ECI1_HUMAN
ID ECI1_HUMAN Reviewed; 302 AA.
AC P42126; A8K512; Q13290; Q7Z2L6; Q7Z2L7; Q9BUB8; Q9BW05; Q9UDG6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Enoyl-CoA delta isomerase 1, mitochondrial;
DE EC=5.3.3.8;
DE AltName: Full=3,2-trans-enoyl-CoA isomerase;
DE AltName: Full=Delta(3),Delta(2)-enoyl-CoA isomerase;
DE Short=D3,D2-enoyl-CoA isomerase;
DE AltName: Full=Dodecenoyl-CoA isomerase;
DE Flags: Precursor;
GN Name=ECI1; Synonyms=DCI;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Liver, and Placenta;
RX PubMed=7829074; DOI=10.1006/geno.1994.1480;
RA Janssen U., Fink T., Lichter P., Stoffel W.;
RT "Human mitochondrial 3,2-trans-enoyl-CoA isomerase (DCI): gene structure
RT and localization to chromosome 16p13.3.";
RL Genomics 23:223-228(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-302 (ISOFORM 1).
RX PubMed=8198519; DOI=10.1042/bj3000001;
RA Kilponen J.M., Haeyrinen H.M., Rehn M.V., Hiltunen K.J.;
RT "cDNA cloning and amino acid sequence of human mitochondrial delta 3 delta
RT 2-enoyl-CoA isomerase: comparison of the human enzyme with its rat
RT counterpart, mitochondrial short-chain isomerase.";
RL Biochem. J. 300:1-5(1994).
RN [6]
RP PROTEIN SEQUENCE OF 42-84; 89-116; 190-220; 242-255 AND 288-298, CATALYTIC
RP ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=7818490; DOI=10.1042/bj3040849;
RA Takahashi Y., Hirata Y., Burstein Y., Listowsky I.;
RT "Delta 3, delta 2-enoyl-CoA isomerase is the protein that copurifies with
RT human glutathione S-transferases from S-hexylglutathione affinity
RT matrices.";
RL Biochem. J. 304:849-852(1994).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
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 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 [10]
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).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 43-302 IN COMPLEX WITH
RP OCTANOYL-COENZYME A, SUBUNIT, AND MUTAGENESIS OF GLU-178.
RX PubMed=15351645; DOI=10.1016/j.jmb.2004.07.039;
RA Partanen S.T., Novikov D.K., Popov A.N., Mursula A.M., Hiltunen J.K.,
RA Wierenga R.K.;
RT "The 1.3 A crystal structure of human mitochondrial Delta3-Delta2-enoyl-CoA
RT isomerase shows a novel mode of binding for the fatty acyl group.";
RL J. Mol. Biol. 342:1197-1208(2004).
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.
CC {ECO:0000269|PubMed:7818490}.
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:7818490};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45901;
CC Evidence={ECO:0000305|PubMed:7818490};
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:7818490};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229;
CC Evidence={ECO:0000305|PubMed:7818490};
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:0000269|PubMed:7818490};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46045;
CC Evidence={ECO:0000305|PubMed:7818490};
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:P23965};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29849;
CC Evidence={ECO:0000250|UniProtKB:P23965};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:7818490}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:15351645}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P23965}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P42126-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42126-2; Sequence=VSP_001358;
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level).
CC {ECO:0000269|PubMed:7818490}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; Z25820; CAA81065.1; -; mRNA.
DR EMBL; Z25821; CAA81066.1; -; Genomic_DNA.
DR EMBL; Z25822; CAA81066.1; JOINED; Genomic_DNA.
DR EMBL; Z25823; CAA81066.1; JOINED; Genomic_DNA.
DR EMBL; Z25824; CAA81066.1; JOINED; Genomic_DNA.
DR EMBL; AK291127; BAF83816.1; -; mRNA.
DR EMBL; CH471112; EAW85524.1; -; Genomic_DNA.
DR EMBL; BC000762; AAH00762.1; -; mRNA.
DR EMBL; BC002746; AAH02746.1; -; mRNA.
DR EMBL; BC020228; AAH20228.1; -; mRNA.
DR EMBL; BC019316; AAH19316.1; -; mRNA.
DR EMBL; L24774; AAA35485.1; -; mRNA.
DR CCDS; CCDS10464.1; -. [P42126-1]
DR CCDS; CCDS58410.1; -. [P42126-2]
DR PIR; A55723; A55723.
DR RefSeq; NP_001171500.1; NM_001178029.1. [P42126-2]
DR RefSeq; NP_001910.2; NM_001919.3. [P42126-1]
DR PDB; 1SG4; X-ray; 1.30 A; A/B/C=43-302.
DR PDBsum; 1SG4; -.
DR AlphaFoldDB; P42126; -.
DR SMR; P42126; -.
DR BioGRID; 108000; 42.
DR IntAct; P42126; 10.
DR MINT; P42126; -.
DR STRING; 9606.ENSP00000301729; -.
DR DrugBank; DB03127; Benzamidine.
DR DrugBank; DB02910; Octanoyl-Coenzyme A.
DR SwissLipids; SLP:000001184; -.
DR iPTMnet; P42126; -.
DR PhosphoSitePlus; P42126; -.
DR SwissPalm; P42126; -.
