ORC2_HUMAN
ID ORC2_HUMAN Reviewed; 577 AA.
AC Q13416; Q13204; Q53TX5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Origin recognition complex subunit 2;
GN Name=ORC2; Synonyms=ORC2L;
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].
RX PubMed=7502077; DOI=10.1126/science.270.5242.1667;
RA Gavin K.A., Hidaka M., Stillman B.D.;
RT "Conserved initiator proteins in eukaryotes.";
RL Science 270:1667-1671(1995).
RN [2]
RP SEQUENCE REVISION TO 41-42.
RA Hidaka M., Stillman B.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8808289; DOI=10.1006/geno.1996.0018;
RA Takahara K., Bong M., Brevard R., Eddy R.L., Haley L.L., Sait S.J.,
RA Shows T.B., Hoffman G.G., Greenspan D.S.;
RT "Mouse and human homologues of the yeast origin of replication recognition
RT complex subunit ORC2 and chromosomal localization of the cognate human gene
RT ORC2L.";
RL Genomics 31:119-122(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-106 AND GLN-521.
RG NIEHS SNPs program;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [8]
RP INTERACTION WITH MCM10.
RX PubMed=11095689; DOI=10.1093/nar/28.23.4769;
RA Izumi M., Yanagi K., Mizuno T., Yokoi M., Kawasaki Y., Moon K.Y.,
RA Hurwitz J., Yatagai F., Hanaoka F.;
RT "The human homolog of Saccharomyces cerevisiae Mcm10 interacts with
RT replication factors and dissociates from nuclease-resistant nuclear
RT structures in G(2) phase.";
RL Nucleic Acids Res. 28:4769-4777(2000).
RN [9]
RP IDENTIFICATION IN THE ORC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP ASSEMBLY OF THE ORC COMPLEX.
RX PubMed=12909626; DOI=10.1074/jbc.m307535200;
RA Ohta S., Tatsumi Y., Fujita M., Tsurimoto T., Obuse C.;
RT "The ORC1 cycle in human cells: II. Dynamic changes in the human ORC
RT complex during the cell cycle.";
RL J. Biol. Chem. 278:41535-41540(2003).
RN [10]
RP RECONSTITUTION OF THE ORC COMPLEX, AND DISASSEMBLY OF THE ORC COMPLEX.
RX PubMed=17716973; DOI=10.1074/jbc.m705905200;
RA Siddiqui K., Stillman B.;
RT "ATP-dependent assembly of the human origin recognition complex.";
RL J. Biol. Chem. 282:32370-32383(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-116 AND SER-280, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-116; SER-122; SER-138 AND
RP THR-226, AND IDENTIFICATION BY 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 [13]
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 [14]
RP FUNCTION, AND INTERACTION WITH LRWD1.
RX PubMed=22935713; DOI=10.4161/cc.21870;
RA Shen Z., Prasanth S.G.;
RT "Orc2 protects ORCA from ubiquitin-mediated degradation.";
RL Cell Cycle 11:3578-3589(2012).
RN [15]
RP FUNCTION, AND BINDING TO HISTONE H3 AND H4 TRIMETHYLATION MARKS.
RX PubMed=22427655; DOI=10.1074/jbc.m111.337980;
RA Chan K.M., Zhang Z.;
RT "Leucine-rich repeat and WD repeat-containing protein 1 is recruited to
RT pericentric heterochromatin by trimethylated lysine 9 of histone H3 and
RT maintains heterochromatin silencing.";
RL J. Biol. Chem. 287:15024-15033(2012).
RN [16]
RP INTERACTION WITH LRWD1.
RX PubMed=22645314; DOI=10.1128/mcb.00362-12;
RA Shen Z., Chakraborty A., Jain A., Giri S., Ha T., Prasanth K.V.,
RA Prasanth S.G.;
RT "Dynamic association of ORCA with prereplicative complex components
RT regulates DNA replication initiation.";
RL Mol. Cell. Biol. 32:3107-3120(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-116; THR-226; SER-248 AND
RP SER-280, AND 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 [18]
RP INTERACTION WITH POLQ.
