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Database: UniProt
Entry: NNRE_MOUSE
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Original site: NNRE_MOUSE 
ID   NNRE_MOUSE              Reviewed;         282 AA.
AC   Q8K4Z3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=NAD(P)H-hydrate epimerase {ECO:0000255|HAMAP-Rule:MF_03159};
DE            EC=5.1.99.6 {ECO:0000269|PubMed:21994945};
DE   AltName: Full=Apolipoprotein A-I-binding protein {ECO:0000255|HAMAP-Rule:MF_03159, ECO:0000303|PubMed:21994945};
DE            Short=AI-BP {ECO:0000255|HAMAP-Rule:MF_03159};
DE   AltName: Full=NAD(P)HX epimerase {ECO:0000250|UniProtKB:Q8NCW5, ECO:0000303|PubMed:21994945};
DE   Flags: Precursor;
GN   Name=Naxe {ECO:0000250|UniProtKB:Q8NCW5}; Synonyms=Aibp, Apoa1bp;
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 [MRNA].
RC   STRAIN=Swiss Webster;
RX   PubMed=11991719; DOI=10.1006/geno.2002.6761;
RA   Ritter M., Buechler C., Boettcher A., Barlage S., Schmitz-Madry A.,
RA   Orso E., Bared S.M., Schmiedeknecht G., Baehr C.H., Fricker G., Schmitz G.;
RT   "Cloning and characterization of a novel apolipoprotein A-I-binding
RT   protein, AI-BP, secreted by cells of the kidney proximal tubules in
RT   response to HDL or ApoA-I.";
RL   Genomics 79:693-702(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF
RP   25-282, SUBUNIT, PHOSPHORYLATION AT SER-43, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Testis;
RX   PubMed=18202122; DOI=10.1210/en.2007-0582;
RA   Jha K.N., Shumilin I.A., Digilio L.C., Chertihin O., Zheng H., Schmitz G.,
RA   Visconti P.E., Flickinger C.J., Minor W., Herr J.C.;
RT   "Biochemical and structural characterization of apolipoprotein A-I binding
RT   protein, a novel phosphoprotein with a potential role in sperm
RT   capacitation.";
RL   Endocrinology 149:2108-2120(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=18614015; DOI=10.1016/j.cell.2008.06.016;
RA   Pagliarini D.J., Calvo S.E., Chang B., Sheth S.A., Vafai S.B., Ong S.E.,
RA   Walford G.A., Sugiana C., Boneh A., Chen W.K., Hill D.E., Vidal M.,
RA   Evans J.G., Thorburn D.R., Carr S.A., Mootha V.K.;
RT   "A mitochondrial protein compendium elucidates complex I disease biology.";
RL   Cell 134:112-123(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP   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   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=21994945; DOI=10.1074/jbc.c111.310847;
RA   Marbaix A.Y., Noel G., Detroux A.M., Vertommen D., Van Schaftingen E.,
RA   Linster C.L.;
RT   "Extremely conserved ATP- or ADP-dependent enzymatic system for
RT   nicotinamide nucleotide repair.";
RL   J. Biol. Chem. 286:41246-41252(2011).
RN   [9]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-138, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Catalyzes the epimerization of the S- and R-forms of
CC       NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or
CC       heat-dependent hydration (By similarity) (PubMed:21994945). This is a
CC       prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow
CC       the repair of both epimers of NAD(P)HX (By similarity). Accelerates
CC       cholesterol efflux from endothelial cells to high-density lipoprotein
CC       (HDL) and thereby regulates angiogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:Q8NCW5, ECO:0000255|HAMAP-Rule:MF_03159,
CC       ECO:0000269|PubMed:21994945}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215,
CC         ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6;
CC         Evidence={ECO:0000269|PubMed:21994945};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227,
CC         ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6;
CC         Evidence={ECO:0000269|PubMed:21994945};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03159};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03159};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.6 uM for (R)-NADHX {ECO:0000269|PubMed:21994945};
CC         KM=0.33 uM for (R)-NADPHX {ECO:0000269|PubMed:21994945};
CC         Vmax=0.26 umol/min/mg enzyme toward (R)-NADHX
CC         {ECO:0000269|PubMed:21994945};
CC         Vmax=1.2 umol/min/mg enzyme toward (R)-NADPHX
CC         {ECO:0000269|PubMed:21994945};
CC   -!- SUBUNIT: Homodimer (PubMed:18202122). Interacts with APOA1 and APOA2
CC       (By similarity). {ECO:0000250|UniProtKB:Q8NCW5,
CC       ECO:0000269|PubMed:18202122}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}.
