ARP8_HUMAN
ID ARP8_HUMAN Reviewed; 624 AA.
AC Q9H981; B3KSW7; Q8N566; Q9H663;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Actin-related protein 8;
DE Short=hArp8;
DE AltName: Full=INO80 complex subunit N;
GN Name=ACTR8; Synonyms=ARP8, INO80N;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Small intestine;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [4]
RP IDENTIFICATION IN INO80 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16230350; DOI=10.1074/jbc.m509128200;
RA Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K.,
RA Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P.,
RA Conaway R.C., Conaway J.W.;
RT "A mammalian chromatin remodeling complex with similarities to the yeast
RT INO80 complex.";
RL J. Biol. Chem. 280:41207-41212(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP FUNCTION IN MITOSIS, INTERACTION WITH ACTR5, AND SUBCELLULAR LOCATION.
RX PubMed=18163988; DOI=10.1016/j.yexcr.2007.11.020;
RA Aoyama N., Oka A., Kitayama K., Kurumizaka H., Harata M.;
RT "The actin-related protein hArp8 accumulates on the mitotic chromosomes and
RT functions in chromosome alignment.";
RL Exp. Cell Res. 314:859-868(2008).
RN [7]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18922472; DOI=10.1016/j.molcel.2008.08.027;
RA Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P.,
RA Florens L., Conaway R.C., Cohen R.E., Conaway J.W.;
RT "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the
RT proteasome and in the Ino80 chromatin-remodeling complex.";
RL Mol. Cell 31:909-917(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=21303910; DOI=10.1074/jbc.m111.222505;
RA Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
RA Conaway J.W., Conaway R.C.;
RT "Subunit organization of the human INO80 chromatin remodeling complex: An
RT evolutionarily conserved core complex catalyzes ATP-dependent nucleosome
RT remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-412, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 34-624, FUNCTION, SUBUNIT, AND
RP ATP-BINDING SITES.
RX PubMed=22977180; DOI=10.1093/nar/gks842;
RA Gerhold C.B., Winkler D.D., Lakomek K., Seifert F.U., Fenn S., Kessler B.,
RA Witte G., Luger K., Hopfner K.P.;
RT "Structure of Actin-related protein 8 and its contribution to nucleosome
RT binding.";
RL Nucleic Acids Res. 40:11036-11046(2012).
CC -!- FUNCTION: Plays an important role in the functional organization of
CC mitotic chromosomes. Exhibits low basal ATPase activity, and unable to
CC polymerize.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling INO80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. Required for the recruitment of
CC INO80 (and probably the INO80 complex) to sites of DNA damage. Strongly
CC prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting
CC it may act as a nucleosome recognition module within the complex.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the DBINO domain
CC of INO80. Interacts with ACTR5; the interaction is observed in
CC asynchronous (interphase) cells but not in metaphase-arrested cells
CC indicative for a possible dissociation of the INO80 complex in mitotic
CC cells. Exists as monomers and dimers, but the dimer is most probably
CC the biologically relevant form required for stable interactions with
CC histones that exploits the twofold symmetry of the nucleosome core.
CC {ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:18163988,
CC ECO:0000269|PubMed:18922472, ECO:0000269|PubMed:21303910,
CC ECO:0000269|PubMed:22977180}.
CC -!- INTERACTION:
CC Q9H981; Q9H9F9: ACTR5; NbExp=3; IntAct=EBI-769597, EBI-769418;
CC Q9H981; Q9Y5K5: UCHL5; NbExp=3; IntAct=EBI-769597, EBI-1051183;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18163988}. Chromosome
CC {ECO:0000269|PubMed:18163988}. Note=Specifically localizes to mitotic
CC chromosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H981-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H981-2; Sequence=VSP_040507;
CC Name=3;
CC IsoId=Q9H981-3; Sequence=VSP_040506, VSP_040508;
CC -!- SIMILARITY: Belongs to the actin family. ARP8 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15402.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK022996; BAB14352.1; -; mRNA.
DR EMBL; AK094507; BAG52879.1; -; mRNA.
DR EMBL; AK026232; BAB15402.1; ALT_INIT; mRNA.
DR EMBL; AC012467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032744; AAH32744.1; -; mRNA.
DR CCDS; CCDS2875.1; -. [Q9H981-1]
DR RefSeq; NP_075050.3; NM_022899.4. [Q9H981-1]
DR RefSeq; XP_005265644.1; XM_005265587.4. [Q9H981-1]
DR RefSeq; XP_011532551.1; XM_011534249.2. [Q9H981-2]
DR PDB; 4FO0; X-ray; 2.60 A; A=34-624.
DR PDBsum; 4FO0; -.
DR AlphaFoldDB; Q9H981; -.
DR SMR; Q9H981; -.
DR BioGRID; 125062; 67.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR CORUM; Q9H981; -.
DR IntAct; Q9H981; 26.
DR MINT; Q9H981; -.
DR STRING; 9606.ENSP00000336842; -.
DR iPTMnet; Q9H981; -.
DR PhosphoSitePlus; Q9H981; -.
DR BioMuta; ACTR8; -.
DR DMDM; 116241257; -.
DR EPD; Q9H981; -.
DR jPOST; Q9H981; -.
DR MassIVE; Q9H981; -.
DR MaxQB; Q9H981; -.
DR PaxDb; Q9H981; -.
DR PeptideAtlas; Q9H981; -.
