PDE7A_HUMAN
ID PDE7A_HUMAN Reviewed; 482 AA.
AC Q13946; A0AVH6; A8K436; A8K9G5; O15380; Q96T72;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A;
DE EC=3.1.4.53 {ECO:0000269|PubMed:8389765};
DE AltName: Full=HCP1 {ECO:0000303|PubMed:8389765};
DE AltName: Full=TM22;
GN Name=PDE7A {ECO:0000303|PubMed:9195912, ECO:0000312|HGNC:HGNC:8791};
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 PDE7A1), FUNCTION, CATALYTIC ACTIVITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8389765; DOI=10.1016/s0021-9258(18)31474-1;
RA Michaeli T., Bloom T.J., Martins T., Loughney K., Ferguson K., Riggs M.,
RA Rodgers L., Beavo J.A., Wigler M.;
RT "Isolation and characterization of a previously undetected human cAMP
RT phosphodiesterase by complementation of cAMP phosphodiesterase-deficient
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 268:12925-12932(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE7A2), FUNCTION, CATALYTIC ACTIVITY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Skeletal muscle;
RX PubMed=9195912; DOI=10.1074/jbc.272.26.16152;
RA Han P., Zhu X., Michaeli T.;
RT "Alternative splicing of the high affinity cAMP-specific phosphodiesterase
RT (PDE7A) mRNA in human skeletal muscle and heart.";
RL J. Biol. Chem. 272:16152-16157(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE7A3).
RX PubMed=11371644; DOI=10.1073/pnas.101131098;
RA Glavas N.A., Ostenson C., Schaefer J.B., Vasta V., Beavo J.A.;
RT "T cell activation up-regulates cyclic nucleotide phosphodiesterases 8A1
RT and 7A3.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6319-6324(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE7A1).
RC TISSUE=Kidney, and Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE7A2).
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 [7]
RP INTERACTION WITH CBFA2T3.
RX PubMed=15470020; DOI=10.4049/jimmunol.173.8.4806;
RA Asirvatham A.L., Galligan S.G., Schillace R.V., Davey M.P., Vasta V.,
RA Beavo J.A., Carr D.W.;
RT "A-kinase anchoring proteins interact with phosphodiesterases in T
RT lymphocyte cell lines.";
RL J. Immunol. 173:4806-4814(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 130-482 IN COMPLEX WITH METAL
RP IONS AND THE INHIBITOR IBMX, AND ACTIVITY REGULATION.
RX PubMed=15994308; DOI=10.1074/jbc.m504398200;
RA Wang H., Liu Y., Chen Y., Robinson H., Ke H.;
RT "Multiple elements jointly determine inhibitor selectivity of cyclic
RT nucleotide phosphodiesterases 4 and 7.";
RL J. Biol. Chem. 280:30949-30955(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 139-456 IN COMPLEX WITH METAL
RP IONS, FUNCTION, AND COFACTOR.
RX PubMed=19350606; DOI=10.1002/cmdc.200900043;
RA Castano T., Wang H., Campillo N.E., Ballester S., Gonzalez-Garcia C.,
RA Hernandez J., Perez C., Cuenca J., Perez-Castillo A., Martinez A.,
RA Huertas O., Gelpi J.L., Luque F.J., Ke H., Gil C.;
RT "Synthesis, structural analysis, and biological evaluation of
RT thioxoquinazoline derivatives as phosphodiesterase 7 inhibitors.";
RL ChemMedChem 4:866-876(2009).
CC -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC regulator of many important physiological processes (PubMed:8389765,
CC PubMed:9195912, PubMed:19350606). May have a role in muscle signal
CC transduction (PubMed:9195912). {ECO:0000269|PubMed:19350606,
CC ECO:0000269|PubMed:8389765, ECO:0000269|PubMed:9195912}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC ChEBI:CHEBI:456215; EC=3.1.4.53;
CC Evidence={ECO:0000269|PubMed:8389765, ECO:0000269|PubMed:9195912};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:19350606};
CC Note=Binds 2 divalent metal cations per subunit (PubMed:19350606). Site
CC 1 may preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions (PubMed:19350606).
CC {ECO:0000269|PubMed:19350606};
CC -!- ACTIVITY REGULATION: Insensitive to all selective PDE inhibitors.
CC {ECO:0000269|PubMed:15994308}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 uM for 3',5'-cyclic AMP {ECO:0000269|PubMed:8389765};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000269|PubMed:8389765,
CC ECO:0000269|PubMed:9195912}.
CC -!- SUBUNIT: Interacts with CBFA2T3. {ECO:0000269|PubMed:15470020,
CC ECO:0000269|PubMed:15994308, ECO:0000269|PubMed:19350606}.
CC -!- SUBCELLULAR LOCATION: [Isoform PDE7A1]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:9195912}. Note=PDE7A1 (57 kDa) is located mostly to
CC soluble cellular fractions. {ECO:0000269|PubMed:9195912}.