CC       Secreted {ECO:0000255|HAMAP-Rule:MF_03159, ECO:0000269|PubMed:18202122,
CC       ECO:0000269|PubMed:18614015}. Note=In sperm, secretion gradually
CC       increases during capacitation.
CC   -!- TISSUE SPECIFICITY: Detected in testis and sperm (at protein level).
CC       Expressed at high levels in heart, liver, kidney, and testis.
CC       {ECO:0000269|PubMed:18202122}.
CC   -!- PTM: Undergoes physiological phosphorylation during sperm capacitation,
CC       downstream to PKA activation. {ECO:0000255|HAMAP-Rule:MF_03159,
CC       ECO:0000269|PubMed:18202122}.
CC   -!- SIMILARITY: Belongs to the NnrE/AIBP family. {ECO:0000255|HAMAP-
CC       Rule:MF_03159}.
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DR   EMBL; AJ344092; CAC86966.1; -; mRNA.
DR   EMBL; AY566271; AAT70236.1; -; mRNA.
DR   EMBL; AK159846; BAE35424.1; -; mRNA.
DR   EMBL; BC058362; AAH58362.1; -; mRNA.
DR   CCDS; CCDS17464.1; -.
DR   RefSeq; NP_659146.1; NM_144897.3.
DR   PDB; 2DG2; X-ray; 2.45 A; A/B/C/D/E/F=25-282.
DR   PDB; 2O8N; X-ray; 2.00 A; A=25-282.
DR   PDB; 3RNO; X-ray; 2.50 A; A=25-282.
DR   PDB; 3RO7; X-ray; 2.50 A; A=25-282.
DR   PDB; 3ROE; X-ray; 2.11 A; A/B/C/D/E/F=25-282.
DR   PDB; 3ROG; X-ray; 2.05 A; A=25-282.
DR   PDB; 3ROX; X-ray; 2.40 A; A=25-282.
DR   PDB; 3ROZ; X-ray; 2.80 A; A=25-282.
DR   PDBsum; 2DG2; -.
DR   PDBsum; 2O8N; -.
DR   PDBsum; 3RNO; -.
DR   PDBsum; 3RO7; -.
DR   PDBsum; 3ROE; -.
DR   PDBsum; 3ROG; -.
DR   PDBsum; 3ROX; -.
DR   PDBsum; 3ROZ; -.
DR   AlphaFoldDB; Q8K4Z3; -.
DR   SMR; Q8K4Z3; -.
DR   BioGRID; 232930; 3.
DR   DIP; DIP-59952N; -.
DR   ELM; Q8K4Z3; -.
DR   STRING; 10090.ENSMUSP00000029708; -.
DR   GlyGen; Q8K4Z3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8K4Z3; -.
DR   PhosphoSitePlus; Q8K4Z3; -.
DR   SwissPalm; Q8K4Z3; -.
DR   REPRODUCTION-2DPAGE; Q8K4Z3; -.
DR   EPD; Q8K4Z3; -.
DR   jPOST; Q8K4Z3; -.
DR   MaxQB; Q8K4Z3; -.
DR   PaxDb; 10090-ENSMUSP00000029708; -.
DR   PeptideAtlas; Q8K4Z3; -.
DR   ProteomicsDB; 253089; -.
DR   Pumba; Q8K4Z3; -.
DR   TopDownProteomics; Q8K4Z3; -.
DR   Antibodypedia; 34221; 237 antibodies from 29 providers.
DR   DNASU; 246703; -.
DR   Ensembl; ENSMUST00000029708.8; ENSMUSP00000029708.7; ENSMUSG00000028070.8.
DR   GeneID; 246703; -.
DR   KEGG; mmu:246703; -.
DR   UCSC; uc008ptu.1; mouse.
DR   AGR; MGI:2180167; -.
DR   CTD; 128240; -.
DR   MGI; MGI:2180167; Naxe.
DR   VEuPathDB; HostDB:ENSMUSG00000028070; -.
DR   eggNOG; KOG2585; Eukaryota.
DR   GeneTree; ENSGT00390000007227; -.
