EME1_HUMAN
ID EME1_HUMAN Reviewed; 570 AA.
AC Q96AY2; Q96N62;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Crossover junction endonuclease EME1;
DE EC=3.1.22.-;
DE AltName: Full=MMS4 homolog;
DE Short=hMMS4;
GN Name=EME1; Synonyms=MMS4;
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] (ISOFORM 1), AND VARIANT ASP-69.
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 MRNA] (ISOFORM 2), AND VARIANT ASP-69.
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 [3]
RP FUNCTION, AND INTERACTION WITH MUS81.
RX PubMed=12686547; DOI=10.1074/jbc.m302484200;
RA Oegruenc M., Sancar A.;
RT "Identification and characterization of human MUS81-MMS4 structure-specific
RT endonuclease.";
RL J. Biol. Chem. 278:21715-21720(2003).
RN [4]
RP FUNCTION, AND INTERACTION WITH MUS81.
RX PubMed=12721304; DOI=10.1074/jbc.m302882200;
RA Ciccia A., Constantinou A., West S.C.;
RT "Identification and characterization of the human mus81-eme1
RT endonuclease.";
RL J. Biol. Chem. 278:25172-25178(2003).
RN [5]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH MUS81, AND SUBCELLULAR
RP LOCATION.
RX PubMed=14617801; DOI=10.1091/mbc.e03-08-0580;
RA Blais V., Gao H., Elwell C.A., Boddy M.N., Gaillard P.-H.L., Russell P.,
RA McGowan C.H.;
RT "RNA interference inhibition of Mus81 reduces mitotic recombination in
RT human cells.";
RL Mol. Biol. Cell 15:552-562(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-85 AND SER-87, AND
RP IDENTIFICATION BY 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 [7]
RP FUNCTION, AND INTERACTION WITH MUS81.
RX PubMed=17289582; DOI=10.1016/j.molcel.2007.01.003;
RA Ciccia A., Ling C., Coulthard R., Yan Z., Xue Y., Meetei A.R.,
RA Laghmani el H., Joenje H., McDonald N., de Winter J.P., Wang W., West S.C.;
RT "Identification of FAAP24, a Fanconi anemia core complex protein that
RT interacts with FANCM.";
RL Mol. Cell 25:331-343(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-150, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-15, 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-85; SER-87; SER-111;
RP SER-117 AND THR-150, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-85 AND SER-87, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-87; SER-111 AND
RP THR-150, 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-103; LYS-136 AND LYS-141, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Interacts with MUS81 to form a DNA structure-specific
CC endonuclease with substrate preference for branched DNA structures with
CC a 5'-end at the branch nick. Typical substrates include 3'-flap
CC structures, replication forks and nicked Holliday junctions. May be
CC required in mitosis for the processing of stalled or collapsed
CC replication forks. {ECO:0000269|PubMed:12686547,
CC ECO:0000269|PubMed:12721304, ECO:0000269|PubMed:14617801,
CC ECO:0000269|PubMed:17289582}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: May self-associate. Interacts with MUS81.
CC {ECO:0000269|PubMed:12686547, ECO:0000269|PubMed:12721304,
CC ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:17289582}.
CC -!- INTERACTION:
CC Q96AY2; Q96NY9: MUS81; NbExp=9; IntAct=EBI-2370825, EBI-2370806;
CC Q96AY2; Q8IY92: SLX4; NbExp=4; IntAct=EBI-2370825, EBI-2370740;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14617801}.
CC Note=Recruited to regions of DNA damage in S-phase cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96AY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AY2-2; Sequence=VSP_017284;
CC -!- SIMILARITY: Belongs to the EME1/MMS4 family. {ECO:0000305}.
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DR EMBL; AK055926; BAB71047.1; -; mRNA.
DR EMBL; BC016470; AAH16470.1; -; mRNA.
DR CCDS; CCDS11565.1; -. [Q96AY2-1]
DR CCDS; CCDS54141.1; -. [Q96AY2-2]
DR RefSeq; NP_001159603.1; NM_001166131.1. [Q96AY2-2]
DR RefSeq; NP_689676.2; NM_152463.2. [Q96AY2-1]
DR PDB; 2ZIU; X-ray; 2.70 A; B=246-570.
