APC7_HUMAN
ID APC7_HUMAN Reviewed; 565 AA.
AC Q9UJX3; Q96AC4; Q96GF4; Q9BU24; Q9NT16;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 5.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Anaphase-promoting complex subunit 7 {ECO:0000305};
DE Short=APC7;
DE AltName: Full=Cyclosome subunit 7;
GN Name=ANAPC7 {ECO:0000312|HGNC:HGNC:17380}; 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] (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 110-565 (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 282-565 (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 1-147, HOMODIMERIZATION, TPR
RP REPEATS, AND MUTAGENESIS OF LEU-22 AND LEU-26.
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 1-506 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 -!- SEQUENCE CAUTION:
CC Sequence=AAF05754.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH17316.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AF191340; AAF05754.1; ALT_INIT; 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 CCDS; CCDS44971.1; -. [Q9UJX3-2]
DR CCDS; CCDS9145.2; -. [Q9UJX3-1]
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=1-147.
DR PDB; 4UI9; EM; 3.60 A; X/Y=1-506.
DR PDB; 5A31; EM; 4.30 A; X/Y=1-506.
DR PDB; 5G04; EM; 4.00 A; X/Y=1-506.
DR PDB; 5G05; EM; 3.40 A; X/Y=1-506.
DR PDB; 5KHR; EM; 6.10 A; X/Y=1-565.
DR PDB; 5KHU; EM; 4.80 A; X/Y=1-565.
DR PDB; 5L9T; EM; 6.40 A; X/Y=1-565.
DR PDB; 5L9U; EM; 6.40 A; X/Y=1-565.
DR PDB; 5LCW; EM; 4.00 A; X/Y=1-506.
DR PDB; 6Q6G; EM; 3.20 A; Y/Z=1-521.
DR PDB; 6Q6H; EM; 3.20 A; Y/Z=1-521.
DR PDB; 6TLJ; EM; 3.80 A; X/Y=1-506.
DR PDB; 6TM5; EM; 3.90 A; X/Y=1-506.
DR PDB; 6TNT; EM; 3.78 A; X/Y=1-506.
DR PDB; 7QE7; EM; 2.90 A; Y/Z=1-565.
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 PDBsum; 7QE7; -.
DR AlphaFoldDB; Q9UJX3; -.
DR BioGRID; 119538; 154.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR CORUM; Q9UJX3; -.
DR DIP; DIP-39765N; -.
DR ELM; Q9UJX3; -.
DR IntAct; Q9UJX3; 52.
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 MaxQB; 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; 97 antibodies from 26 providers.
DR DNASU; 51434; -.
DR Ensembl; ENST00000450008.3; ENSP00000402314.3; ENSG00000196510.14. [Q9UJX3-2]
DR Ensembl; ENST00000455511.9; ENSP00000394394.4; ENSG00000196510.14. [Q9UJX3-1]
DR GeneID; 51434; -.
DR KEGG; hsa:51434; -.
DR MANE-Select; ENST00000455511.9; ENSP00000394394.4; NM_016238.3; NP_057322.3.
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 OpenTargets; ENSG00000196510; -.
DR PharmGKB; PA134901290; -.
DR VEuPathDB; HostDB:ENSG00000196510; -.
DR eggNOG; KOG1174; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
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-68867; Assembly of the pre-replicative complex.
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 SignaLink; Q9UJX3; -.
DR SIGNOR; Q9UJX3; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 51434; 23 hits in 1087 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 pancreatic ductal cell and 184 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 GO; GO:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR DisProt; DP01479; -.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 3.
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..565
FT /note="Anaphase-promoting complex subunit 7"
FT /id="PRO_0000106261"
FT REPEAT 101..134
FT /note="TPR 1"
FT REPEAT 169..202
FT /note="TPR 2"
FT REPEAT 203..236
FT /note="TPR 3"
FT REPEAT 237..270
FT /note="TPR 4"
FT REPEAT 339..372
FT /note="TPR 5"
FT REPEAT 373..406
FT /note="TPR 6"
FT REPEAT 407..441
FT /note="TPR 7"
FT REPEAT 442..474
FT /note="TPR 8"
FT REPEAT 475..508
FT /note="TPR 9"
FT REPEAT 509..531
FT /note="TPR 10"
FT REGION 513..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..548
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVM3"
FT VAR_SEQ 503..565
FT /note="SLDPNDQKSLEGMQKMEKEESPTDATQEEDVDDMEGSGEEGDLEGSDSEAAQ
FT WADQEQWFGMQ -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039043"
FT MUTAGEN 22
FT /note="L->R: Loss of homodimerization; when associated with
FT K-26."
FT /evidence="ECO:0000269|PubMed:19091741"
FT MUTAGEN 26
FT /note="L->K: Loss of homodimerization; when associated with
FT R-22."
FT /evidence="ECO:0000269|PubMed:19091741"
FT CONFLICT 150
FT /note="Q -> R (in Ref. 1; AAF05754)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="P -> L (in Ref. 1; AAF05754)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="S -> R (in Ref. 3; CAB70828)"
FT /evidence="ECO:0000305"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:3FFL"
FT HELIX 16..32
FT /evidence="ECO:0007829|PDB:3FFL"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:3FFL"
FT HELIX 59..74
FT /evidence="ECO:0007829|PDB:3FFL"
FT HELIX 101..114
FT /evidence="ECO:0007829|PDB:3FFL"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:3FFL"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3FFL"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:3FFL"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 255..266
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 321..334
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 339..352
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 355..368
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 373..385
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 389..403
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 424..437
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 442..454
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 459..469
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 475..487
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 491..504
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 509..520
FT /evidence="ECO:0007829|PDB:7QE7"
SQ SEQUENCE 565 AA; 63133 MW; B86B7145E9E03EC3 CRC64;
MNVIDHVRDM AAAGLHSNVR LLSSLLLTMS NNNPELFSPP QKYQLLVYHA DSLFHDKEYR
NAVSKYTMAL QQKKALSKTS KVRPSTGNSA STPQSQCLPS EIEVKYKMAE CYTMLKQDKD
AIAILDGIPS RQRTPKINMM LANLYKKAGQ ERPSVTSYKE VLRQCPLALD AILGLLSLSV
KGAEVASMTM NVIQTVPNLD WLSVWIKAYA FVHTGDNSRA ISTICSLEKK SLLRDNVDLL
GSLADLYFRA GDNKNSVLKF EQAQMLDPYL IKGMDVYGYL LAREGRLEDV ENLGCRLFNI
SDQHAEPWVV SGCHSFYSKR YSRALYLGAK AIQLNSNSVQ ALLLKGAALR NMGRVQEAII
HFREAIRLAP CRLDCYEGLI ECYLASNSIR EAMVMANNVY KTLGANAQTL TLLATVCLED
PVTQEKAKTL LDKALTQRPD YIKAVVKKAE LLSREQKYED GIALLRNALA NQSDCVLHRI
LGDFLVAVNE YQEAMDQYSI ALSLDPNDQK SLEGMQKMEK EESPTDATQE EDVDDMEGSG
EEGDLEGSDS EAAQWADQEQ WFGMQ
