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Database: UniProt
Entry: Q9UJX3
LinkDB: Q9UJX3
Original site: Q9UJX3 
ID   APC7_HUMAN              Reviewed;         599 AA.
AC   Q9UJX3; Q96AC4; Q96GF4; Q9BU24; Q9NT16;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 4.
DT   29-SEP-2021, entry version 196.
DE   RecName: Full=Anaphase-promoting complex subunit 7;
DE            Short=APC7;
DE   AltName: Full=Cyclosome subunit 7;
GN   Name=ANAPC7; Synonyms=APC7;
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] OF 34-599 (ISOFORM 1), AND SUBUNIT.
RX   PubMed=9469815; DOI=10.1126/science.279.5354.1219;
RA   Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W.;
RT   "Identification of a cullin homology region in a subunit of the anaphase-
RT   promoting complex.";
RL   Science 279:1219-1222(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-599 (ISOFORM 1).
RC   TISSUE=Ovary, and Skin;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 316-599 (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   FUNCTION OF THE APC/C.
RX   PubMed=18485873; DOI=10.1016/j.cell.2008.04.012;
RA   Jin L., Williamson A., Banerjee S., Philipp I., Rape M.;
RT   "Mechanism of ubiquitin-chain formation by the human anaphase-promoting
RT   complex.";
RL   Cell 133:653-665(2008).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18445686; DOI=10.1242/jcs.019174;
RA   Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA   Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT   "EML3 is a nuclear microtubule-binding protein required for the correct
RT   alignment of chromosomes in metaphase.";
RL   J. Cell Sci. 121:1718-1726(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
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].
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   [10]
RP   ELECTRON MICROSCOPY OF THE APC/C.
RX   PubMed=16364912; DOI=10.1016/j.molcel.2005.11.008;
RA   Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A.,
RA   Engel A., Peters J.-M., Stark H.;
RT   "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a
RT   cryo-electron microscopy model of vertebrate APC/C.";
RL   Mol. Cell 20:867-879(2005).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 35-181, HOMODIMERIZATION, TPR
RP   REPEATS, AND MUTAGENESIS OF LEU-56 AND LEU-60.
RX   PubMed=19091741; DOI=10.1074/jbc.m804887200;
RA   Han D., Kim K., Kim Y., Kang Y., Lee J.Y., Kim Y.;
RT   "Crystal structure of the N-terminal domain of anaphase-promoting complex
RT   subunit 7.";
RL   J. Biol. Chem. 284:15137-15146(2009).
RN   [12]
RP   STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, AND SUBUNIT.
RX   PubMed=25043029; DOI=10.1038/nature13543;
RA   Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT   "Molecular architecture and mechanism of the anaphase-promoting complex.";
RL   Nature 513:388-393(2014).
RN   [13] {ECO:0007744|PDB:4UI9, ECO:0007744|PDB:5A31}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 35-599 OF APC/C, AND
RP   SUBUNIT.
RX   PubMed=26083744; DOI=10.1038/nature14471;
RA   Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT   "Atomic structure of the APC/C and its mechanism of protein
RT   ubiquitination.";
RL   Nature 522:450-454(2015).
CC   -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC       progression through mitosis and the G1 phase of the cell cycle. The
CC       APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation of
CC       'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC       formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
CC       {ECO:0000269|PubMed:18485873}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: V-shaped homodimer. The mammalian APC/C is composed at least
CC       of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5,
CC       CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13,
CC       ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains
CC       with a combined molecular mass of around 1.2 MDa; APC/C interacts with
CC       FZR1 and FBXO5 (PubMed:25043029, PubMed:26083744).
CC       {ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744,
CC       ECO:0000269|PubMed:9469815}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:18445686}. Nucleus {ECO:0000269|PubMed:18445686}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18445686}.
CC       Note=Localizes to spindle during metaphase and to cytoplasmic
CC       microtubules during interphase. {ECO:0000269|PubMed:18445686}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UJX3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UJX3-2; Sequence=VSP_039043;
CC   -!- SIMILARITY: Belongs to the APC7 family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-35 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH17316.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR   EMBL; AF191340; AAF05754.1; -; mRNA.
DR   EMBL; BC002941; AAH02941.2; -; mRNA.
DR   EMBL; BC009498; AAH09498.2; -; mRNA.
DR   EMBL; BC017316; AAH17316.2; ALT_SEQ; mRNA.
DR   EMBL; AL137586; CAB70828.1; -; mRNA.
DR   PIR; T46297; T46297.
DR   RefSeq; NP_001131136.1; NM_001137664.1. [Q9UJX3-2]
DR   RefSeq; NP_057322.2; NM_016238.2.
DR   PDB; 3FFL; X-ray; 2.50 A; A/B/C/D=35-181.
DR   PDB; 4UI9; EM; 3.60 A; X/Y=35-599.
DR   PDB; 5A31; EM; 4.30 A; X/Y=1-599.
DR   PDB; 5G04; EM; 4.00 A; X/Y=1-599.