DR PDB; 2ZIV; X-ray; 2.70 A; B=246-367, B=403-570.
DR PDB; 2ZIW; X-ray; 2.80 A; B=246-570.
DR PDB; 2ZIX; X-ray; 3.50 A; B=246-570.
DR PDB; 4P0P; X-ray; 2.80 A; B=178-570.
DR PDB; 4P0Q; X-ray; 2.85 A; B=178-570.
DR PDB; 4P0R; X-ray; 6.50 A; B/D=178-570.
DR PDB; 4P0S; X-ray; 6.00 A; B/D/F/H=178-570.
DR PDBsum; 2ZIU; -.
DR PDBsum; 2ZIV; -.
DR PDBsum; 2ZIW; -.
DR PDBsum; 2ZIX; -.
DR PDBsum; 4P0P; -.
DR PDBsum; 4P0Q; -.
DR PDBsum; 4P0R; -.
DR PDBsum; 4P0S; -.
DR AlphaFoldDB; Q96AY2; -.
DR SMR; Q96AY2; -.
DR BioGRID; 127026; 55.
DR ComplexPortal; CPX-511; Deoxyribonuclease complex MUS81-EME1.
DR DIP; DIP-48629N; -.
DR IntAct; Q96AY2; 42.
DR MINT; Q96AY2; -.
DR STRING; 9606.ENSP00000376952; -.
DR iPTMnet; Q96AY2; -.
DR PhosphoSitePlus; Q96AY2; -.
DR BioMuta; EME1; -.
DR DMDM; 88909612; -.
DR EPD; Q96AY2; -.
DR jPOST; Q96AY2; -.
DR MassIVE; Q96AY2; -.
DR MaxQB; Q96AY2; -.
DR PaxDb; Q96AY2; -.
DR PeptideAtlas; Q96AY2; -.
DR PRIDE; Q96AY2; -.
DR ProteomicsDB; 76018; -. [Q96AY2-1]
DR ProteomicsDB; 76019; -. [Q96AY2-2]
DR Antibodypedia; 4245; 231 antibodies from 31 providers.
DR DNASU; 146956; -.
DR Ensembl; ENST00000338165.9; ENSP00000339897.4; ENSG00000154920.15. [Q96AY2-1]
DR Ensembl; ENST00000393271.6; ENSP00000376952.2; ENSG00000154920.15. [Q96AY2-2]
DR Ensembl; ENST00000511648.6; ENSP00000421700.2; ENSG00000154920.15. [Q96AY2-2]
DR GeneID; 146956; -.
DR KEGG; hsa:146956; -.
DR MANE-Select; ENST00000338165.9; ENSP00000339897.4; NM_152463.4; NP_689676.2.
DR UCSC; uc002iqs.3; human. [Q96AY2-1]
DR CTD; 146956; -.
DR DisGeNET; 146956; -.
DR GeneCards; EME1; -.
DR HGNC; HGNC:24965; EME1.
DR HPA; ENSG00000154920; Tissue enhanced (bone marrow, epididymis, testis).
DR MIM; 610885; gene.
DR neXtProt; NX_Q96AY2; -.
DR OpenTargets; ENSG00000154920; -.
DR PharmGKB; PA134904115; -.
DR VEuPathDB; HostDB:ENSG00000154920; -.
DR eggNOG; ENOG502R8ER; Eukaryota.
DR GeneTree; ENSGT00530000063937; -.
DR HOGENOM; CLU_034099_2_0_1; -.
DR InParanoid; Q96AY2; -.
DR OMA; FCVESDW; -.
DR OrthoDB; 1595761at2759; -.
DR PhylomeDB; Q96AY2; -.
DR TreeFam; TF325310; -.
DR PathwayCommons; Q96AY2; -.
DR Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR SignaLink; Q96AY2; -.
DR BioGRID-ORCS; 146956; 28 hits in 1081 CRISPR screens.
DR EvolutionaryTrace; Q96AY2; -.
DR GeneWiki; EME1; -.
DR GenomeRNAi; 146956; -.
DR Pharos; Q96AY2; Tbio.
DR PRO; PR:Q96AY2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96AY2; protein.
DR Bgee; ENSG00000154920; Expressed in cauda epididymis and 177 other tissues.
