ID   CNDP2_MOUSE             Reviewed;         475 AA.
AC   Q9D1A2; Q3TA80; Q3TI32; Q3U7B9; Q99PV1;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Cytosolic non-specific dipeptidase;
DE            EC=3.4.13.18 {ECO:0000269|PubMed:15749831, ECO:0000269|PubMed:31587987};
DE   AltName: Full=CNDP dipeptidase 2;
DE   AltName: Full=Glutamate carboxypeptidase-like protein 1;
DE   AltName: Full=Threonyl dipeptidase {ECO:0000303|PubMed:31587987};
GN   Name=Cndp2; Synonyms=Cn2;
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   TISSUE=Brain;
RA   Yoshikawa T., Nagasugi Y., Sugano S., Hashimoto K., Masuho Y., Seki N.;
RT   "Novel mouse gene differentially expressed in kidney.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC   TISSUE=Bone marrow macrophage, Embryonic heart, Heart, and Spleen;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
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   [4]
RP   PROTEIN SEQUENCE OF 6-17; 311-329 AND 414-430, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   ACTIVITY REGULATION, COFACTOR, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=15749831; DOI=10.1093/jb/mvi016;
RA   Otani H., Okumura N., Hashida-Okumura A., Nagai K.;
RT   "Identification and characterization of a mouse dipeptidase that hydrolyzes
RT   L-carnosine.";
RL   J. Biochem. 137:167-175(2005).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-166.
RX   PubMed=31587987; DOI=10.1016/j.chembiol.2019.09.009;
RA   Kim J.T., Li V.L., Terrell S.M., Fischer C.R., Long J.Z.;
RT   "Family-wide Annotation of Enzymatic Pathways by Parallel In Vivo
RT   Metabolomics.";
RL   Cell Chem. Biol. 26:1623-1629(2019).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MANGANESE AND
RP   BESTATIN, MUTAGENESIS OF HIS-228, COFACTOR, AND SUBUNIT.
RX   PubMed=18550540; DOI=10.1074/jbc.m801657200;
RA   Unno H., Yamashita T., Ujita S., Okumura N., Otani H., Okumura A.,
RA   Nagai K., Kusunoki M.;
RT   "Structural basis for substrate recognition and hydrolysis by mouse
RT   carnosinase CN2.";
RL   J. Biol. Chem. 283:27289-27299(2008).
CC   -!- FUNCTION: Catalyzes the peptide bond hydrolysis in dipeptides,
CC       displaying a non-redundant activity toward threonyl dipeptides
CC       (PubMed:31587987). Mediates threonyl dipeptide catabolism in a tissue-
CC       specific way (PubMed:31587987). Has high dipeptidase activity toward
CC       cysteinylglycine, an intermediate metabolite in glutathione metabolism
CC       (By similarity). Metabolizes N-lactoyl-amino acids, both through
CC       hydrolysis to form lactic acid and amino acids, as well as through
CC       their formation by reverse proteolysis (By similarity). Plays a role in
CC       the regulation of cell cycle arrest and apoptosis (By similarity).
CC       {ECO:0000250|UniProtKB:Q96KP4, ECO:0000269|PubMed:31587987}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of dipeptides, preferentially hydrophobic
CC         dipeptides including prolyl amino acids.; EC=3.4.13.18;
CC         Evidence={ECO:0000269|PubMed:15749831, ECO:0000269|PubMed:31587987};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-threonyl-L-threonine = 2 L-threonine;
CC         Xref=Rhea:RHEA:67360, ChEBI:CHEBI:15377, ChEBI:CHEBI:57926,
CC         ChEBI:CHEBI:169953; Evidence={ECO:0000269|PubMed:31587987};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67361;
CC         Evidence={ECO:0000269|PubMed:31587987};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-threonyl-L-serine = L-serine + L-threonine;
CC         Xref=Rhea:RHEA:67364, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:169954;
CC         Evidence={ECO:0000269|PubMed:31587987};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67365;
CC         Evidence={ECO:0000269|PubMed:31587987};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-seryl-L-threonine = L-serine + L-threonine;
CC         Xref=Rhea:RHEA:67372, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:169955;
CC         Evidence={ECO:0000269|PubMed:31587987};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67373;
CC         Evidence={ECO:0000269|PubMed:31587987};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine;
CC         Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:61694;
CC         Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784;
CC         Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-alanyl-L-cysteine = L-alanine + L-cysteine;
CC         Xref=Rhea:RHEA:67380, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:169958;
CC         Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67381;
CC         Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactate + L-phenylalanine = H2O + N-[(S)-lactoyl]-L-
CC         phenylalanine; Xref=Rhea:RHEA:66724, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16651, ChEBI:CHEBI:58095, ChEBI:CHEBI:167456;
CC         Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66725;
CC         Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:66726;
CC         Evidence={ECO:0000250|UniProtKB:Q96KP4};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:15749831, ECO:0000269|PubMed:18550540};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:15749831,
CC       ECO:0000269|PubMed:18550540};
CC   -!- ACTIVITY REGULATION: Inhibited by bestatin.
