ID ECI2_MOUSE Reviewed; 391 AA.
AC Q9WUR2; Q99M61; Q9D785;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Enoyl-CoA delta isomerase 2;
DE EC=5.3.3.8 {ECO:0000269|PubMed:24344334};
DE AltName: Full=Delta(3),delta(2)-enoyl-CoA isomerase;
DE Short=D3,D2-enoyl-CoA isomerase;
DE AltName: Full=Dodecenoyl-CoA isomerase;
DE AltName: Full=Peroxisomal 3,2-trans-enoyl-CoA isomerase {ECO:0000303|PubMed:10419495};
DE Short=pECI {ECO:0000303|PubMed:10419495};
DE Flags: Precursor;
GN Name=Eci2 {ECO:0000312|MGI:MGI:1346064};
GN Synonyms=Peci {ECO:0000303|PubMed:10419495};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10419495; DOI=10.1074/jbc.274.31.21797;
RA Geisbrecht B.V., Zhang D., Schulz H., Gould S.J.;
RT "Characterization of PECI, a novel monofunctional D3,D2-enoyl-CoA isomerase
RT of mammalian peroxisomes.";
RL J. Biol. Chem. 274:21797-21803(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-391 (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-49; LYS-53; LYS-60; LYS-68; LYS-79; LYS-88; LYS-90;
RP LYS-127; LYS-159 AND LYS-286, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60 AND LYS-90, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24344334; DOI=10.1096/fj.13-240416;
RA van Weeghel M., Ofman R., Argmann C.A., Ruiter J.P., Claessen N.,
RA Oussoren S.V., Wanders R.J., Aten J., Houten S.M.;
RT "Identification and characterization of Eci3, a murine kidney-specific
RT Delta3,Delta2-enoyl-CoA isomerase.";
RL FASEB J. 28:1365-1374(2014).
CC -!- FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into
CC the 2-trans form in a range of enoyl-CoA species (PubMed:24344334). Has
CC a preference for 3-trans substrates (By similarity).
CC {ECO:0000250|UniProtKB:Q5XIC0, ECO:0000269|PubMed:24344334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC EC=5.3.3.8; Evidence={ECO:0000269|PubMed:24344334};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45901;
CC Evidence={ECO:0000305|PubMed:24344334};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC EC=5.3.3.8; Evidence={ECO:0000269|PubMed:24344334};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229;
CC Evidence={ECO:0000305|PubMed:24344334};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E)-nonenoyl-CoA = (2E)-nonenoyl-CoA; Xref=Rhea:RHEA:46068,
CC ChEBI:CHEBI:76292, ChEBI:CHEBI:85655;
CC Evidence={ECO:0000269|PubMed:24344334};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46069;
CC Evidence={ECO:0000305|PubMed:24344334};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-tetradecenoyl-CoA = (3Z)-tetradecenoyl-CoA;
CC Xref=Rhea:RHEA:29847, ChEBI:CHEBI:61405, ChEBI:CHEBI:61968;
CC Evidence={ECO:0000250|UniProtKB:Q5XIC0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29849;
CC Evidence={ECO:0000250|UniProtKB:Q5XIC0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E)-tetradecenoyl-CoA = (2E)-tetradecenoyl-CoA;
CC Xref=Rhea:RHEA:47476, ChEBI:CHEBI:61405, ChEBI:CHEBI:87710;
CC Evidence={ECO:0000250|UniProtKB:Q5XIC0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47477;
CC Evidence={ECO:0000250|UniProtKB:Q5XIC0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E)-octenoyl-CoA = (2E)-octenoyl-CoA; Xref=Rhea:RHEA:49852,
CC ChEBI:CHEBI:62242, ChEBI:CHEBI:131962;
CC Evidence={ECO:0000250|UniProtKB:Q5XIC0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49853;
CC Evidence={ECO:0000250|UniProtKB:Q5XIC0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z)-octenoyl-CoA = (2E)-octenoyl-CoA; Xref=Rhea:RHEA:46044,
CC ChEBI:CHEBI:62242, ChEBI:CHEBI:85640;
CC Evidence={ECO:0000250|UniProtKB:O75521};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46045;
CC Evidence={ECO:0000250|UniProtKB:O75521};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:24344334}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:24344334}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Peroxisome matrix
CC {ECO:0000269|PubMed:24344334}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WUR2-1; Sequence=Displayed;
CC Name=2; Synonyms=PECI {ECO:0000303|PubMed:10419495};
CC IsoId=Q9WUR2-2; Sequence=VSP_037855;
CC -!- TISSUE SPECIFICITY: Expressed in liver and kidney (at protein level).
CC {ECO:0000269|PubMed:24344334}.
CC -!- PTM: Acetylation of Lys-60 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- SIMILARITY: In the C-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01983.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF153613; AAD34174.1; -; mRNA.
DR EMBL; AK009478; BAB26315.2; -; mRNA.
DR EMBL; BC001983; AAH01983.1; ALT_INIT; mRNA.