RX PubMed=24989122; DOI=10.1038/ncomms5285;
RA Fernandez-Vidal A., Guitton-Sert L., Cadoret J.C., Drac M., Schwob E.,
RA Baldacci G., Cazaux C., Hoffmann J.S.;
RT "A role for DNA polymerase theta in the timing of DNA replication.";
RL Nat. Commun. 5:4285-4285(2014).
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication. DNA-binding is ATP-dependent. The specific DNA
CC sequences that define origins of replication have not been identified
CC yet. ORC is required to assemble the pre-replication complex necessary
CC to initiate DNA replication. Binds histone H3 and H4 trimethylation
CC marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting
CC it from ubiquitin-mediated proteasomal degradation. Also stabilizes
CC ORC3. {ECO:0000269|PubMed:22427655, ECO:0000269|PubMed:22935713}.
CC -!- SUBUNIT: Component of ORC, a complex composed of at least 6 subunits:
CC ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle
CC dependent manner. It is sequentially assembled at the exit from
CC anaphase of mitosis and disassembled as cells enter S phase
CC (PubMed:12909626, PubMed:17716973). Interacts with DBF4 (By
CC similarity). Interacts with MCM10 (PubMed:11095689). Interacts with
CC LRWD1 throughout the cell cycle; this interaction, wich occurs only
CC with non-ubiquitinated form of LRWD1, prevents LRWD1 ubiquitination and
CC hence stabilizes the protein (PubMed:22645314). Interacts with POLQ
CC (PubMed:24989122). {ECO:0000250|UniProtKB:Q60862,
CC ECO:0000269|PubMed:11095689, ECO:0000269|PubMed:12909626,
CC ECO:0000269|PubMed:17716973, ECO:0000269|PubMed:22645314,
CC ECO:0000269|PubMed:22935713}.
CC -!- INTERACTION:
CC Q13416; Q99459: CDC5L; NbExp=2; IntAct=EBI-374957, EBI-374880;
CC Q13416; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-374957, EBI-11962928;
CC Q13416; Q08050: FOXM1; NbExp=2; IntAct=EBI-374957, EBI-866480;
CC Q13416; Q7L590: MCM10; NbExp=5; IntAct=EBI-374957, EBI-374912;
CC Q13416; P25205: MCM3; NbExp=2; IntAct=EBI-374957, EBI-355153;
CC Q13416; Q13415: ORC1; NbExp=14; IntAct=EBI-374957, EBI-374847;
CC Q13416; Q9UBD5: ORC3; NbExp=28; IntAct=EBI-374957, EBI-374916;
CC Q13416; O43929: ORC4; NbExp=12; IntAct=EBI-374957, EBI-374889;
CC Q13416; O43913: ORC5; NbExp=15; IntAct=EBI-374957, EBI-374928;
CC Q13416; Q9NS91: RAD18; NbExp=3; IntAct=EBI-374957, EBI-2339393;
CC Q13416; P57055: RIPPLY3; NbExp=3; IntAct=EBI-374957, EBI-12092053;
CC Q13416; Q15554: TERF2; NbExp=3; IntAct=EBI-374957, EBI-706637;
CC Q13416; P03211: EBNA1; Xeno; NbExp=6; IntAct=EBI-374957, EBI-996522;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the ORC2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/orc2l/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U40268; AAC50326.2; -; mRNA.
DR EMBL; U27459; AAB33970.1; -; mRNA.
DR EMBL; AY652588; AAT46690.1; -; Genomic_DNA.
DR EMBL; AC005037; AAY14725.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70228.1; -; Genomic_DNA.
DR EMBL; BC014834; AAH14834.1; -; mRNA.
DR CCDS; CCDS2334.1; -.
DR RefSeq; NP_006181.1; NM_006190.4.