DR PRIDE; Q9H981; -.
DR ProteomicsDB; 81292; -. [Q9H981-1]
DR ProteomicsDB; 81293; -. [Q9H981-2]
DR ProteomicsDB; 81294; -. [Q9H981-3]
DR Antibodypedia; 31436; 53 antibodies from 15 providers.
DR DNASU; 93973; -.
DR Ensembl; ENST00000335754.8; ENSP00000336842.3; ENSG00000113812.14. [Q9H981-1]
DR Ensembl; ENST00000482349.5; ENSP00000419429.1; ENSG00000113812.14. [Q9H981-2]
DR GeneID; 93973; -.
DR KEGG; hsa:93973; -.
DR MANE-Select; ENST00000335754.8; ENSP00000336842.3; NM_022899.5; NP_075050.3.
DR UCSC; uc003dhc.5; human. [Q9H981-1]
DR CTD; 93973; -.
DR DisGeNET; 93973; -.
DR GeneCards; ACTR8; -.
DR HGNC; HGNC:14672; ACTR8.
DR HPA; ENSG00000113812; Low tissue specificity.
DR MIM; 619716; gene.
DR neXtProt; NX_Q9H981; -.
DR OpenTargets; ENSG00000113812; -.
DR PharmGKB; PA24491; -.
DR VEuPathDB; HostDB:ENSG00000113812; -.
DR eggNOG; KOG0797; Eukaryota.
DR GeneTree; ENSGT00390000001763; -.
DR HOGENOM; CLU_006974_1_0_1; -.
DR InParanoid; Q9H981; -.
DR OMA; CFIQESL; -.
DR OrthoDB; 1258783at2759; -.
DR PhylomeDB; Q9H981; -.
DR TreeFam; TF324575; -.
DR PathwayCommons; Q9H981; -.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q9H981; -.
DR BioGRID-ORCS; 93973; 503 hits in 1085 CRISPR screens.
DR ChiTaRS; ACTR8; human.
DR GenomeRNAi; 93973; -.
DR Pharos; Q9H981; Tbio.
DR PRO; PR:Q9H981; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H981; protein.
DR Bgee; ENSG00000113812; Expressed in stromal cell of endometrium and 176 other tissues.
DR ExpressionAtlas; Q9H981; baseline and differential.
DR Genevisible; Q9H981; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IMP:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR DisProt; DP00873; -.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR027668; Arp8/plant_Arp9.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF13; PTHR11937:SF13; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell cycle;
KW Cell division; Chromosome; DNA damage; DNA recombination; DNA repair;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..624
FT /note="Actin-related protein 8"
FT /id="PRO_0000089123"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 283..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..250
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040506"
FT VAR_SEQ 1..111
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040507"
FT VAR_SEQ 305..354
FT /note="LCLAYGGSDVSRCFYWLMQRAGFPYRECQLTNKMDCLLLQHLKETFCHLD
FT -> IFSWN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040508"
FT VARIANT 56
FT /note="T -> I (in dbSNP:rs3733082)"
FT /id="VAR_028033"
FT CONFLICT 596
FT /note="D -> G (in Ref. 1; BAB14352)"
FT /evidence="ECO:0000305"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4FO0"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:4FO0"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 266..274
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 374..381
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 384..390
FT /evidence="ECO:0007829|PDB:4FO0"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 503..506
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 511..520
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 525..533
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 534..540
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 547..558
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 561..566
FT /evidence="ECO:0007829|PDB:4FO0"
FT STRAND 571..575
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 576..578
FT /evidence="ECO:0007829|PDB:4FO0"
FT TURN 581..583
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 584..594
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 596..600
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 605..611
FT /evidence="ECO:0007829|PDB:4FO0"
FT HELIX 614..619
FT /evidence="ECO:0007829|PDB:4FO0"
SQ SEQUENCE 624 AA; 70484 MW; DA71C49B9D2C4E19 CRC64;
MTQAEKGDTE NGKEKGGEKE KEQRGVKRPI VPALVPESLQ EQIQSNFIIV IHPGSTTLRI
GRATDTLPAS IPHVIARRHK QQGQPLYKDS WLLREGLNKP ESNEQRQNGL KMVDQAIWSK
KMSNGTRRIP VSPEQARSYN KQMRPAILDH CSGNKWTNTS HHPEYLVGEE ALYVNPLDCY
NIHWPIRRGQ LNIHPGPGGS LTAVLADIEV IWSHAIQKYL EIPLKDLKYY RCILLIPDIY
NKQHVKELVN MILMKMGFSG IVVHQESVCA TYGSGLSSTC IVDVGDQKTS VCCVEDGVSH
RNTRLCLAYG GSDVSRCFYW LMQRAGFPYR ECQLTNKMDC LLLQHLKETF CHLDQDISGL
QDHEFQIRHP DSPALLYQFR LGDEKLQAPM ALFYPATFGI VGQKMTTLQH RSQGDPEDPH
DEHYLLATQS KQEQSAKATA DRKSASKPIG FEGDLRGQSS DLPERLHSQE VDLGSAQGDG
LMAGNDSEEA LTALMSRKTA ISLFEGKALG LDKAILHSID CCSSDDTKKK MYSSILVVGG
GLMFHKAQEF LQHRILNKMP PSFRRIIENV DVITRPKDMD PRLIAWKGGA VLACLDTTQE
LWIYQREWQR FGVRMLRERA AFVW
