CNDP2_MOUSE
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 03-AUG-2022, entry version 158.
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, 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 [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}.
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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; 22.
DR IntAct; Q9D1A2; 1.
DR STRING; 10090.ENSMUSP00000128696; -.
DR MEROPS; M20.005; -.
DR iPTMnet; Q9D1A2; -.
DR PhosphoSitePlus; Q9D1A2; -.
DR SwissPalm; Q9D1A2; -.
DR REPRODUCTION-2DPAGE; Q9D1A2; -.
DR EPD; Q9D1A2; -.
DR jPOST; Q9D1A2; -.
DR MaxQB; Q9D1A2; -.
DR PaxDb; Q9D1A2; -.
DR PeptideAtlas; Q9D1A2; -.
DR PRIDE; Q9D1A2; -.
DR ProteomicsDB; 283648; -.
DR Antibodypedia; 23332; 420 antibodies from 31 providers.
DR DNASU; 66054; -.
DR Ensembl; ENSMUST00000025546; ENSMUSP00000025546; ENSMUSG00000024644.
DR Ensembl; ENSMUST00000168419; ENSMUSP00000128696; ENSMUSG00000024644.
DR GeneID; 66054; -.
DR KEGG; mmu:66054; -.
DR UCSC; uc008fut.2; mouse.
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; 733473at2759; -.
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; 3 hits in 73 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 256 other tissues.
DR ExpressionAtlas; Q9D1A2; baseline and differential.
DR Genevisible; Q9D1A2; MM.
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 InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR017153; CNDP/DUG1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
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