DR RefSeq; XP_006712618.1; XM_006712555.3.
DR PDB; 5C8H; X-ray; 2.01 A; A=458-577.
DR PDB; 5UJ8; X-ray; 6.00 A; E/F/G/H=231-577.
DR PDB; 5UJM; EM; 18.00 A; B=231-577.
DR PDB; 7CTE; EM; 3.80 A; B=1-577.
DR PDB; 7CTF; EM; 4.80 A; B=1-577.
DR PDB; 7CTG; EM; 5.00 A; B=1-577.
DR PDB; 7JPO; EM; 3.20 A; B=1-577.
DR PDB; 7JPP; EM; 3.70 A; B=1-577.
DR PDB; 7JPQ; EM; 3.50 A; B=1-577.
DR PDB; 7JPR; EM; 4.00 A; B=1-577.
DR PDB; 7JPS; EM; 4.40 A; B=1-577.
DR PDBsum; 5C8H; -.
DR PDBsum; 5UJ8; -.
DR PDBsum; 5UJM; -.
DR PDBsum; 7CTE; -.
DR PDBsum; 7CTF; -.
DR PDBsum; 7CTG; -.
DR PDBsum; 7JPO; -.
DR PDBsum; 7JPP; -.
DR PDBsum; 7JPQ; -.
DR PDBsum; 7JPR; -.
DR PDBsum; 7JPS; -.
DR AlphaFoldDB; Q13416; -.
DR SMR; Q13416; -.
DR BioGRID; 111041; 94.
DR ComplexPortal; CPX-1880; Nuclear origin of replication recognition complex.
DR CORUM; Q13416; -.
DR DIP; DIP-29689N; -.
DR ELM; Q13416; -.
DR IntAct; Q13416; 48.
DR MINT; Q13416; -.
DR STRING; 9606.ENSP00000234296; -.
DR iPTMnet; Q13416; -.
DR PhosphoSitePlus; Q13416; -.
DR BioMuta; ORC2; -.
DR DMDM; 8488999; -.
DR EPD; Q13416; -.
DR jPOST; Q13416; -.
DR MassIVE; Q13416; -.
DR MaxQB; Q13416; -.
DR PaxDb; Q13416; -.
DR PeptideAtlas; Q13416; -.
DR PRIDE; Q13416; -.
DR ProteomicsDB; 59395; -.
DR Antibodypedia; 34131; 226 antibodies from 37 providers.
DR DNASU; 4999; -.
DR Ensembl; ENST00000234296.7; ENSP00000234296.2; ENSG00000115942.9.
DR GeneID; 4999; -.
DR KEGG; hsa:4999; -.
DR MANE-Select; ENST00000234296.7; ENSP00000234296.2; NM_006190.5; NP_006181.1.
DR UCSC; uc002uwr.4; human.
DR CTD; 4999; -.
DR DisGeNET; 4999; -.
DR GeneCards; ORC2; -.
DR HGNC; HGNC:8488; ORC2.
DR HPA; ENSG00000115942; Low tissue specificity.
DR MIM; 601182; gene.
DR neXtProt; NX_Q13416; -.
DR OpenTargets; ENSG00000115942; -.
DR PharmGKB; PA32809; -.
DR VEuPathDB; HostDB:ENSG00000115942; -.
DR eggNOG; KOG2928; Eukaryota.
DR GeneTree; ENSGT00390000015228; -.
DR HOGENOM; CLU_018596_3_0_1; -.
DR InParanoid; Q13416; -.
DR OMA; FPQWAFE; -.
DR OrthoDB; 1404162at2759; -.
DR PhylomeDB; Q13416; -.
DR TreeFam; TF101092; -.
DR BRENDA; 3.6.4.B8; 2681.
DR PathwayCommons; Q13416; -.
DR Reactome; R-HSA-113507; E2F-enabled inhibition of pre-replication complex formation.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR SignaLink; Q13416; -.