CC -!- SUBCELLULAR LOCATION: [Isoform PDE7A2]: Cytoplasm
CC {ECO:0000269|PubMed:9195912}. Note=PDE7A2 (50 kDa) is located to
CC particulate cellular fractions. {ECO:0000269|PubMed:9195912}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=PDE7A1 {ECO:0000303|PubMed:9195912};
CC IsoId=Q13946-1; Sequence=Displayed;
CC Name=PDE7A2 {ECO:0000303|PubMed:9195912};
CC IsoId=Q13946-2; Sequence=VSP_004593;
CC Name=PDE7A3 {ECO:0000303|PubMed:11371644};
CC IsoId=Q13946-3; Sequence=VSP_038645, VSP_038646;
CC -!- TISSUE SPECIFICITY: [Isoform PDE7A1]: Found at high levels in skeletal
CC muscle and at low levels in a variety of tissues including brain and
CC heart (PubMed:9195912). It is expressed as well in two T-cell lines
CC (PubMed:9195912). {ECO:0000269|PubMed:9195912}.
CC -!- TISSUE SPECIFICITY: [Isoform PDE7A2]: Found abundantly in skeletal
CC muscle and at low levels in heart. {ECO:0000269|PubMed:9195912}.
CC -!- DEVELOPMENTAL STAGE: [Isoform PDE7A1]: Developmentally regulated
CC (PubMed:9195912). PDE7A1 and PDE7A2 are found in several fetal tissues,
CC expression is reduced throughout development (PubMed:9195912). It
CC persists strongly only in adult skeletal muscle (PubMed:9195912).
CC {ECO:0000269|PubMed:9195912}.
CC -!- DEVELOPMENTAL STAGE: [Isoform PDE7A2]: Developmentally regulated
CC (PubMed:9195912). PDE7A1 and PDE7A2 are found in several fetal tissues,
CC expression is reduced throughout development (PubMed:9195912). It
CC persists strongly only in adult skeletal muscle (PubMed:9195912).
CC {ECO:0000269|PubMed:9195912}.
CC -!- DOMAIN: Composed of a C-terminal catalytic domain containing two
CC putative divalent metal sites and an N-terminal regulatory domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE7 subfamily. {ECO:0000305}.
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DR EMBL; L12052; AAA35644.2; -; mRNA.
DR EMBL; U67932; AAB65772.1; -; mRNA.
DR EMBL; AF332652; AAK57640.1; -; mRNA.
DR EMBL; AK290801; BAF83490.1; -; mRNA.
DR EMBL; AK292680; BAF85369.1; -; mRNA.
DR EMBL; AC055822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126360; AAI26361.1; -; mRNA.
DR CCDS; CCDS34901.1; -. [Q13946-2]
DR CCDS; CCDS56538.1; -. [Q13946-1]
DR RefSeq; NP_001229247.1; NM_001242318.2. [Q13946-1]
DR RefSeq; NP_002594.1; NM_002603.3. [Q13946-2]
DR RefSeq; XP_011515842.1; XM_011517540.2. [Q13946-2]
DR PDB; 1ZKL; X-ray; 1.67 A; A=130-482.
DR PDB; 3G3N; X-ray; 2.40 A; A=139-456.
DR PDB; 4PM0; X-ray; 2.10 A; A=130-482.
DR PDB; 4Y2B; X-ray; 2.20 A; A=130-482.
DR PDBsum; 1ZKL; -.
DR PDBsum; 3G3N; -.
DR PDBsum; 4PM0; -.
DR PDBsum; 4Y2B; -.
DR AlphaFoldDB; Q13946; -.
DR SMR; Q13946; -.
DR BioGRID; 111176; 15.
DR IntAct; Q13946; 5.
DR STRING; 9606.ENSP00000385632; -.
DR BindingDB; Q13946; -.
DR ChEMBL; CHEMBL3012; -.
DR DrugBank; DB08602; 3-(2,6-difluorophenyl)-2-(methylthio)quinazolin-4(3H)-one.
DR DrugBank; DB07954; 3-isobutyl-1-methyl-7H-xanthine.
DR DrugBank; DB00201; Caffeine.
DR DrugBank; DB09283; Trapidil.
DR DrugCentral; Q13946; -.
DR GuidetoPHARMACOLOGY; 1305; -.
DR iPTMnet; Q13946; -.
DR PhosphoSitePlus; Q13946; -.
DR BioMuta; PDE7A; -.
DR DMDM; 3182958; -.
DR EPD; Q13946; -.
DR jPOST; Q13946; -.
DR MassIVE; Q13946; -.
DR MaxQB; Q13946; -.
DR PaxDb; Q13946; -.
DR PeptideAtlas; Q13946; -.
DR PRIDE; Q13946; -.
DR ProteomicsDB; 59762; -. [Q13946-1]
DR ProteomicsDB; 59763; -. [Q13946-2]
DR ProteomicsDB; 59764; -. [Q13946-3]
DR Antibodypedia; 4363; 201 antibodies from 28 providers.
DR DNASU; 5150; -.
DR Ensembl; ENST00000379419.8; ENSP00000368730.4; ENSG00000205268.11. [Q13946-2]
DR Ensembl; ENST00000396642.7; ENSP00000379881.3; ENSG00000205268.11. [Q13946-3]
DR Ensembl; ENST00000401827.8; ENSP00000385632.4; ENSG00000205268.11. [Q13946-1]
DR GeneID; 5150; -.