DR   PDB; 5G05; EM; 3.40 A; X/Y=1-599.
DR   PDB; 5KHR; EM; 6.10 A; X/Y=35-599.
DR   PDB; 5KHU; EM; 4.80 A; X/Y=35-599.
DR   PDB; 5L9T; EM; 6.40 A; X/Y=35-599.
DR   PDB; 5L9U; EM; 6.40 A; X/Y=35-599.
DR   PDB; 5LCW; EM; 4.00 A; X/Y=1-599.
DR   PDB; 6Q6G; EM; 3.20 A; Y/Z=1-599.
DR   PDB; 6Q6H; EM; 3.20 A; Y/Z=1-599.
DR   PDB; 6TLJ; EM; 3.80 A; X/Y=1-599.
DR   PDB; 6TM5; EM; 3.90 A; X/Y=1-599.
DR   PDB; 6TNT; EM; 3.78 A; X/Y=1-599.
DR   PDBsum; 3FFL; -.
DR   PDBsum; 4UI9; -.
DR   PDBsum; 5A31; -.
DR   PDBsum; 5G04; -.
DR   PDBsum; 5G05; -.
DR   PDBsum; 5KHR; -.
DR   PDBsum; 5KHU; -.
DR   PDBsum; 5L9T; -.
DR   PDBsum; 5L9U; -.
DR   PDBsum; 5LCW; -.
DR   PDBsum; 6Q6G; -.
DR   PDBsum; 6Q6H; -.
DR   PDBsum; 6TLJ; -.
DR   PDBsum; 6TM5; -.
DR   PDBsum; 6TNT; -.
DR   SMR; Q9UJX3; -.
DR   BioGRID; 119538; 113.
DR   ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR   CORUM; Q9UJX3; -.
DR   DIP; DIP-39765N; -.
DR   ELM; Q9UJX3; -.
DR   IntAct; Q9UJX3; 49.
DR   MINT; Q9UJX3; -.
DR   STRING; 9606.ENSP00000394394; -.
DR   iPTMnet; Q9UJX3; -.
DR   PhosphoSitePlus; Q9UJX3; -.
DR   BioMuta; ANAPC7; -.
DR   DMDM; 294862527; -.
DR   EPD; Q9UJX3; -.
DR   jPOST; Q9UJX3; -.
DR   MassIVE; Q9UJX3; -.
DR   PaxDb; Q9UJX3; -.
DR   PeptideAtlas; Q9UJX3; -.
DR   PRIDE; Q9UJX3; -.
DR   ProteomicsDB; 84682; -. [Q9UJX3-1]
DR   ProteomicsDB; 84683; -. [Q9UJX3-2]
DR   TopDownProteomics; Q9UJX3-2; -. [Q9UJX3-2]
DR   Antibodypedia; 4033; 90 antibodies.
DR   DNASU; 51434; -.
DR   Ensembl; ENST00000450008; ENSP00000402314; ENSG00000196510.
DR   Ensembl; ENST00000455511; ENSP00000394394; ENSG00000196510.
DR   GeneID; 51434; -.
DR   KEGG; hsa:51434; -.
DR   UCSC; uc001tqo.2; human. [Q9UJX3-1]
DR   CTD; 51434; -.
DR   DisGeNET; 51434; -.
DR   GeneCards; ANAPC7; -.
DR   HGNC; HGNC:17380; ANAPC7.
DR   HPA; ENSG00000196510; Low tissue specificity.
DR   MIM; 606949; gene.
DR   neXtProt; NX_Q9UJX3; -.
DR   PharmGKB; PA134901290; -.
DR   VEuPathDB; HostDB:ENSG00000196510; -.
DR   eggNOG; KOG1174; Eukaryota.
DR   HOGENOM; CLU_026953_2_0_1; -.
DR   InParanoid; Q9UJX3; -.
DR   OMA; YRFEVYK; -.
DR   PhylomeDB; Q9UJX3; -.
DR   TreeFam; TF105445; -.
DR   PathwayCommons; Q9UJX3; -.
DR   Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR   Reactome; R-HSA-176412; Phosphorylation of the APC/C.
DR   Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR   Reactome; R-HSA-9687136; Aberrant regulation of mitotic exit in cancer due to RB1 defects.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; Q9UJX3; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 51434; 22 hits in 1024 CRISPR screens.
DR   ChiTaRS; ANAPC7; human.
DR   EvolutionaryTrace; Q9UJX3; -.
DR   GeneWiki; ANAPC7; -.
DR   GenomeRNAi; 51434; -.
DR   Pharos; Q9UJX3; Tbio.
DR   PRO; PR:Q9UJX3; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9UJX3; protein.
DR   Bgee; ENSG00000196510; Expressed in esophagus mucosa and 218 other tissues.
DR   ExpressionAtlas; Q9UJX3; baseline and differential.
DR   Genevisible; Q9UJX3; HS.
DR   GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IBA:GO_Central.
DR   GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   DisProt; DP01479; -.
