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PTGR2_HUMAN
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   03-AUG-2022, entry version 166.
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; 17.
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   BioMuta; PTGR2; -.
DR   DMDM; 62901454; -.
DR   REPRODUCTION-2DPAGE; IPI00167515; -.
DR   EPD; Q8N8N7; -.
DR   jPOST; Q8N8N7; -.
DR   MassIVE; Q8N8N7; -.
DR   MaxQB; Q8N8N7; -.
DR   PaxDb; Q8N8N7; -.
DR   PeptideAtlas; Q8N8N7; -.
DR   PRIDE; Q8N8N7; -.
DR   ProteomicsDB; 72438; -. [Q8N8N7-1]
DR   ProteomicsDB; 72439; -. [Q8N8N7-2]
DR   Antibodypedia; 30; 236 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   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; ECPKGVD; -.
DR   PhylomeDB; Q8N8N7; -.
DR   TreeFam; TF324201; -.
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; 12 hits in 1078 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 158 other 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   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; PTHR43205; 1.
DR   Pfam; PF16884; ADH_N_2; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 2.
DR   SUPFAM; SSF51735; SSF51735; 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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