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PTGR2_MOUSE
ID   PTGR2_MOUSE             Reviewed;         351 AA.
AC   Q8VDQ1; Q3TG36; Q3ULY3; Q8BZA2; Q9D1W8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Prostaglandin reductase 2 {ECO:0000305};
DE            Short=PRG-2;
DE            EC=1.3.1.48 {ECO:0000269|PubMed:17449869};
DE   AltName: Full=15-oxoprostaglandin 13-reductase;
DE   AltName: Full=Zinc-binding alcohol dehydrogenase domain-containing protein 1;
GN   Name=Ptgr2 {ECO:0000312|MGI:MGI:1916372}; Synonyms=Zadh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Embryonic heart, Mammary gland, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF TYR-259.
RX   PubMed=17449869; DOI=10.1074/jbc.m702289200;
RA   Chou W.-L., Chuang L.-M., Chou C.-C., Wang A.H.-J., Lawson J.A.,
RA   FitzGerald G.A., Chang Z.-F.;
RT   "Identification of a novel prostaglandin reductase reveals the involvement
RT   of prostaglandin E2 catabolism in regulation of peroxisome proliferator-
RT   activated receptor gamma activation.";
RL   J. Biol. Chem. 282:18162-18172(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX   PubMed=15229897; DOI=10.1002/prot.20163;
RA   Levin I., Schwarzenbacher R., McMullan D., Abdubek P., Ambing E.,
RA   Biorac T., Cambell J., Canaves J.M., Chiu H.-J., Dai X., Deacon A.M.,
RA   DiDonato M., Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K.,
RA   Hampton E., Jaroszewski L., Karlak C., Klock H.E., Koesema E., Kreusch A.,
RA   Kuhn P., Lesley S.A., McPhillips T.M., Miller M.D., Morse A., Moy K.,
RA   Ouyang J., Page R., Quijano K., Reyes R., Robb A., Sims E., Spraggon G.,
RA   Stevens R.C., van den Bedem H., Velasquez J., Vincent J., von Delft F.,
RA   Wang X., West B., Wolf G., Xu Q., Hodgson K.O., Wooley J., Wilson I.A.;
RT   "Crystal structure of a putative NADPH-dependent oxidoreductase (GI:
RT   18204011) from mouse at 2.10 A resolution.";
RL   Proteins 56:629-633(2004).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NADPH.
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).
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. Overexpression represses
CC       transcriptional activity of PPARG and inhibits adipocyte
CC       differentiation. {ECO:0000269|PubMed:17449869}.
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:17449869};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11918;
CC         Evidence={ECO:0000305|PubMed:17449869};
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:17449869};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11914;
CC         Evidence={ECO:0000305|PubMed:17449869};
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:0000269|PubMed:17449869};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590;
CC         Evidence={ECO:0000305|PubMed:17449869};
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:0000269|PubMed:17449869};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586;
CC         Evidence={ECO:0000305|PubMed:17449869};
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:0000269|PubMed:17449869};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594;
CC         Evidence={ECO:0000305|PubMed:17449869};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=49.6 uM for 15-keto-PGE2 {ECO:0000269|PubMed:17449869};
CC         KM=34.4 uM for 15-keto-PGE1 {ECO:0000269|PubMed:17449869};
CC         KM=108.8 uM for 15-keto-PGF2-alpha {ECO:0000269|PubMed:17449869};
CC         KM=59.2 uM for 15-keto-PGF2-beta {ECO:0000269|PubMed:17449869};
CC         KM=94.6 uM for NADPH {ECO:0000269|PubMed:17449869};
CC         Vmax=178.4 umol/min/mg enzyme for 15-keto-PGE2
CC         {ECO:0000269|PubMed:17449869};
CC         Vmax=115.0 umol/min/mg enzyme for 15-keto-PGE1
CC         {ECO:0000269|PubMed:17449869};
CC         Vmax=230.9 umol/min/mg enzyme for 15-keto-PGF2-alpha
CC         {ECO:0000269|PubMed:17449869};
CC         Vmax=206.4 umol/min/mg enzyme for 15-keto-PGF2-beta
CC         {ECO:0000269|PubMed:17449869};
CC         Vmax=144.7 umol/min/mg enzyme for NADPH
CC         {ECO:0000269|PubMed:17449869};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15229897,
CC       ECO:0000269|PubMed:19000823}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VDQ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VDQ1-2; Sequence=VSP_013528, VSP_013529;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in adipose
CC       tissues. {ECO:0000269|PubMed:17449869}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the late phase of adipocyte
CC       differentiation (at protein level). {ECO:0000269|PubMed:17449869}.
