ID PTGR2_HUMAN Reviewed; 351 AA.
AC Q8N8N7; Q3L8A4; Q6MZH8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 175.
DE RecName: Full=Prostaglandin reductase 2 {ECO:0000305};
DE Short=PRG-2;
DE EC=1.3.1.48 {ECO:0000269|PubMed:19000823};
DE AltName: Full=15-oxoprostaglandin 13-reductase;
DE AltName: Full=Zinc-binding alcohol dehydrogenase domain-containing protein 1;
GN Name=PTGR2 {ECO:0000312|HGNC:HGNC:20149}; Synonyms=ZADH1;
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), TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RX PubMed=15004468; DOI=10.1159/000076293;
RA Zhang L., Zhang F., Huo K.;
RT "Cloning and characterization of a novel splicing variant of the ZADH1
RT gene.";
RL Cytogenet. Genome Res. 103:79-83(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zheng H., Xie Y., Mao Y.;
RT "Cloning and characterization of a putative dehydrogenase.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
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 [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
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 [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEXES WITH NADPH;
RP 15-KETO-PGE2 AND INDOMETHACIN, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-64 AND TYR-259.
RX PubMed=19000823; DOI=10.1016/j.str.2008.09.007;
RA Wu Y.H., Ko T.P., Guo R.T., Hu S.M., Chuang L.M., Wang A.H.;
RT "Structural basis for catalytic and inhibitory mechanisms of human
RT prostaglandin reductase PTGR2.";
RL Structure 16:1714-1723(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS
RP AND NADP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human zinc-binding alcohol dehydrogenase 1.";
RL Submitted (JAN-2009) to the PDB data bank.
CC -!- FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on
CC 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha
CC with highest activity towards 15-keto-PGE2 (PubMed:19000823).
CC Overexpression represses transcriptional activity of PPARG and inhibits
CC adipocyte differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q8VDQ1, ECO:0000269|PubMed:19000823}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin E2 + NAD(+) = 15-
CC oxoprostaglandin E2 + H(+) + NADH; Xref=Rhea:RHEA:11916,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57402,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.48;
CC Evidence={ECO:0000269|PubMed:19000823};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11918;
CC Evidence={ECO:0000305|PubMed:19000823};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin E2 + NADP(+) = 15-
CC oxoprostaglandin E2 + H(+) + NADPH; Xref=Rhea:RHEA:11912,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57402,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.48;
CC Evidence={ECO:0000269|PubMed:19000823};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11914;
CC Evidence={ECO:0000305|PubMed:19000823};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-PGF2alpha + NADP(+) = 15-oxoprostaglandin
CC F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:50588, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133374,
CC ChEBI:CHEBI:133409; Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-
CC oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:50584,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:133408;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin F1alpha + NADP(+) = 15-
CC oxoprostaglandin F1alpha + H(+) + NADPH; Xref=Rhea:RHEA:50592,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:79072, ChEBI:CHEBI:133411;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594;
CC Evidence={ECO:0000250|UniProtKB:Q8VDQ1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.21 uM for 15-keto-PGE2 {ECO:0000269|PubMed:19000823};
CC KM=15.87 uM for NADPH {ECO:0000269|PubMed:19000823};
CC Vmax=159 nmol/min/mg enzyme for 15-keto-PGE2
CC {ECO:0000269|PubMed:19000823};
CC Vmax=67 nmol/min/mg enzyme for NADPH {ECO:0000269|PubMed:19000823};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8N8N7; Q7L4P6: BEND5; NbExp=3; IntAct=EBI-17614618, EBI-724373;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ZADH1b;
CC IsoId=Q8N8N7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N8N7-2; Sequence=VSP_013526, VSP_013527;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15004468}.
CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC {ECO:0000305}.
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DR EMBL; AY346133; AAR05101.1; -; mRNA.
DR EMBL; AY424308; AAR82927.1; -; mRNA.
DR EMBL; AK096410; BAC04781.1; -; mRNA.
DR EMBL; BX641118; CAE46055.1; -; mRNA.
DR EMBL; CH471061; EAW81132.1; -; Genomic_DNA.
DR EMBL; BC059364; AAH59364.1; -; mRNA.
DR CCDS; CCDS9820.1; -. [Q8N8N7-1]
DR RefSeq; NP_001139626.1; NM_001146154.1. [Q8N8N7-1]
DR RefSeq; NP_001139627.1; NM_001146155.1. [Q8N8N7-1]
DR RefSeq; NP_689657.1; NM_152444.2. [Q8N8N7-1]
DR PDB; 2VNA; X-ray; 2.17 A; A=1-349.
DR PDB; 2W4Q; X-ray; 2.00 A; A=1-349.
DR PDB; 2W98; X-ray; 1.85 A; A/B=1-349.
DR PDB; 2ZB4; X-ray; 1.63 A; A=1-351.
DR PDB; 2ZB7; X-ray; 1.80 A; A=1-351.
DR PDB; 2ZB8; X-ray; 2.00 A; A=1-351.
DR PDBsum; 2VNA; -.
DR PDBsum; 2W4Q; -.
DR PDBsum; 2W98; -.
DR PDBsum; 2ZB4; -.
DR PDBsum; 2ZB7; -.
DR PDBsum; 2ZB8; -.
DR AlphaFoldDB; Q8N8N7; -.
DR SMR; Q8N8N7; -.
DR BioGRID; 126915; 27.
DR IntAct; Q8N8N7; 5.
DR STRING; 9606.ENSP00000452280; -.
DR DrugBank; DB07177; (5E,13E)-11-HYDROXY-9,15-DIOXOPROSTA-5,13-DIEN-1-OIC ACID.
DR DrugBank; DB00328; Indomethacin.