DR BioMuta; ECI1; -.
DR DMDM; 1169204; -.
DR OGP; P42126; -.
DR EPD; P42126; -.
DR jPOST; P42126; -.
DR MassIVE; P42126; -.
DR MaxQB; P42126; -.
DR PaxDb; P42126; -.
DR PeptideAtlas; P42126; -.
DR PRIDE; P42126; -.
DR ProteomicsDB; 55485; -. [P42126-1]
DR ProteomicsDB; 55486; -. [P42126-2]
DR TopDownProteomics; P42126-1; -. [P42126-1]
DR TopDownProteomics; P42126-2; -. [P42126-2]
DR Antibodypedia; 23677; 286 antibodies from 31 providers.
DR DNASU; 1632; -.
DR Ensembl; ENST00000301729.9; ENSP00000301729.4; ENSG00000167969.13. [P42126-1]
DR Ensembl; ENST00000562238.5; ENSP00000456319.1; ENSG00000167969.13. [P42126-2]
DR GeneID; 1632; -.
DR KEGG; hsa:1632; -.
DR MANE-Select; ENST00000301729.9; ENSP00000301729.4; NM_001919.4; NP_001910.2.
DR UCSC; uc002cpr.4; human. [P42126-1]
DR CTD; 1632; -.
DR DisGeNET; 1632; -.
DR GeneCards; ECI1; -.
DR HGNC; HGNC:2703; ECI1.
DR HPA; ENSG00000167969; Low tissue specificity.
DR MIM; 600305; gene.
DR neXtProt; NX_P42126; -.
DR OpenTargets; ENSG00000167969; -.
DR PharmGKB; PA27173; -.
DR VEuPathDB; HostDB:ENSG00000167969; -.
DR eggNOG; KOG1683; Eukaryota.
DR GeneTree; ENSGT00390000005678; -.
DR InParanoid; P42126; -.
DR OMA; WFMSSFL; -.
DR OrthoDB; 974911at2759; -.
DR PhylomeDB; P42126; -.
DR TreeFam; TF314436; -.
DR BRENDA; 5.3.3.8; 2681.
DR PathwayCommons; P42126; -.
DR Reactome; R-HSA-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
DR SignaLink; P42126; -.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 1632; 13 hits in 1075 CRISPR screens.
DR ChiTaRS; ECI1; human.
DR EvolutionaryTrace; P42126; -.
DR GenomeRNAi; 1632; -.
DR Pharos; P42126; Tbio.
DR PRO; PR:P42126; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P42126; protein.
DR Bgee; ENSG00000167969; Expressed in apex of heart and 191 other tissues.
DR ExpressionAtlas; P42126; baseline and differential.
DR Genevisible; P42126; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; ISS:UniProtKB.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0016863; F:intramolecular oxidoreductase activity, transposing C=C bonds; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
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 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Fatty acid metabolism; Isomerase; Lipid metabolism; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 42..302
FT /note="Enoyl-CoA delta isomerase 1, mitochondrial"
FT /id="PRO_0000007420"
FT BINDING 106..110
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15351645,
FT ECO:0007744|PDB:1SG4"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15351645,
FT ECO:0007744|PDB:1SG4"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15351645,
FT ECO:0007744|PDB:1SG4"
FT SITE 178
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:15351645"
FT MOD_RES 61
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 61
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 84
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 89
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 283
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 283
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT MOD_RES 288
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42125"
FT VAR_SEQ 172..188
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001358"
FT MUTAGEN 178
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15351645"
FT CONFLICT 14
FT /note="L -> P (in Ref. 4; AAH00762/AAH19316)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="R -> P (in Ref. 1; CAA81065)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="S -> C (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="G -> A (in Ref. 1; CAA81065)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="L -> F (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="G -> V (in Ref. 5; AAA35485)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="Missing (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..193
FT /note="TL -> PY (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..207
FT /note="RALQ -> SAPE (in Ref. 5; AAA35485)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="L -> S (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 213..215
FT /note="PPA -> RRP (in Ref. 5; AAA35485)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="Q -> K (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="A -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="D -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="Q -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1SG4"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:1SG4"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1SG4"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 72..87
FT /evidence="ECO:0007829|PDB:1SG4"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:1SG4"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 118..136
FT /evidence="ECO:0007829|PDB:1SG4"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:1SG4"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:1SG4"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:1SG4"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 248..267
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 284..290
FT /evidence="ECO:0007829|PDB:1SG4"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:1SG4"
SQ SEQUENCE 302 AA; 32816 MW; 6E63827DE9BE886B CRC64;
MALVASVRVP ARVLLRAGAR LPGAALGRTE RAAGGGDGAR RFGSQRVLVE PDAGAGVAVM
KFKNPPVNSL SLEFLTELVI SLEKLENDKS FRGVILTSDR PGVFSAGLDL TEMCGRSPAH
YAGYWKAVQE LWLRLYQSNL VLVSAINGAC PAGGCLVALT CDYRILADNP RYCIGLNETQ
LGIIAPFWLK DTLENTIGHR AAERALQLGL LFPPAEALQV GIVDQVVPEE QVQSTALSAI
AQWMAIPDHA RQLTKAMMRK ATASRLVTQR DADVQNFVSF ISKDSIQKSL QMYLERLKEE
KG
