ID PECR_HUMAN Reviewed; 303 AA. AC Q9BY49; B2RE42; Q53TC4; Q6IAK9; Q9NRD4; Q9NY60; Q9P1A4; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 22-FEB-2023, entry version 178. DE RecName: Full=Peroxisomal trans-2-enoyl-CoA reductase {ECO:0000305}; DE Short=TERP; DE EC=1.3.1.38 {ECO:0000269|PubMed:10811639}; DE AltName: Full=2,4-dienoyl-CoA reductase-related protein; DE Short=DCR-RP; DE AltName: Full=HPDHase; DE AltName: Full=Short chain dehydrogenase/reductase family 29C member 1; DE AltName: Full=pVI-ARL; GN Name=PECR {ECO:0000312|HGNC:HGNC:18281}; Synonyms=SDR29C1; GN ORFNames=PRO1004; 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 [MRNA] (ISOFORM 1), ENZYME ACTIVITY, CATALYTIC RP ACTIVITY, AND FUNCTION. RX PubMed=10811639; DOI=10.1074/jbc.m001168200; RA Das A.K., Uhler M.D., Hajra A.K.; RT "Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl- RT coenzyme A reductase cDNAs."; RL J. Biol. Chem. 275:24333-24340(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION RP WITH PEX5, AND MUTAGENESIS OF LEU-303. RX PubMed=11669066; DOI=10.2174/1386207013330832; RA Amery L., Mannaerts G.P., Subramani S., Van Veldhoven P.P., Fransen M.; RT "Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase RT related protein using the M13 phage protein VI phage display technology."; RL Comb. Chem. High Throughput Screen. 4:545-552(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.; RT "A novel gene expressed in human liver non-tumor tissues."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.; RT "Functional prediction of the coding sequences of 79 new genes deduced by RT analysis of cDNA clones from human fetal liver."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=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 [9] RP INDUCTION. RX PubMed=11937624; DOI=10.1093/nar/30.8.1713; RA Braastad C.D., Leguia M., Hendrickson E.A.; RT "Ku86 autoantigen related protein-1 transcription initiates from a CpG RT island and is induced by p53 through a nearby p53 response element."; RL Nucleic Acids Res. 30:1713-1724(2002). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND TYR-179, AND 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 [11] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADENINE AND RP PHOSPHATE. RG Structural genomics consortium (SGC); RT "Crystal structure of peroxisomal trans 2-enoyl CoA reductase (PECRA)."; RL Submitted (MAY-2005) to the PDB data bank. CC -!- FUNCTION: Participates in chain elongation of fatty acids. Catalyzes CC the reduction of trans-2-enoyl-CoAs of varying chain lengths from 6:1 CC to 16:1, having maximum activity with 10:1 CoA. Has no 2,4-dienoyl-CoA CC reductase activity. {ECO:0000269|PubMed:10811639}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (2E)-enoyl-CoA + H(+) + NADPH = a 2,3-saturated acyl-CoA + CC NADP(+); Xref=Rhea:RHEA:33763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.1.38; CC Evidence={ECO:0000269|PubMed:10811639}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33764; CC Evidence={ECO:0000305|PubMed:10811639}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-decenoyl-CoA + H(+) + NADPH = decanoyl-CoA + NADP(+); CC Xref=Rhea:RHEA:44960, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:61406, ChEBI:CHEBI:61430; CC Evidence={ECO:0000269|PubMed:10811639}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44961; CC Evidence={ECO:0000305|PubMed:10811639}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-hexenoyl-CoA + H(+) + NADPH = hexanoyl-CoA + NADP(+); CC Xref=Rhea:RHEA:44956, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620; CC Evidence={ECO:0000250|UniProtKB:Q9JIF5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44957; CC Evidence={ECO:0000250|UniProtKB:Q9JIF5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-octenoyl-CoA + H(+) + NADPH = NADP(+) + octanoyl-CoA; CC Xref=Rhea:RHEA:44952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62242; CC Evidence={ECO:0000250|UniProtKB:Q9JIF5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44953; CC Evidence={ECO:0000250|UniProtKB:Q9JIF5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-dodecenoyl-CoA + H(+) + NADPH = dodecanoyl-CoA + NADP(+); CC Xref=Rhea:RHEA:44964, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, CC ChEBI:CHEBI:57375, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC Evidence={ECO:0000250|UniProtKB:Q9JIF5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44965; CC Evidence={ECO:0000250|UniProtKB:Q9JIF5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-tetradecenoyl-CoA + H(+) + NADPH = NADP(+) + CC tetradecanoyl-CoA; Xref=Rhea:RHEA:44968, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57385, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:61405; Evidence={ECO:0000250|UniProtKB:Q9JIF5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44969; CC Evidence={ECO:0000250|UniProtKB:Q9JIF5}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000269|PubMed:10811639}. CC -!- SUBUNIT: Interacts with PEX5, probably required to target it into CC peroxisomes. {ECO:0000269|PubMed:11669066, ECO:0000269|Ref.11}. CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11669066}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BY49-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BY49-2; Sequence=VSP_013260; CC -!- INDUCTION: Not induced by IR. {ECO:0000269|PubMed:11937624}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF232009; AAF69798.1; -; mRNA. DR EMBL; AJ250303; CAB89810.1; -; mRNA. DR EMBL; AF212234; AAK14920.1; -; mRNA. DR EMBL; AF119841; AAF69595.1; -; mRNA. DR EMBL; CR457145; CAG33426.1; -; mRNA. DR EMBL; AK315795; BAG38139.1; -; mRNA. DR EMBL; AC010686; AAY14657.1; -; Genomic_DNA. DR EMBL; BC002529; AAH02529.1; -; mRNA. DR CCDS; CCDS33375.1; -. [Q9BY49-1] DR RefSeq; NP_060911.2; NM_018441.5. [Q9BY49-1] DR RefSeq; XP_011509780.1; XM_011511478.2. DR PDB; 1YXM; X-ray; 1.90 A; A/B/C/D=1-303. DR PDBsum; 1YXM; -. DR AlphaFoldDB; Q9BY49; -. DR SMR; Q9BY49; -. DR BioGRID; 120932; 23. DR IntAct; Q9BY49; 15. DR STRING; 9606.ENSP00000265322; -. DR DrugBank; DB00173; Adenine. DR SwissLipids; SLP:000001094; -. DR iPTMnet; Q9BY49; -. DR PhosphoSitePlus; Q9BY49; -. DR BioMuta; PECR; -. DR DMDM; 62287123; -. DR EPD; Q9BY49; -. DR jPOST; Q9BY49; -. DR MassIVE; Q9BY49; -. DR MaxQB; Q9BY49; -. DR PaxDb; Q9BY49; -. DR PeptideAtlas; Q9BY49; -. DR ProteomicsDB; 79584; -. [Q9BY49-1] DR ProteomicsDB; 79585; -. [Q9BY49-2] DR Antibodypedia; 20074; 204 antibodies from 27 providers. DR DNASU; 55825; -. DR Ensembl; ENST00000265322.8; ENSP00000265322.7; ENSG00000115425.14. [Q9BY49-1] DR GeneID; 55825; -. DR KEGG; hsa:55825; -. DR MANE-Select; ENST00000265322.8; ENSP00000265322.7; NM_018441.6; NP_060911.2. DR UCSC; uc002vft.4; human. [Q9BY49-1] DR AGR; HGNC:18281; -. DR CTD; 55825; -. DR DisGeNET; 55825; -. DR GeneCards; PECR; -. DR HGNC; HGNC:18281; PECR. DR HPA; ENSG00000115425; Tissue enriched (liver). DR MIM; 605843; gene. DR neXtProt; NX_Q9BY49; -. DR OpenTargets; ENSG00000115425; -. DR PharmGKB; PA134967510; -. DR VEuPathDB; HostDB:ENSG00000115425; -. DR eggNOG; KOG0725; Eukaryota. DR GeneTree; ENSGT00940000156882; -. DR HOGENOM; CLU_010194_1_2_1; -. DR InParanoid; Q9BY49; -. DR OMA; RIWDSKV; -. DR OrthoDB; 2731281at2759; -. DR PhylomeDB; Q9BY49; -. DR TreeFam; TF315256; -. DR BioCyc; MetaCyc:HS03889-MON; -. DR BRENDA; 1.3.1.38; 2681. DR PathwayCommons; Q9BY49; -. DR Reactome; R-HSA-389599; Alpha-oxidation of phytanate. DR Reactome; R-HSA-9033241; Peroxisomal protein import. DR SignaLink; Q9BY49; -. DR UniPathway; UPA00094; -. DR BioGRID-ORCS; 55825; 12 hits in 1158 CRISPR screens. DR ChiTaRS; PECR; human. DR EvolutionaryTrace; Q9BY49; -. DR GeneWiki; PECR; -. DR GenomeRNAi; 55825; -. DR Pharos; Q9BY49; Tbio. DR PRO; PR:Q9BY49; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9BY49; protein. DR Bgee; ENSG00000115425; Expressed in renal medulla and 191 other tissues. DR ExpressionAtlas; Q9BY49; baseline and differential. DR Genevisible; Q9BY49; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IDA:UniProtKB. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0033306; P:phytol metabolic process; IDA:UniProtKB. DR CDD; cd05369; TER_DECR_SDR_a; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24317; PEROXISOMAL TRANS-2-ENOYL-COA REDUCTASE; 1. DR PANTHER; PTHR24317:SF7; PEROXISOMAL TRANS-2-ENOYL-COA REDUCTASE; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; NADP; KW Oxidoreductase; Peroxisome; Phosphoprotein; Reference proteome. FT CHAIN 1..303 FT /note="Peroxisomal trans-2-enoyl-CoA reductase" FT /id="PRO_0000054740" FT MOTIF 301..303 FT /note="Microbody targeting signal" FT ACT_SITE 179 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 23..47 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT MOD_RES 32 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99MZ7" FT MOD_RES 49 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 179 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..146 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5" FT /id="VSP_013260" FT VARIANT 149 FT /note="E -> K (in dbSNP:rs1429148)" FT /id="VAR_021535" FT VARIANT 297 FT /note="F -> L (in dbSNP:rs9288513)" FT /id="VAR_021536" FT MUTAGEN 303 FT /note="Missing: Abolishes localization to peroxisomes." FT /evidence="ECO:0000269|PubMed:11669066" FT CONFLICT 22 FT /note="I -> F (in Ref. 2; CAB89810)" FT /evidence="ECO:0000305" FT CONFLICT 129 FT /note="E -> R (in Ref. 2; CAB89810)" FT /evidence="ECO:0000305" FT CONFLICT 135 FT /note="T -> S (in Ref. 2; CAB89810)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="S -> P (in Ref. 5; CAG33426)" FT /evidence="ECO:0000305" FT TURN 13..18 FT /evidence="ECO:0007829|PDB:1YXM" FT STRAND 20..24 FT /evidence="ECO:0007829|PDB:1YXM" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 29..40 FT /evidence="ECO:0007829|PDB:1YXM" FT STRAND 44..50 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 52..64 FT /evidence="ECO:0007829|PDB:1YXM" FT STRAND 74..78 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 84..98 FT /evidence="ECO:0007829|PDB:1YXM" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 121..131 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 133..145 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 147..150 FT /evidence="ECO:0007829|PDB:1YXM" FT STRAND 152..157 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 169..188 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:1YXM" FT STRAND 194..201 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 214..221 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 224..227 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 237..247 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:1YXM" FT STRAND 258..262 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 265..267 FT /evidence="ECO:0007829|PDB:1YXM" FT HELIX 288..302 FT /evidence="ECO:0007829|PDB:1YXM" SQ SEQUENCE 303 AA; 32544 MW; BCCE6AB89F58382C CRC64; MASWAKGRSY LAPGLLQGQV AIVTGGATGI GKAIVKELLE LGSNVVIASR KLERLKSAAD ELQANLPPTK QARVIPIQCN IRNEEEVNNL VKSTLDTFGK INFLVNNGGG QFLSPAEHIS SKGWHAVLET NLTGTFYMCK AVYSSWMKEH GGSIVNIIVP TKAGFPLAVH SGAARAGVYN LTKSLALEWA CSGIRINCVA PGVIYSQTAV ENYGSWGQSF FEGSFQKIPA KRIGVPEEVS SVVCFLLSPA ASFITGQSVD VDGGRSLYTH SYEVPDHDNW PKGAGDLSVV KKMKETFKEK AKL //