CC   -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC       {ECO:0000305}.
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DR   EMBL; AK036168; BAC29329.1; -; mRNA.
DR   EMBL; AK021033; BAB32284.1; -; mRNA.
DR   EMBL; AK145232; BAE26315.1; -; mRNA.
DR   EMBL; AK159932; BAE35493.1; -; mRNA.
DR   EMBL; AK168895; BAE40712.1; -; mRNA.
DR   EMBL; BC021466; AAH21466.1; -; mRNA.
DR   CCDS; CCDS36490.1; -. [Q8VDQ1-1]
DR   RefSeq; NP_001239554.1; NM_001252625.1. [Q8VDQ1-1]
DR   RefSeq; NP_001239555.1; NM_001252626.1.
DR   RefSeq; NP_084156.2; NM_029880.3. [Q8VDQ1-1]
DR   PDB; 1VJ1; X-ray; 2.10 A; A=1-351.
DR   PDB; 2ZB3; X-ray; 2.00 A; A=1-351.
DR   PDBsum; 1VJ1; -.
DR   PDBsum; 2ZB3; -.
DR   AlphaFoldDB; Q8VDQ1; -.
DR   SMR; Q8VDQ1; -.
DR   BioGRID; 218562; 2.
DR   IntAct; Q8VDQ1; 2.
DR   MINT; Q8VDQ1; -.
DR   STRING; 10090.ENSMUSP00000115704; -.
DR   SwissLipids; SLP:000001623; -.
DR   iPTMnet; Q8VDQ1; -.
DR   PhosphoSitePlus; Q8VDQ1; -.
DR   SwissPalm; Q8VDQ1; -.
DR   EPD; Q8VDQ1; -.
DR   jPOST; Q8VDQ1; -.
DR   MaxQB; Q8VDQ1; -.
DR   PaxDb; Q8VDQ1; -.
DR   PeptideAtlas; Q8VDQ1; -.
DR   PRIDE; Q8VDQ1; -.
DR   ProteomicsDB; 302006; -. [Q8VDQ1-1]
DR   ProteomicsDB; 302007; -. [Q8VDQ1-2]
DR   DNASU; 77219; -.
DR   Ensembl; ENSMUST00000123614; ENSMUSP00000115704; ENSMUSG00000072946. [Q8VDQ1-1]
DR   Ensembl; ENSMUST00000146377; ENSMUSP00000119981; ENSMUSG00000072946. [Q8VDQ1-1]
DR   Ensembl; ENSMUST00000147363; ENSMUSP00000114766; ENSMUSG00000072946. [Q8VDQ1-2]
DR   GeneID; 77219; -.
DR   KEGG; mmu:77219; -.
DR   UCSC; uc007oep.2; mouse. [Q8VDQ1-1]
DR   CTD; 145482; -.
DR   MGI; MGI:1916372; Ptgr2.
DR   VEuPathDB; HostDB:ENSMUSG00000072946; -.
DR   eggNOG; KOG1196; Eukaryota.
DR   GeneTree; ENSGT00940000156793; -.
DR   InParanoid; Q8VDQ1; -.
DR   OMA; ECPKGVD; -.