DR   HOGENOM; CLU_024853_3_0_1; -.
DR   InParanoid; Q8K4Z3; -.
DR   OMA; RHLFHYG; -.
DR   OrthoDB; 1493at2759; -.
DR   PhylomeDB; Q8K4Z3; -.
DR   TreeFam; TF300197; -.
DR   BRENDA; 5.1.99.6; 3474.
DR   Reactome; R-MMU-197264; Nicotinamide salvaging.
DR   SABIO-RK; Q8K4Z3; -.
DR   BioGRID-ORCS; 246703; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Apoa1bp; mouse.
DR   EvolutionaryTrace; Q8K4Z3; -.
DR   PRO; PR:Q8K4Z3; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8K4Z3; Protein.
DR   Bgee; ENSMUSG00000028070; Expressed in choroid plexus of fourth ventricle and 260 other cell types or tissues.
DR   Genevisible; Q8K4Z3; MM.
DR   GO; GO:0044297; C:cell body; IDA:MGI.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0052856; F:NADHX epimerase activity; ISO:MGI.
DR   GO; GO:0052857; F:NADPHX epimerase activity; ISO:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0031580; P:membrane raft distribution; ISS:UniProtKB.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR   GO; GO:0046496; P:nicotinamide nucleotide metabolic process; ISS:UniProtKB.
DR   GO; GO:0010874; P:regulation of cholesterol efflux; ISS:UniProtKB.
DR   GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR   Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR   HAMAP; MF_01966; NADHX_epimerase; 1.
DR   InterPro; IPR004443; YjeF_N_dom.
DR   InterPro; IPR036652; YjeF_N_dom_sf.
DR   InterPro; IPR032976; YJEFN_prot_NAXE-like.
DR   NCBIfam; TIGR00197; yjeF_nterm; 1.
DR   PANTHER; PTHR13232; NAD(P)H-HYDRATE EPIMERASE; 1.
DR   PANTHER; PTHR13232:SF11; NAD(P)H-HYDRATE EPIMERASE; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR   PROSITE; PS51385; YJEF_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Isomerase; Lipid transport; Metal-binding; Mitochondrion;
KW   NAD; NADP; Nucleotide-binding; Phosphoprotein; Potassium;
KW   Reference proteome; Secreted; Transit peptide; Transport.
FT   TRANSIT         1..53
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   CHAIN           54..282
FT                   /note="NAD(P)H-hydrate epimerase"
FT                   /id="PRO_0000292423"
FT   DOMAIN          59..269
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         113..117
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         114
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         179
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         183..189
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         212
FT                   /ligand="(6S)-NADPHX"
FT                   /ligand_id="ChEBI:CHEBI:64076"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   BINDING         215
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03159"
FT   MOD_RES         43
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000269|PubMed:18202122,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         138
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   HELIX           56..67
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   TURN            68..70
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   HELIX           74..92
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   STRAND          98..102
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   HELIX           113..127
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   STRAND          131..135
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   HELIX           143..154
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   STRAND          159..162
FT                   /evidence="ECO:0007829|PDB:3ROZ"
FT   HELIX           167..173
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   STRAND          175..181
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   HELIX           194..202
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   STRAND          208..213
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   TURN            219..221
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   STRAND          230..237
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   HELIX           240..244
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   STRAND          247..253
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   HELIX           259..264
FT                   /evidence="ECO:0007829|PDB:2O8N"
FT   STRAND          277..280
FT                   /evidence="ECO:0007829|PDB:2O8N"
SQ   SEQUENCE   282 AA;  30973 MW;  DFD95155755D8D96 CRC64;
     MSGLRTLLGL GLLVAGSRLP RVISQQSVCR ARPIWWGTQR RGSETMAGAA VKYLSQEEAQ
     AVDQELFNEY QFSVDQLMEL AGLSCATAIA KAYPPTSMSK SPPTVLVICG PGNNGGDGLV
     CARHLKLFGY QPTIYYPKRP NKPLFTGLVT QCQKMDIPFL GEMPPEPMMV DELYELVVDA
     IFGFSFKGDV REPFHSILSV LSGLTVPIAS IDIPSGWDVE KGNPSGIQPD LLISLTAPKK
     SATHFTGRYH YLGGRFVPPA LEKKYQLNLP SYPDTECVYR LQ
//
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