THOP1_HUMAN
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 03-AUG-2022, entry version 200.
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; 64.
DR IntAct; P52888; 12.
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 BioMuta; THOP1; -.
DR DMDM; 1708983; -.
DR EPD; P52888; -.
DR jPOST; P52888; -.
DR MassIVE; P52888; -.
DR MaxQB; P52888; -.
DR PaxDb; P52888; -.
DR PeptideAtlas; P52888; -.
DR PRIDE; P52888; -.
DR ProteomicsDB; 3634; -.
DR ProteomicsDB; 56547; -. [P52888-1]
DR Antibodypedia; 23054; 255 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 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; 642479at2759; -.
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; 20 hits in 1074 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 123 other tissues.
DR ExpressionAtlas; P52888; baseline and differential.
DR Genevisible; P52888; HS.
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 Gene3D; 1.10.1370.10; -; 1.
DR Gene3D; 1.20.1050.40; -; 1.
DR Gene3D; 3.40.390.10; -; 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; PTHR11804; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
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
