubMed:22016388};
DE AltName: Full=Enoyl-CoA hydratase domain-containing protein 1;
DE AltName: Full=Methylmalonyl-CoA decarboxylase;
DE Short=MMCD;
GN Name=ECHDC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Epididymis;
RA Li J.Y., Wang H.Y., Liu F.J., Liu J.;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 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 [5]
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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
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., Buerckstuemmer T.,
RA 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 [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORMS 2; 5 AND 6), CLEAVAGE
RP OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 5), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 6), AND IDENTIFICATION
RP 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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Decarboxylates ethylmalonyl-CoA, a potentially toxic
CC metabolite, to form butyryl-CoA, suggesting it might be involved in
CC metabolite proofreading (PubMed:22016388). Also has methylmalonyl-CoA
CC decarboxylase activity at lower level (By similarity).
CC {ECO:0000250|UniProtKB:Q9D9V3, ECO:0000269|PubMed:22016388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-ethylmalonyl-CoA + H(+) = butanoyl-CoA + CO2;
CC Xref=Rhea:RHEA:32131, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:60909; EC=4.1.1.94;
CC Evidence={ECO:0000269|PubMed:22016388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32132;
CC Evidence={ECO:0000305|PubMed:22016388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-methylmalonyl-CoA + H(+) = CO2 + propanoyl-CoA;
CC Xref=Rhea:RHEA:61340, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57392; EC=4.1.1.94;
CC Evidence={ECO:0000250|UniProtKB:Q9D9V3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61341;
CC Evidence={ECO:0000250|UniProtKB:Q9D9V3};
CC -!- INTERACTION:
CC Q9NTX5; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-2807146, EBI-739467;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:22016388}.
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 Name=4; Synonyms=HEL-S-76;
CC IsoId=Q9NTX5-4; Sequence=VSP_042581, VSP_042583;
CC Name=5;
CC IsoId=Q9NTX5-5; Sequence=VSP_022498, VSP_042583;
CC Name=6;
CC IsoId=Q9NTX5-6; Sequence=VSP_022498, VSP_042582;
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67657.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; EU668355; ACF94508.1; -; mRNA.
DR EMBL; AL834469; CAD39128.1; -; mRNA.
DR EMBL; AK303812; BAH14056.1; -; mRNA.
DR EMBL; AF220192; AAF67657.1; ALT_FRAME; mRNA.
DR EMBL; AL109939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48107.1; -; Genomic_DNA.
DR EMBL; BC003549; AAH03549.1; -; mRNA.
DR CCDS; CCDS34530.1; -. [Q9NTX5-5]
DR CCDS; CCDS43504.1; -. [Q9NTX5-2]
DR CCDS; CCDS47471.1; -. [Q9NTX5-1]
DR CCDS; CCDS47472.1; -. [Q9NTX5-3]
DR CCDS; CCDS55054.1; -. [Q9NTX5-4]
DR RefSeq; NP_001002030.1; NM_001002030.1. [Q9NTX5-2]
DR RefSeq; NP_001099014.1; NM_001105544.1. [Q9NTX5-3]
DR RefSeq; NP_001099015.1; NM_001105545.1. [Q9NTX5-4]
DR RefSeq; NP_001132982.1; NM_001139510.1. [Q9NTX5-1]
DR RefSeq; NP_060949.2; NM_018479.3. [Q9NTX5-5]
DR RefSeq; XP_005267104.1; XM_005267047.2. [Q9NTX5-2]
DR RefSeq; XP_005267105.1; XM_005267048.1. [Q9NTX5-2]
DR RefSeq; XP_005267107.1; XM_005267050.2. [Q9NTX5-5]
DR RefSeq; XP_016866545.1; XM_017011056.1. [Q9NTX5-3]
DR AlphaFoldDB; Q9NTX5; -.
DR SMR; Q9NTX5; -.
DR BioGRID; 120964; 75.
DR IntAct; Q9NTX5; 13.
DR STRING; 9606.ENSP00000436585; -.
DR GlyGen; Q9NTX5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NTX5; -.
DR PhosphoSitePlus; Q9NTX5; -.
DR BioMuta; ECHDC1; -.
DR DMDM; 124007138; -.
DR EPD; Q9NTX5; -.
DR jPOST; Q9NTX5; -.
DR MassIVE; Q9NTX5; -.
DR MaxQB; Q9NTX5; -.
DR PaxDb; Q9NTX5; -.
DR PeptideAtlas; Q9NTX5; -.
DR PRIDE; Q9NTX5; -.
DR ProteomicsDB; 82636; -. [Q9NTX5-1]
DR ProteomicsDB; 82637; -. [Q9NTX5-2]
DR ProteomicsDB; 82638; -. [Q9NTX5-3]
DR ProteomicsDB; 82639; -. [Q9NTX5-4]
DR ProteomicsDB; 82640; -. [Q9NTX5-5]
DR ProteomicsDB; 82641; -. [Q9NTX5-6]
DR Antibodypedia; 32755; 137 antibodies from 20 providers.
