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   27-MAR-2024, entry version 183.
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/";
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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   EMDB; EMD-22417; -.
DR   EMDB; EMD-22418; -.
DR   EMDB; EMD-22419; -.
DR   EMDB; EMD-22420; -.
DR   EMDB; EMD-22421; -.
DR   EMDB; EMD-30462; -.
DR   EMDB; EMD-30463; -.
DR   EMDB; EMD-30464; -.
DR   SMR; Q13416; -.
DR   BioGRID; 111041; 104.
DR   ComplexPortal; CPX-1880; Nuclear origin recognition complex.
DR   CORUM; Q13416; -.
DR   DIP; DIP-29689N; -.
DR   ELM; Q13416; -.
DR   IntAct; Q13416; 49.
DR   MINT; Q13416; -.
DR   STRING; 9606.ENSP00000234296; -.
DR   GlyGen; Q13416; 2 sites, 1 O-linked glycan (2 sites).
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; 9606-ENSP00000234296; -.
DR   PeptideAtlas; Q13416; -.
DR   ProteomicsDB; 59395; -.
DR   Pumba; Q13416; -.
DR   Antibodypedia; 34131; 254 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   AGR; HGNC:8488; -.
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; AHERYFF; -.
DR   OrthoDB; 9018at2759; -.
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; 70 hits in 1163 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 177 other cell types or tissues.
DR   ExpressionAtlas; Q13416; baseline and differential.
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; IDA:ComplexPortal.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR   InterPro; IPR007220; ORC2.
DR   PANTHER; PTHR14052; ORIGIN RECOGNITION COMPLEX SUBUNIT 2; 1.
DR   PANTHER; PTHR14052:SF0; ORIGIN RECOGNITION COMPLEX SUBUNIT 2; 1.
DR   Pfam; PF04084; ORC2; 1.
DR   Genevisible; Q13416; HS.
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
//