ID   THOP1_HUMAN             Reviewed;         689 AA.
AC   P52888; B3KSE2; Q9UCB3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 207.
DE   RecName: Full=Thimet oligopeptidase {ECO:0000303|PubMed:17251185};
DE            EC=3.4.24.15 {ECO:0000305|PubMed:7639763};
DE   AltName: Full=Endopeptidase 24.15 {ECO:0000303|Ref.2};
DE   AltName: Full=MP78 {ECO:0000303|PubMed:7639763};
GN   Name=THOP1;
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), FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Brain;
RX   PubMed=7639763; DOI=10.1006/bbrc.1995.2099;
RA   Thompson A., Huber G., Malherbe P.;
RT   "Cloning and functional expression of a metalloendopeptidase from human
RT   brain with the ability to cleave a beta-APP substrate peptide.";
RL   Biochem. Biophys. Res. Commun. 213:66-73(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Taylor G.R., Otulakowski G., Lau C.Y., Munroe D.G.;
RT   "cDNA cloning and gene structure of a human gene encoding a highly
RT   conserved metalloendopeptidase (EC 3.4.24.15).";
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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 GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung, and Placenta;
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   [6]
RP   PROTEIN SEQUENCE OF 67-78; 181-197 AND 199-200.
RC   TISSUE=Brain;
RX   PubMed=8286339; DOI=10.1021/bi00167a025;
RA   Papastoitsis G., Siman R., Scott R., Abraham C.R.;
RT   "Identification of a metalloprotease from Alzheimer's disease brain able to
RT   degrade the beta-amyloid precursor protein and generate amyloidogenic
RT   fragments.";
RL   Biochemistry 33:192-199(1994).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257 AND LYS-538, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [8]
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
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   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 16-688, ZINC-BINDING SITES,
RP   COFACTOR, ACTIVE SITE, FUNCTION, AND SUBUNIT.
RX   PubMed=17251185; DOI=10.1074/jbc.m609897200;
RA   Lim E.J., Sampath S., Coll-Rodriguez J., Schmidt J., Ray K., Rodgers D.W.;
RT   "Swapping the substrate specificities of the neuropeptidases neurolysin and
RT   thimet oligopeptidase.";
RL   J. Biol. Chem. 282:9722-9732(2007).
CC   -!- FUNCTION: Involved in the metabolism of neuropeptides under 20 amino
CC       acid residues long. Involved in cytoplasmic peptide degradation
CC       (PubMed:7639763, PubMed:17251185). Able to degrade the amyloid-beta
CC       precursor protein and generate amyloidogenic fragments (PubMed:7639763,
CC       PubMed:17251185). Also acts as a regulator of cannabinoid signaling
CC       pathway by mediating degradation of hemopressin, an antagonist peptide
CC       of the cannabinoid receptor CNR1 (By similarity).
CC       {ECO:0000250|UniProtKB:P24155, ECO:0000269|PubMed:17251185,
CC       ECO:0000269|PubMed:7639763}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of bonds with hydrophobic residues at
CC         P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15
CC         residues.; EC=3.4.24.15; Evidence={ECO:0000305|PubMed:7639763};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:17251185};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17251185};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P47788}.
CC   -!- INTERACTION:
CC       P52888; O95208-2: EPN2; NbExp=3; IntAct=EBI-372399, EBI-12135243;
CC       P52888; Q96CV9: OPTN; NbExp=3; IntAct=EBI-372399, EBI-748974;
CC       P52888; P62161: Calm3; Xeno; NbExp=2; IntAct=EBI-372399, EBI-397530;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47788}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P52888-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P52888-2; Sequence=VSP_056494, VSP_056495;
CC   -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR   EMBL; Z50115; CAA90477.1; -; mRNA.
DR   EMBL; U29366; AAA82607.1; -; mRNA.
DR   EMBL; AK093392; BAG52704.1; -; mRNA.