DR SwissLipids; SLP:000001640; -. [Q8N8N7-1]
DR GlyGen; Q8N8N7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N8N7; -.
DR PhosphoSitePlus; Q8N8N7; -.
DR SwissPalm; Q8N8N7; -.
DR BioMuta; PTGR2; -.
DR DMDM; 62901454; -.
DR REPRODUCTION-2DPAGE; IPI00167515; -.
DR EPD; Q8N8N7; -.
DR jPOST; Q8N8N7; -.
DR MassIVE; Q8N8N7; -.
DR MaxQB; Q8N8N7; -.
DR PaxDb; 9606-ENSP00000452280; -.
DR PeptideAtlas; Q8N8N7; -.
DR ProteomicsDB; 72438; -. [Q8N8N7-1]
DR ProteomicsDB; 72439; -. [Q8N8N7-2]
DR Pumba; Q8N8N7; -.
DR Antibodypedia; 30; 252 antibodies from 30 providers.
DR DNASU; 145482; -.
DR Ensembl; ENST00000267568.8; ENSP00000267568.4; ENSG00000140043.12. [Q8N8N7-1]
DR Ensembl; ENST00000555228.5; ENSP00000450975.1; ENSG00000140043.12. [Q8N8N7-1]
DR Ensembl; ENST00000555661.6; ENSP00000452280.1; ENSG00000140043.12. [Q8N8N7-1]
DR GeneID; 145482; -.
DR KEGG; hsa:145482; -.
DR MANE-Select; ENST00000555661.6; ENSP00000452280.1; NM_001146154.2; NP_001139626.1.
DR AGR; HGNC:20149; -.
DR CTD; 145482; -.
DR DisGeNET; 145482; -.
DR GeneCards; PTGR2; -.
DR HGNC; HGNC:20149; PTGR2.
DR HPA; ENSG00000140043; Low tissue specificity.
DR MIM; 608642; gene.
DR neXtProt; NX_Q8N8N7; -.
DR OpenTargets; ENSG00000140043; -.
DR PharmGKB; PA162400323; -.
DR VEuPathDB; HostDB:ENSG00000140043; -.
DR eggNOG; KOG1196; Eukaryota.
DR GeneTree; ENSGT00940000156793; -.
DR HOGENOM; CLU_026673_29_2_1; -.
DR InParanoid; Q8N8N7; -.
DR OMA; EEKCRYA; -.
DR OrthoDB; 179761at2759; -.
DR PhylomeDB; Q8N8N7; -.
DR TreeFam; TF324201; -.
DR BioCyc; MetaCyc:HS06681-MONOMER; -.
DR PathwayCommons; Q8N8N7; -.
DR Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR SABIO-RK; Q8N8N7; -.
DR SignaLink; Q8N8N7; -.
DR BioGRID-ORCS; 145482; 14 hits in 1158 CRISPR screens.
DR ChiTaRS; PTGR2; human.
DR EvolutionaryTrace; Q8N8N7; -.
DR GenomeRNAi; 145482; -.
DR Pharos; Q8N8N7; Tbio.
DR PRO; PR:Q8N8N7; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8N8N7; Protein.
DR Bgee; ENSG00000140043; Expressed in hindlimb stylopod muscle and 160 other cell types or tissues.
DR ExpressionAtlas; Q8N8N7; baseline and differential.
DR Genevisible; Q8N8N7; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036132; F:13-prostaglandin reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; IDA:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
DR CDD; cd08293; PTGR2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR041694; ADH_N_2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR045010; MDR_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR037399; PTGR2.
DR PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR PANTHER; PTHR43205:SF5; PROSTAGLANDIN REDUCTASE 2; 1.
DR Pfam; PF16884; ADH_N_2; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Lipid metabolism; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..351
FT /note="Prostaglandin reductase 2"
FT /id="PRO_0000218070"
FT BINDING 99..100
FT /ligand="substrate"
FT BINDING 165..168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 253..259
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 287..289
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 288..290
FT /ligand="substrate"
FT BINDING 337
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT VAR_SEQ 174..180
FT /note="IGHFLGC -> VNFLRII (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013526"
FT VAR_SEQ 181..351
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013527"
FT MUTAGEN 64
FT /note="Y->F: Increases affinity for 15-keto-PGE2. Reduces
FT affinity for NADP and Vmax."
FT /evidence="ECO:0000269|PubMed:19000823"
FT MUTAGEN 259
FT /note="Y->F: Increases affinity for 15-keto-PGE2. Reduces
FT affinity for NADP and Vmax."
FT /evidence="ECO:0000269|PubMed:19000823"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 95..110
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2W98"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:2ZB4"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2ZB4"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 234..242
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:2ZB4"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:2ZB4"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:2ZB4"
SQ SEQUENCE 351 AA; 38499 MW; 118ED6D2FB984F3A CRC64;
MIVQRVVLNS RPGKNGNPVA ENFRMEEVYL PDNINEGQVQ VRTLYLSVDP YMRCRMNEDT
GTDYITPWQL SQVVDGGGIG IIEESKHTNL TKGDFVTSFY WPWQTKVILD GNSLEKVDPQ
LVDGHLSYFL GAIGMPGLTS LIGIQEKGHI TAGSNKTMVV SGAAGACGSV AGQIGHFLGC
SRVVGICGTH EKCILLTSEL GFDAAINYKK DNVAEQLRES CPAGVDVYFD NVGGNISDTV
ISQMNENSHI ILCGQISQYN KDVPYPPPLS PAIEAIQKER NITRERFLVL NYKDKFEPGI
LQLSQWFKEG KLKIKETVIN GLENMGAAFQ SMMTGGNIGK QIVCISEEIS L
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