DR CCDS; CCDS26450.1; -. [Q9WUR2-2]
DR CCDS; CCDS49234.1; -. [Q9WUR2-1]
DR RefSeq; NP_001103801.1; NM_001110331.1. [Q9WUR2-1]
DR RefSeq; NP_035998.2; NM_011868.3. [Q9WUR2-2]
DR RefSeq; XP_006516736.1; XM_006516673.2. [Q9WUR2-2]
DR RefSeq; XP_006516737.1; XM_006516674.2. [Q9WUR2-2]
DR RefSeq; XP_006516738.1; XM_006516675.2. [Q9WUR2-2]
DR RefSeq; XP_006516739.1; XM_006516676.3. [Q9WUR2-2]
DR RefSeq; XP_006516740.1; XM_006516677.1. [Q9WUR2-2]
DR AlphaFoldDB; Q9WUR2; -.
DR SMR; Q9WUR2; -.
DR BioGRID; 204838; 18.
DR IntAct; Q9WUR2; 5.
DR MINT; Q9WUR2; -.
DR STRING; 10090.ENSMUSP00000131735; -.
DR SwissLipids; SLP:000001194; -.
DR GlyGen; Q9WUR2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9WUR2; -.
DR PhosphoSitePlus; Q9WUR2; -.
DR SwissPalm; Q9WUR2; -.
DR EPD; Q9WUR2; -.
DR jPOST; Q9WUR2; -.
DR MaxQB; Q9WUR2; -.
DR PaxDb; 10090-ENSMUSP00000131735; -.
DR PeptideAtlas; Q9WUR2; -.
DR ProteomicsDB; 277713; -. [Q9WUR2-1]
DR ProteomicsDB; 277714; -. [Q9WUR2-2]
DR Pumba; Q9WUR2; -.
DR Ensembl; ENSMUST00000021854.14; ENSMUSP00000021854.7; ENSMUSG00000021417.16. [Q9WUR2-2]
DR Ensembl; ENSMUST00000171229.8; ENSMUSP00000131735.2; ENSMUSG00000021417.16. [Q9WUR2-1]
DR Ensembl; ENSMUST00000178421.8; ENSMUSP00000137411.2; ENSMUSG00000021417.16. [Q9WUR2-2]
DR GeneID; 23986; -.
DR KEGG; mmu:23986; -.
DR UCSC; uc007qbx.3; mouse. [Q9WUR2-1]
DR AGR; MGI:1346064; -.
DR CTD; 10455; -.
DR MGI; MGI:1346064; Eci2.
DR VEuPathDB; HostDB:ENSMUSG00000021417; -.
DR eggNOG; KOG0016; Eukaryota.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000155105; -.
DR HOGENOM; CLU_009834_7_2_1; -.
DR InParanoid; Q9WUR2; -.
DR OMA; LHCDFVY; -.
DR OrthoDB; 553487at2759; -.
DR PhylomeDB; Q9WUR2; -.
DR TreeFam; TF313375; -.
DR Reactome; R-MMU-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 23986; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Eci2; mouse.
DR PRO; PR:Q9WUR2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9WUR2; Protein.
DR Bgee; ENSMUSG00000021417; Expressed in saccule of membranous labyrinth and 274 other cell types or tissues.
DR ExpressionAtlas; Q9WUR2; baseline and differential.
DR Genevisible; Q9WUR2; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:MGI.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR GO; GO:0016863; F:intramolecular oxidoreductase activity, transposing C=C bonds; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0009062; P:fatty acid catabolic process; ISS:UniProtKB.
DR CDD; cd00435; ACBP; 1.
DR CDD; cd06558; crotonase-like; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1.
DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR PANTHER; PTHR43684; -; 1.
DR PANTHER; PTHR43684:SF1; ENOYL-COA DELTA ISOMERASE 2; 1.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF00378; ECH_1; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isomerase; Mitochondrion; Peroxisome;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..391
FT /note="Enoyl-CoA delta isomerase 2"
FT /id="PRO_0000214028"
FT DOMAIN 37..122
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 116..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..319
FT /note="ECH-like"
FT MOTIF 389..391
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 64..68
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 196..200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q05871"
FT SITE 277
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q05871"
FT MOD_RES 49
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75521"
FT MOD_RES 49
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 53
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 60
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 60
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 68
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 79
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 88
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 90
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 90
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75521"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75521"
FT MOD_RES 127
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 159
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 286
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10419495"
FT /id="VSP_037855"
FT CONFLICT 35
FT /note="R -> K (in Ref. 2; BAB26315)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="R -> C (in Ref. 3; AAH01983)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="R -> Q (in Ref. 3; AAH01983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 43268 MW; 0B93D3908DF77AF8 CRC64;
MAAVTWSRAR CWCPSVLQVF RLQVAKLHLG RPTMRASQQD FENALNQVKL LKKDPGNEVK
LRLYALYKQA TEGPCNMPKP GMLDFVNKAK WDAWNALGSL PKETARQNYV DLVSSLSSSS
EAPSQGKRGA DEKARESKDI LVTSEDGITK ITFNRPTKKN AISFQMYRDI ILALKNASTD
NTVMAVFTGT GDYYCSGNDL TNFTSATGGI EEAASNGAVL LRDFVNSFID FPKPLVAVVN
GPAVGISVTL LGLFDAVFAS DRATFHTPFS QLGQSPEACS SYTFPKMMGS AKAAEMLLFG
KKLTAREAWA QGLVTEVFPE STFETEVWTR LKTYAKLPPN AMRISKELIR KNEKEKLYAV
NAEECTTLQA RWLSEECMNA IMSFVSRKPK L
//