DR DNASU; 55862; -.
DR Ensembl; ENST00000368289.6; ENSP00000357272.2; ENSG00000093144.19. [Q9NTX5-5]
DR Ensembl; ENST00000368291.6; ENSP00000357274.2; ENSG00000093144.19. [Q9NTX5-5]
DR Ensembl; ENST00000430841.6; ENSP00000402492.2; ENSG00000093144.19. [Q9NTX5-2]
DR Ensembl; ENST00000454591.6; ENSP00000404866.2; ENSG00000093144.19. [Q9NTX5-3]
DR Ensembl; ENST00000454859.8; ENSP00000401751.3; ENSG00000093144.19. [Q9NTX5-2]
DR Ensembl; ENST00000474289.6; ENSP00000434908.1; ENSG00000093144.19. [Q9NTX5-2]
DR Ensembl; ENST00000528402.5; ENSP00000436109.1; ENSG00000093144.19. [Q9NTX5-4]
DR Ensembl; ENST00000531967.5; ENSP00000436585.1; ENSG00000093144.19. [Q9NTX5-1]
DR GeneID; 55862; -.
DR KEGG; hsa:55862; -.
DR MANE-Select; ENST00000454859.8; ENSP00000401751.3; NM_001002030.2; NP_001002030.1. [Q9NTX5-2]
DR UCSC; uc003qax.4; human. [Q9NTX5-1]
DR CTD; 55862; -.
DR DisGeNET; 55862; -.
DR GeneCards; ECHDC1; -.
DR HGNC; HGNC:21489; ECHDC1.
DR HPA; ENSG00000093144; Low tissue specificity.
DR MIM; 612136; gene.
DR neXtProt; NX_Q9NTX5; -.
DR OpenTargets; ENSG00000093144; -.
DR PharmGKB; PA134871524; -.
DR VEuPathDB; HostDB:ENSG00000093144; -.
DR eggNOG; KOG1680; Eukaryota.
DR GeneTree; ENSGT00880000138038; -.
DR HOGENOM; CLU_2757120_0_0_1; -.
DR InParanoid; Q9NTX5; -.
DR OMA; HKQMGLV; -.
DR OrthoDB; 1234730at2759; -.
DR PhylomeDB; Q9NTX5; -.
DR TreeFam; TF315986; -.
DR BRENDA; 4.1.1.94; 2681.
DR PathwayCommons; Q9NTX5; -.
DR SignaLink; Q9NTX5; -.
DR BioGRID-ORCS; 55862; 9 hits in 1076 CRISPR screens.
DR ChiTaRS; ECHDC1; human.
DR GenomeRNAi; 55862; -.
DR Pharos; Q9NTX5; Tbio.
DR PRO; PR:Q9NTX5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NTX5; protein.
DR Bgee; ENSG00000093144; Expressed in pigmented layer of retina and 197 other tissues.
DR ExpressionAtlas; Q9NTX5; baseline and differential.
DR Genevisible; Q9NTX5; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016831; F:carboxy-lyase activity; ISS:UniProtKB.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Lyase; Reference proteome.
FT CHAIN 1..307
FT /note="Ethylmalonyl-CoA decarboxylase"
FT /id="PRO_0000273246"
FT MOD_RES 217
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D9V3"
FT MOD_RES 217
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D9V3"
FT MOD_RES 301
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D9V3"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_042581"
FT VAR_SEQ 1..6
FT /note="Missing (in isoform 2, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.4"
FT /id="VSP_022498"
FT VAR_SEQ 125..144
FT /note="TPEDGMAVCMFMQNTLTRFM -> LQR (in isoform 6)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_042582"
FT VAR_SEQ 128..307
FT /note="DGMAVCMFMQNTLTRFMRLPLISVALVQGWALGGGAEFTTACDFRLMTPESK
FT IRFVHKEMGIIPSWGGTTRLVEIIGSRQALKVLSGALKLDSKNALNIGMVEEVLQSSDE
FT TKSLEEAQEWLKQFIQGPPEVIRALKKSVCSGRELYLEEALQNERDLLGTVWGGPANLE
FT AIAKKGKFNK -> TSFNKCCAGSRLGIGWRSRIYYSM (in isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_042583"
FT CONFLICT 243
FT /note="E -> G (in Ref. 3; BAH14056)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="L -> M (in Ref. 3; BAH14056)"
FT /evidence="ECO:0000305"
FT INIT_MET Q9NTX5-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q9NTX5-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT INIT_MET Q9NTX5-5:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q9NTX5-5:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT INIT_MET Q9NTX5-6:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q9NTX5-6:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
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