DR   EMBL; AC006538; AAD13118.1; -; Genomic_DNA.
DR   EMBL; BC000135; AAH00135.1; -; mRNA.
DR   EMBL; BC002391; AAH02391.1; -; mRNA.
DR   CCDS; CCDS12095.1; -. [P52888-1]
DR   PIR; JC4197; HYHUTH.
DR   RefSeq; NP_003240.1; NM_003249.4. [P52888-1]
DR   PDB; 1S4B; X-ray; 2.00 A; P=16-689.
DR   PDB; 2O36; X-ray; 1.95 A; A=16-688.
DR   PDBsum; 1S4B; -.
DR   PDBsum; 2O36; -.
DR   AlphaFoldDB; P52888; -.
DR   SMR; P52888; -.
DR   BioGRID; 112921; 84.
DR   IntAct; P52888; 13.
DR   MINT; P52888; -.
DR   STRING; 9606.ENSP00000304467; -.
DR   MEROPS; M03.001; -.
DR   GlyGen; P52888; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P52888; -.
DR   PhosphoSitePlus; P52888; -.
DR   SwissPalm; P52888; -.
DR   BioMuta; THOP1; -.
DR   DMDM; 1708983; -.
DR   EPD; P52888; -.
DR   jPOST; P52888; -.
DR   MassIVE; P52888; -.
DR   MaxQB; P52888; -.
DR   PaxDb; 9606-ENSP00000304467; -.
DR   PeptideAtlas; P52888; -.
DR   ProteomicsDB; 3634; -.
DR   ProteomicsDB; 56547; -. [P52888-1]
DR   Pumba; P52888; -.
DR   Antibodypedia; 23054; 277 antibodies from 30 providers.
DR   DNASU; 7064; -.
DR   Ensembl; ENST00000307741.11; ENSP00000304467.5; ENSG00000172009.15. [P52888-1]
DR   Ensembl; ENST00000395212.8; ENSP00000378638.3; ENSG00000172009.15. [P52888-2]
DR   GeneID; 7064; -.
DR   KEGG; hsa:7064; -.
DR   MANE-Select; ENST00000307741.11; ENSP00000304467.5; NM_003249.5; NP_003240.1.
DR   UCSC; uc002lwj.4; human. [P52888-1]
DR   AGR; HGNC:11793; -.
DR   CTD; 7064; -.
DR   DisGeNET; 7064; -.
DR   GeneCards; THOP1; -.
DR   HGNC; HGNC:11793; THOP1.
DR   HPA; ENSG00000172009; Low tissue specificity.
DR   MIM; 601117; gene.
DR   neXtProt; NX_P52888; -.
DR   OpenTargets; ENSG00000172009; -.
DR   PharmGKB; PA36505; -.
DR   VEuPathDB; HostDB:ENSG00000172009; -.
DR   eggNOG; KOG2089; Eukaryota.
DR   GeneTree; ENSGT00950000183171; -.
DR   HOGENOM; CLU_001805_2_0_1; -.
DR   InParanoid; P52888; -.
DR   OMA; KNFQSAM; -.
DR   OrthoDB; 735202at2759; -.
DR   PhylomeDB; P52888; -.
DR   TreeFam; TF300459; -.
DR   BRENDA; 3.4.24.15; 2681.
DR   PathwayCommons; P52888; -.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; P52888; -.
DR   SIGNOR; P52888; -.
DR   BioGRID-ORCS; 7064; 22 hits in 1155 CRISPR screens.
DR   ChiTaRS; THOP1; human.
DR   EvolutionaryTrace; P52888; -.
DR   GeneWiki; THOP1; -.
DR   GenomeRNAi; 7064; -.
DR   Pharos; P52888; Tbio.
DR   PRO; PR:P52888; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P52888; Protein.
DR   Bgee; ENSG00000172009; Expressed in left testis and 125 other cell types or tissues.