DR KEGG; hsa:5150; -.
DR MANE-Select; ENST00000401827.8; ENSP00000385632.4; NM_001242318.3; NP_001229247.1.
DR UCSC; uc003xvp.4; human. [Q13946-1]
DR CTD; 5150; -.
DR DisGeNET; 5150; -.
DR GeneCards; PDE7A; -.
DR HGNC; HGNC:8791; PDE7A.
DR HPA; ENSG00000205268; Tissue enhanced (lymphoid tissue, tongue).
DR MIM; 171885; gene.
DR neXtProt; NX_Q13946; -.
DR OpenTargets; ENSG00000205268; -.
DR PharmGKB; PA33139; -.
DR VEuPathDB; HostDB:ENSG00000205268; -.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000157658; -.
DR HOGENOM; CLU_005940_6_5_1; -.
DR OMA; PMGITLI; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; Q13946; -.
DR TreeFam; TF314638; -.
DR BRENDA; 3.1.4.53; 2681.
DR PathwayCommons; Q13946; -.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR SignaLink; Q13946; -.
DR UniPathway; UPA00762; UER00747.
DR BioGRID-ORCS; 5150; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; PDE7A; human.
DR EvolutionaryTrace; Q13946; -.
DR GeneWiki; PDE7A; -.
DR GenomeRNAi; 5150; -.
DR Pharos; Q13946; Tclin.
DR PRO; PR:Q13946; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q13946; protein.
DR Bgee; ENSG00000205268; Expressed in secondary oocyte and 186 other tissues.
DR ExpressionAtlas; Q13946; baseline and differential.
DR Genevisible; Q13946; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; cAMP; Cytoplasm; Hydrolase;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..482
FT /note="High affinity cAMP-specific 3',5'-cyclic
FT phosphodiesterase 7A"
FT /id="PRO_0000198833"
FT DOMAIN 136..458
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O76083"
FT BINDING 216
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15994308,
FT ECO:0000269|PubMed:19350606"
FT BINDING 252
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15994308,
FT ECO:0000269|PubMed:19350606"
FT BINDING 253
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15994308,
FT ECO:0000269|PubMed:19350606"
FT BINDING 253
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15994308,
FT ECO:0000269|PubMed:19350606"
FT BINDING 362
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15994308,
FT ECO:0000269|PubMed:19350606"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..46
FT /note="MEVCYQLPVLPLDRPVPQHVLSRRGAISFSSSSALFGCPNPRQLSQ -> MG
FT ITLIWCLALVLIKWITSK (in isoform PDE7A2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9195912"
FT /id="VSP_004593"
FT VAR_SEQ 416..424
FT /note="FMTYLVEPL -> NYTYLDIAG (in isoform PDE7A3)"
FT /evidence="ECO:0000303|PubMed:11371644"
FT /id="VSP_038645"
FT VAR_SEQ 425..482
FT /note="Missing (in isoform PDE7A3)"
FT /evidence="ECO:0000303|PubMed:11371644"
FT /id="VSP_038646"
FT VARIANT 76
FT /note="G -> E (in dbSNP:rs11557049)"
FT /id="VAR_056661"
FT CONFLICT 204
FT /note="D -> G (in Ref. 4; BAF83490)"
FT /evidence="ECO:0000305"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:1ZKL"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:1ZKL"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:1ZKL"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:1ZKL"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 280..296
FT /evidence="ECO:0007829|PDB:1ZKL"
FT TURN 297..301
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 304..319
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 326..339
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 370..393
FT /evidence="ECO:0007829|PDB:1ZKL"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 409..419
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 421..431
FT /evidence="ECO:0007829|PDB:1ZKL"
FT HELIX 435..453
FT /evidence="ECO:0007829|PDB:1ZKL"
SQ SEQUENCE 482 AA; 55505 MW; 3B3C8F6E9154F88C CRC64;
MEVCYQLPVL PLDRPVPQHV LSRRGAISFS SSSALFGCPN PRQLSQRRGA ISYDSSDQTA
LYIRMLGDVR VRSRAGFESE RRGSHPYIDF RIFHSQSEIE VSVSARNIRR LLSFQRYLRS
SRFFRGTAVS NSLNILDDDY NGQAKCMLEK VGNWNFDIFL FDRLTNGNSL VSLTFHLFSL
HGLIEYFHLD MMKLRRFLVM IQEDYHSQNP YHNAVHAADV TQAMHCYLKE PKLANSVTPW
DILLSLIAAA THDLDHPGVN QPFLIKTNHY LATLYKNTSV LENHHWRSAV GLLRESGLFS
HLPLESRQQM ETQIGALILA TDISRQNEYL SLFRSHLDRG DLCLEDTRHR HLVLQMALKC
ADICNPCRTW ELSKQWSEKV TEEFFHQGDI EKKYHLGVSP LCDRHTESIA NIQIGFMTYL
VEPLFTEWAR FSNTRLSQTM LGHVGLNKAS WKGLQREQSS SEDTDAAFEL NSQLLPQENR
LS