DR SIGNOR; Q13416; -.
DR BioGRID-ORCS; 4999; 52 hits in 1083 CRISPR screens.
DR ChiTaRS; ORC2; human.
DR GeneWiki; ORC2; -.
DR GeneWiki; ORC2L; -.
DR GenomeRNAi; 4999; -.
DR Pharos; Q13416; Tbio.
DR PRO; PR:Q13416; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q13416; protein.
DR Bgee; ENSG00000115942; Expressed in calcaneal tendon and 175 other tissues.
DR ExpressionAtlas; Q13416; baseline and differential.
DR Genevisible; Q13416; HS.
DR GO; GO:0005813; C:centrosome; IDA:CACAO.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0000792; C:heterochromatin; IDA:CACAO.
DR GO; GO:0000939; C:inner kinetochore; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000808; C:origin recognition complex; IDA:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; TAS:ProtInc.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR InterPro; IPR007220; ORC2.
DR PANTHER; PTHR14052; PTHR14052; 1.
DR Pfam; PF04084; ORC2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..577
FT /note="Origin recognition complex subunit 2"
FT /id="PRO_0000127075"
FT REPEAT 1..100
FT /note="Involved in LRWD1-binding"
FT REGION 81..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 106
FT /note="M -> K (in dbSNP:rs2307361)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014515"
FT VARIANT 521
FT /note="R -> Q (in dbSNP:rs16835624)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_021276"
FT CONFLICT 131
FT /note="I -> V (in Ref. 3; AAB33970)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="T -> L (in Ref. 3; AAB33970)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="I -> M (in Ref. 3; AAB33970)"
FT /evidence="ECO:0000305"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:7JPQ"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 369..382
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 403..413
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 418..424
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 435..440
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 456..463
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:7JPQ"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:7JPQ"
FT HELIX 474..481
FT /evidence="ECO:0007829|PDB:5C8H"
FT HELIX 486..501
FT /evidence="ECO:0007829|PDB:5C8H"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:5C8H"
FT HELIX 513..522
FT /evidence="ECO:0007829|PDB:5C8H"
FT HELIX 529..541
FT /evidence="ECO:0007829|PDB:5C8H"
FT STRAND 546..549
FT /evidence="ECO:0007829|PDB:5C8H"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:5C8H"
FT HELIX 563..572
FT /evidence="ECO:0007829|PDB:5C8H"
SQ SEQUENCE 577 AA; 65972 MW; DF3F9C2CF147DA5F CRC64;
MSKPELKEDK MLEVHFVGDD DVLNHILDRE GGAKLKKERA QLLVNPKKII KKPEYDLEED
DQEVLKDQNY VEIMGRDVQE SLKNGSATGG GNKVYSFQNR KHSEKMAKLA SELAKTPQKS
VSFSLKNDPE ITINVPQSSK GHSASDKVQP KNNDKSEFLS TAPRSLRKRL IVPRSHSDSE
SEYSASNSED DEGVAQEHEE DTNAVIFSQK IQAQNRVVSA PVGKETPSKR MKRDKTSDLV
EEYFEAHSSS KVLTSDRTLQ KLKRAKLDQQ TLRNLLSKVS PSFSAELKQL NQQYEKLFHK
WMLQLHLGFN IVLYGLGSKR DLLERFRTTM LQDSIHVVIN GFFPGISVKS VLNSITEEVL
DHMGTFRSIL DQLDWIVNKF KEDSSLELFL LIHNLDSQML RGEKSQQIIG QLSSLHNIYL
IASIDHLNAP LMWDHAKQSL FNWLWYETTT YSPYTEETSY ENSLLVKQSG SLPLSSLTHV
LRSLTPNARG IFRLLIKYQL DNQDNPSYIG LSFQDFYQQC REAFLVNSDL TLRAQLTEFR
DHKLIRTKKG TDGVEYLLIP VDNGTLTDFL EKEEEEA