DR   ExpressionAtlas; P52888; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd06455; M3A_TOP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR024080; Neurolysin/TOP_N.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF50; THIMET OLIGOPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; P52888; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
KW   Phosphoprotein; Protease; Reference proteome; Zinc.
FT   CHAIN           1..689
FT                   /note="Thimet oligopeptidase"
FT                   /id="PRO_0000078153"
FT   ACT_SITE        474
FT                   /evidence="ECO:0000269|PubMed:17251185"
FT   BINDING         473
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:17251185"
FT   BINDING         477
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:17251185"
FT   BINDING         480
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:17251185"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C1A5"
FT   MOD_RES         257
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         278
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C1A5"
FT   MOD_RES         538
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..489
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056494"
FT   VAR_SEQ         636
FT                   /note="K -> KFPHYEVRPLRHVSLCLPLTWCDPGSGQPPESLTRNRWLPALRAGPA
FT                   LPGCNIALGSLQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056495"
FT   HELIX           30..52
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   TURN            61..64
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           65..83
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           85..88
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           92..113
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           116..128
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           136..151
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   TURN            152..155
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           158..184
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   STRAND          188..191
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   TURN            193..198
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           201..204
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   STRAND          215..220
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           221..230
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           234..244
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   TURN            245..248
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           249..269
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           275..280
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           288..324
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   TURN            334..336
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           337..348
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           353..356
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           357..359
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           362..377
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   STRAND          379..383
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   STRAND          395..401
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   TURN            402..404
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   STRAND          407..414
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   STRAND          426..431
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   STRAND          444..449
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           465..483
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           489..491
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   TURN            498..502
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           503..509
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           510..513
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           515..520
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   TURN            525..527
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           533..541
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           542..544
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           547..564
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           572..582
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           594..597
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           599..602
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   TURN            606..610
FT                   /evidence="ECO:0007829|PDB:1S4B"
FT   HELIX           611..630
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           635..644
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   TURN            645..648
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           649..651
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           654..662
FT                   /evidence="ECO:0007829|PDB:2O36"
FT   HELIX           669..674
FT                   /evidence="ECO:0007829|PDB:2O36"
SQ   SEQUENCE   689 AA;  78840 MW;  092D53DD63B322DE CRC64;
     MKPPAACAGD MADAASPCSV VNDLRWDLSA QQIEERTREL IEQTKRVYDQ VGTQEFEDVS
     YESTLKALAD VEVTYTVQRN ILDFPQHVSP SKDIRTASTE ADKKLSEFDV EMSMREDVYQ
     RIVWLQEKVQ KDSLRPEAAR YLERLIKLGR RNGLHLPRET QENIKRIKKK LSLLCIDFNK
     NLNEDTTFLP FTLQELGGLP EDFLNSLEKM EDGKLKVTLK YPHYFPLLKK CHVPETRRKV
     EEAFNCRCKE ENCAILKELV TLRAQKSRLL GFHTHADYVL EMNMAKTSQT VATFLDELAQ
     KLKPLGEQER AVILELKRAE CERRGLPFDG RIRAWDMRYY MNQVEETRYC VDQNLLKEYF
     PVQVVTHGLL GIYQELLGLA FHHEEGASAW HEDVRLYTAR DAASGEVVGK FYLDLYPREG
     KYGHAACFGL QPGCLRQDGS RQIAIAAMVA NFTKPTADAP SLLQHDEVET YFHEFGHVMH
     QLCSQAEFAM FSGTHVERDF VEAPSQMLEN WVWEQEPLLR MSRHYRTGSA VPRELLEKLI
     ESRQANTGLF NLRQIVLAKV DQALHTQTDA DPAEEYARLC QEILGVPATP GTNMPATFGH
     LAGGYDAQYY GYLWSEVYSM DMFHTRFKQE GVLNSKVGMD YRSCILRPGG SEDASAMLRR
     FLGRDPKQDA FLLSKGLQVG GCEPEPQVC
//