DR   Gene3D; 1.25.40.10; -; 4.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; SSF48452; 2.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW   Cytoplasm; Cytoskeleton; Mitosis; Nucleus; Reference proteome; Repeat;
KW   TPR repeat; Ubl conjugation pathway.
FT   CHAIN           1..599
FT                   /note="Anaphase-promoting complex subunit 7"
FT                   /id="PRO_0000106261"
FT   REPEAT          135..168
FT                   /note="TPR 1"
FT   REPEAT          203..236
FT                   /note="TPR 2"
FT   REPEAT          237..270
FT                   /note="TPR 3"
FT   REPEAT          271..304
FT                   /note="TPR 4"
FT   REPEAT          373..406
FT                   /note="TPR 5"
FT   REPEAT          407..440
FT                   /note="TPR 6"
FT   REPEAT          441..475
FT                   /note="TPR 7"
FT   REPEAT          476..508
FT                   /note="TPR 8"
FT   REPEAT          509..542
FT                   /note="TPR 9"
FT   REPEAT          543..565
FT                   /note="TPR 10"
FT   REGION          547..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..582
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         263
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM3"
FT   VAR_SEQ         537..599
FT                   /note="SLDPNDQKSLEGMQKMEKEESPTDATQEEDVDDMEGSGEEGDLEGSDSEAAQ
FT                   WADQEQWFGMQ -> R (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_039043"
FT   MUTAGEN         56
FT                   /note="L->R: Loss of homodimerization; when associated with
FT                   K-60."
FT                   /evidence="ECO:0000269|PubMed:19091741"
FT   MUTAGEN         60
FT                   /note="L->K: Loss of homodimerization; when associated with
FT                   R-56."
FT                   /evidence="ECO:0000269|PubMed:19091741"
FT   CONFLICT        184
FT                   /note="Q -> R (in Ref. 1; AAF05754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="P -> L (in Ref. 1; AAF05754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        537
FT                   /note="S -> R (in Ref. 3; CAB70828)"
FT                   /evidence="ECO:0000305"
FT   HELIX           37..46
FT                   /evidence="ECO:0007829|PDB:3FFL"
FT   HELIX           50..66
FT                   /evidence="ECO:0007829|PDB:3FFL"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           73..89
FT                   /evidence="ECO:0007829|PDB:3FFL"
FT   HELIX           93..108
FT                   /evidence="ECO:0007829|PDB:3FFL"
FT   HELIX           135..148
FT                   /evidence="ECO:0007829|PDB:3FFL"
FT   HELIX           152..160
FT                   /evidence="ECO:0007829|PDB:3FFL"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:3FFL"
FT   HELIX           169..178
FT                   /evidence="ECO:0007829|PDB:3FFL"
FT   HELIX           185..198
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           203..210
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   TURN            211..213
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           216..222
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           224..229
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   STRAND          230..232
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           235..246
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   TURN            247..249
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           251..264
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           271..284
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           289..300
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           308..317
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           321..332
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   STRAND          336..339
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           340..351
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           355..368
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           373..386
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           389..402
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           407..419
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           423..437
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           441..450
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   TURN            451..453
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           455..457
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           458..469
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           476..488
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           493..503
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           509..519
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   TURN            520..523
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           525..538
FT                   /evidence="ECO:0007829|PDB:6Q6G"
FT   HELIX           543..554
FT                   /evidence="ECO:0007829|PDB:6Q6G"
SQ   SEQUENCE   599 AA;  66855 MW;  D187A1D9DA41DE2C CRC64;
     MDPGDAAILE SSLRILYRLF ESVLPPLPAA LQSRMNVIDH VRDMAAAGLH SNVRLLSSLL
     LTMSNNNPEL FSPPQKYQLL VYHADSLFHD KEYRNAVSKY TMALQQKKAL SKTSKVRPST
     GNSASTPQSQ CLPSEIEVKY KMAECYTMLK QDKDAIAILD GIPSRQRTPK INMMLANLYK
     KAGQERPSVT SYKEVLRQCP LALDAILGLL SLSVKGAEVA SMTMNVIQTV PNLDWLSVWI
     KAYAFVHTGD NSRAISTICS LEKKSLLRDN VDLLGSLADL YFRAGDNKNS VLKFEQAQML
     DPYLIKGMDV YGYLLAREGR LEDVENLGCR LFNISDQHAE PWVVSGCHSF YSKRYSRALY
     LGAKAIQLNS NSVQALLLKG AALRNMGRVQ EAIIHFREAI RLAPCRLDCY EGLIECYLAS
     NSIREAMVMA NNVYKTLGAN AQTLTLLATV CLEDPVTQEK AKTLLDKALT QRPDYIKAVV
     KKAELLSREQ KYEDGIALLR NALANQSDCV LHRILGDFLV AVNEYQEAMD QYSIALSLDP
     NDQKSLEGMQ KMEKEESPTD ATQEEDVDDM EGSGEEGDLE GSDSEAAQWA DQEQWFGMQ
//
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