CC       {ECO:0000269|PubMed:15749831}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18550540}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96KP4}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the parafascicular nucleus of
CC       the thalamus, tuberomammillary nucleus of the hypothalamus and the
CC       mitral cell layer of the olfactory bulb. {ECO:0000269|PubMed:15749831}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB046738; BAB21596.1; -; mRNA.
DR   EMBL; AK003779; BAB22991.1; -; mRNA.
DR   EMBL; AK151013; BAE30033.1; -; mRNA.
DR   EMBL; AK152729; BAE31451.1; -; mRNA.
DR   EMBL; AK168029; BAE40014.1; -; mRNA.
DR   EMBL; AK168652; BAE40509.1; -; mRNA.
DR   EMBL; AK172034; BAE42789.1; -; mRNA.
DR   EMBL; BC005532; AAH05532.1; -; mRNA.
DR   CCDS; CCDS29383.1; -.
DR   RefSeq; NP_001276460.1; NM_001289531.1.
DR   RefSeq; NP_075638.2; NM_023149.3.
DR   PDB; 2ZOF; X-ray; 2.30 A; A/B=1-475.
DR   PDB; 2ZOG; X-ray; 1.70 A; A/B=1-475.
DR   PDBsum; 2ZOF; -.
DR   PDBsum; 2ZOG; -.
DR   AlphaFoldDB; Q9D1A2; -.
DR   SMR; Q9D1A2; -.
DR   BioGRID; 211181; 24.
DR   IntAct; Q9D1A2; 2.
DR   STRING; 10090.ENSMUSP00000128696; -.
DR   MEROPS; M20.005; -.
DR   GlyGen; Q9D1A2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9D1A2; -.
DR   PhosphoSitePlus; Q9D1A2; -.
DR   SwissPalm; Q9D1A2; -.
DR   REPRODUCTION-2DPAGE; Q9D1A2; -.
DR   EPD; Q9D1A2; -.
DR   jPOST; Q9D1A2; -.
DR   MaxQB; Q9D1A2; -.
DR   PaxDb; 10090-ENSMUSP00000128696; -.
DR   PeptideAtlas; Q9D1A2; -.
DR   ProteomicsDB; 283648; -.
DR   Pumba; Q9D1A2; -.
DR   Antibodypedia; 23332; 457 antibodies from 31 providers.
DR   DNASU; 66054; -.
DR   Ensembl; ENSMUST00000025546.17; ENSMUSP00000025546.10; ENSMUSG00000024644.18.
DR   Ensembl; ENSMUST00000168419.3; ENSMUSP00000128696.2; ENSMUSG00000024644.18.
DR   GeneID; 66054; -.
DR   KEGG; mmu:66054; -.
DR   UCSC; uc008fut.2; mouse.
DR   AGR; MGI:1913304; -.
DR   CTD; 55748; -.
DR   MGI; MGI:1913304; Cndp2.
DR   VEuPathDB; HostDB:ENSMUSG00000024644; -.
DR   eggNOG; KOG2276; Eukaryota.
DR   GeneTree; ENSGT00940000156500; -.
DR   HOGENOM; CLU_029469_3_1_1; -.
DR   InParanoid; Q9D1A2; -.
DR   OMA; HITIPGF; -.
DR   OrthoDB; 177966at2759; -.
DR   PhylomeDB; Q9D1A2; -.
DR   TreeFam; TF300633; -.