DR ExpressionAtlas; Q96AY2; baseline and differential.
DR Genevisible; Q96AY2; HS.
DR GO; GO:1905347; C:endodeoxyribonuclease complex; IPI:ComplexPortal.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central.
DR GO; GO:0043596; C:nuclear replication fork; IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IDA:ComplexPortal.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0031297; P:replication fork processing; IDA:ComplexPortal.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0072429; P:response to intra-S DNA damage checkpoint signaling; IMP:MGI.
DR DisProt; DP01877; -.
DR Gene3D; 1.10.150.670; -; 1.
DR Gene3D; 3.40.1620.30; -; 1.
DR Gene3D; 4.10.800.30; -; 1.
DR IDEAL; IID00096; -.
DR InterPro; IPR042530; EME1/EME2_C.
DR InterPro; IPR043086; EME1_nucdom_sub1.
DR InterPro; IPR043087; Eme1_nucdom_sub2.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR033310; Mms4/EME1/EME2.
DR PANTHER; PTHR21077; PTHR21077; 1.
DR Pfam; PF02732; ERCC4; 1.
DR SMART; SM00891; ERCC4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA recombination;
KW DNA repair; Endonuclease; Hydrolase; Isopeptide bond; Magnesium;
KW Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..570
FT /note="Crossover junction endonuclease EME1"
FT /id="PRO_0000223630"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 370
FT /note="F -> FSLELLFFDFLPCT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017284"
FT VARIANT 5
FT /note="K -> N (in dbSNP:rs35248609)"
FT /id="VAR_055708"
FT VARIANT 49
FT /note="I -> V (in dbSNP:rs9896405)"
FT /id="VAR_025337"
FT VARIANT 63
FT /note="F -> L (in dbSNP:rs17714854)"
FT /id="VAR_055709"
FT VARIANT 69
FT /note="E -> D (in dbSNP:rs3760413)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_025338"
FT VARIANT 347
FT /note="V -> I (in dbSNP:rs7222520)"
FT /id="VAR_055710"
FT VARIANT 350
FT /note="I -> T (in dbSNP:rs12450550)"
FT /id="VAR_025339"
FT CONFLICT 214
FT /note="R -> Q (in Ref. 1; BAB71047)"
FT /evidence="ECO:0000305"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4P0P"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:4P0Q"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:4P0P"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 405..418
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 429..444
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 456..460
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:4P0P"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 478..486
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:2ZIX"
FT HELIX 494..503
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:4P0Q"
FT HELIX 507..515
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:2ZIU"
FT TURN 524..529
FT /evidence="ECO:0007829|PDB:2ZIU"
FT TURN 532..535
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 547..558
FT /evidence="ECO:0007829|PDB:2ZIU"
SQ SEQUENCE 570 AA; 63252 MW; BA08F5655761AF85 CRC64;
MALKKSSPSL DSGDSDSEEL PTFAFLKKEP SSTKRRQPER EEKIVVVDIS DCEASCPPAP
ELFSPPVPEI AETVTQTQPV RLLSSESEDE EEFIPLAQRL TCKFLTHKQL SPEDSSSPVK
SVLDHQNNEG ASCDWKKPFP KIPEVPLHDT PERSAADNKD LILDPCCQLP AYLSTCPGQS
SSLAVTKTNS DILPPQKKTK PSQKVQGRGS HGCRQQRQAR QKESTLRRQE RKNAALVTRM
KAQRPEECLK HIIVVLDPVL LQMEGGGQLL GALQTMECRC VIEAQAVPCS VTWRRRAGPS
EDREDWVEEP TVLVLLRAEA FVSMIDNGKQ GSLDSTMKGK ETLQGFVTDI TAKTAGKALS
LVIVDQEKCF SAQNPPRRGK QGANKQTKKQ QQRQPEASIG SMVSRVDAEE ALVDLQLHTE
AQAQIVQSWK ELADFTCAFT KAVAEAPFKK LRDETTFSFC LESDWAGGVK VDLAGRGLAL
VWRRQIQQLN RVSLEMASAV VNAYPSPQLL VQAYQQCFSD KERQNLLADI QVRRGEGVTS
TSRRIGPELS RRIYLQMTTL QPHLSLDSAD