DR   OrthoDB; 884151at2759; -.
DR   PhylomeDB; Q8VDQ1; -.
DR   TreeFam; TF324201; -.
DR   BRENDA; 1.3.1.48; 3474.
DR   SABIO-RK; Q8VDQ1; -.
DR   BioGRID-ORCS; 77219; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Ptgr2; mouse.
DR   EvolutionaryTrace; Q8VDQ1; -.
DR   PRO; PR:Q8VDQ1; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8VDQ1; protein.
DR   Bgee; ENSMUSG00000072946; Expressed in interventricular septum and 245 other tissues.
DR   ExpressionAtlas; Q8VDQ1; baseline and differential.
DR   Genevisible; Q8VDQ1; MM.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0036132; F:13-prostaglandin reductase activity; TAS:Reactome.
DR   GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; ISS:UniProtKB.
DR   GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR   CDD; cd08293; PTGR2; 1.
DR   DisProt; DP02579; -.
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; 1.
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_0000218071"
FT   BINDING         99..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165..168
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19000823"
FT   BINDING         192
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19000823"
FT   BINDING         208
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19000823"
FT   BINDING         231
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19000823"
FT   BINDING         253..259
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19000823"
FT   BINDING         287..289
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19000823"
FT   BINDING         288..290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:19000823"
FT   VAR_SEQ         314..316
FT                   /note="VKE -> FLF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_013528"
FT   VAR_SEQ         317..351
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_013529"
FT   MUTAGEN         259
FT                   /note="Y->F: Significant reduction in catalytic
FT                   efficiency."
FT                   /evidence="ECO:0000269|PubMed:17449869"
FT   CONFLICT        18
FT                   /note="P -> T (in Ref. 1; BAB32284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31
FT                   /note="P -> L (in Ref. 2; AAH21466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="V -> I (in Ref. 1; BAE26315 and 2; AAH21466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="T -> A (in Ref. 1; BAE26315 and 2; AAH21466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        239
FT                   /note="A -> T (in Ref. 1; BAE26315 and 2; AAH21466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260..261
FT                   /note="SN -> NK (in Ref. 1; BAE26315 and 2; AAH21466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        318
FT                   /note="M -> V (in Ref. 1; BAE26315 and 2; AAH21466)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           20..22
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          23..28
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          38..47
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           51..55
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          75..85
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          95..110
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:1VJ1"
FT   HELIX           119..122
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           126..130
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   TURN            131..133
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           135..147
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          157..162
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           166..177
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          181..189
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           190..198
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          203..207
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           208..210
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           213..220
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          225..232
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           234..242
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          244..252
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           256..258
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           271..280
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          283..286
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           289..291
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           293..295
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           296..308
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          316..320
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           322..324
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   HELIX           325..333
FT                   /evidence="ECO:0007829|PDB:2ZB3"
FT   STRAND          338..344
FT                   /evidence="ECO:0007829|PDB:2ZB3"
SQ   SEQUENCE   351 AA;  38015 MW;  2766871577A8022F CRC64;
     MIIQRVVLNS RPGKNGNPVA ENFRVEEFSL PDALNEGQVQ VRTLYLSVDP YMRCKMNEDT
     GTDYLAPWQL AQVADGGGIG VVEESKHQKL TKGDFVTSFY WPWQTKAILD GNGLEKVDPQ
     LVDGHLSYFL GAIGMPGLTS LIGVQEKGHI SAGSNQTMVV SGAAGACGSL AGQIGHLLGC
     SRVVGICGTQ EKCLFLTSEL GFDAAVNYKT GNVAEQLREA CPGGVDVYFD NVGGDISNAV
     ISQMNENSHI ILCGQISQYS NDVPYPPPLP PAVEAIRKER NITRERFTVL NYKDKFEPGI
     LQLSQWFKEG KLKVKETMAK GLENMGVAFQ SMMTGGNVGK QIVCISEDSS L
 
 
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