DR   Reactome; R-MMU-174403; Glutathione synthesis and recycling.
DR   Reactome; R-MMU-9753281; Paracetamol ADME.
DR   BioGRID-ORCS; 66054; 4 hits in 78 CRISPR screens.
DR   ChiTaRS; Cndp2; mouse.
DR   EvolutionaryTrace; Q9D1A2; -.
DR   PRO; PR:Q9D1A2; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q9D1A2; Protein.
DR   Bgee; ENSMUSG00000024644; Expressed in vestibular membrane of cochlear duct and 260 other cell types or tissues.
DR   ExpressionAtlas; Q9D1A2; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0103046; F:alanylglutamate dipeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016805; F:dipeptidase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR   GO; GO:0006508; P:proteolysis; IDA:MGI.
DR   CDD; cd05676; M20_dipept_like_CNDP; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR017153; CNDP/DUG1.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR   PANTHER; PTHR43270:SF11; CYTOSOLIC NON-SPECIFIC DIPEPTIDASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
DR   Genevisible; Q9D1A2; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Carboxypeptidase; Cytoplasm; Direct protein sequencing;
KW   Hydrolase; Manganese; Metal-binding; Metalloprotease; Phosphoprotein;
KW   Protease; Reference proteome.
FT   CHAIN           1..475
FT                   /note="Cytosolic non-specific dipeptidase"
FT                   /id="PRO_0000185273"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18550540"
FT   BINDING         132
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18550540"
FT   BINDING         132
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18550540"
FT   BINDING         166..167
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT   BINDING         167
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18550540"
FT   BINDING         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18550540"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT   BINDING         417
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT   BINDING         445
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18550540"
FT   BINDING         445
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT   SITE            228
FT                   /note="Important for catalytic activity"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6Q0N1"
FT   MOD_RES         299
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96KP4"
FT   MUTAGEN         166
FT                   /note="E->A: Loss of threonyl dipeptidase activity."
FT                   /evidence="ECO:0000269|PubMed:31587987"
FT   MUTAGEN         228
FT                   /note="H->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:18550540"
FT   CONFLICT        45
FT                   /note="M -> I (in Ref. 2; BAE31451)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="A -> T (in Ref. 2; BAE42789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        357
FT                   /note="V -> A (in Ref. 1; BAB21596)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1..13
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           15..27
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           38..54
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          93..99
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           107..109
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          124..127
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   TURN            128..133
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           134..149
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          155..164
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           166..168
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           173..179
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   TURN            180..187
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          190..193
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          199..203
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          205..210
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          212..221
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           229..232
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           239..247
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   TURN            260..265
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           271..276
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           284..290
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           301..309
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          313..322
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          325..327
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          334..344
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           350..366
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          372..382
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           392..405
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          410..416
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           420..428
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          430..434
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   STRAND          450..452
FT                   /evidence="ECO:0007829|PDB:2ZOG"
FT   HELIX           453..472
FT                   /evidence="ECO:0007829|PDB:2ZOG"
SQ   SEQUENCE   475 AA;  52767 MW;  086950275A698500 CRC64;
     MSALKAVFQY IDENQDRYVK KLAEWVAIQS VSAWPEKRGE IRRMMEVAAA DVQRLGGSVE
     LVDIGKQKLP DGSEIPLPPI LLGKLGSDPQ KKTVCIYGHL DVQPAALEDG WDSEPFTLVE
     REGKLYGRGS TDDKGPVAGW MNALEAYQKT GQEIPVNLRF CLEGMEESGS EGLDELIFAQ
     KDKFFKDVDY VCISDNYWLG KNKPCITYGL RGICYFFIEV ECSDKDLHSG VYGGSVHEAM
     TDLISLMGCL VDKKGKILIP GINDAVAPVT DEEHALYDHI DFDMEEFAKD VGAETLLHSC
     KKDILMHRWR YPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPDMIP EVVSEQVSSY
     LSKKFAELQS PNKFKVYMGH GGKPWVSDFN HPHYQAGRRA LKTVFGVEPD LTREGGSIPV
     TLTFQEATGK NVMLLPVGSA DDGAHSQNEK LNRLNYIEGT KMLAAYLYEV SQLKN
//