PECR_HUMAN
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 03-AUG-2022, entry version 175.
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}.
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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 PRIDE; Q9BY49; -.
DR ProteomicsDB; 79584; -. [Q9BY49-1]
DR ProteomicsDB; 79585; -. [Q9BY49-2]
DR Antibodypedia; 20074; 203 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 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; 1194344at2759; -.
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; 11 hits in 1077 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 InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 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
