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Methyl-CpG-binding domain protein 4 (EC 3.2.2.-) (Methyl-CpG-binding endonuclease 1) (Methyl-CpG-binding protein MBD4) (Mismatch-specific DNA N-glycosylase)

 MBD4_HUMAN              Reviewed;         580 AA.
O95243; B4DZN2; D3DNC3; D3DNC4; E9PEE4; Q2MD36; Q7Z4T3; Q96F09;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
22-NOV-2017, entry version 148.
RecName: Full=Methyl-CpG-binding domain protein 4;
EC=3.2.2.-;
AltName: Full=Methyl-CpG-binding endonuclease 1;
AltName: Full=Methyl-CpG-binding protein MBD4;
AltName: Full=Mismatch-specific DNA N-glycosylase;
Name=MBD4; Synonyms=MED1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9774669; DOI=10.1128/MCB.18.11.6538;
Hendrich B., Bird A.;
"Identification and characterization of a family of mammalian methyl-
CpG binding proteins.";
Mol. Cell. Biol. 18:6538-6547(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10441743; DOI=10.1007/s003359901112;
Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.;
"Genomic structure and chromosomal mapping of the murine and human
mbd1, mbd2, mbd3, and mbd4 genes.";
Mamm. Genome 10:906-912(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
MLH1.
TISSUE=Fetal brain;
PubMed=10097147; DOI=10.1073/pnas.96.7.3969;
Bellacosa A., Cicchillitti L., Schepis F., Riccio A., Yeung A.T.,
Matsumoto Y., Golemis E.A., Genuardi M., Neri G.;
"MED1, a novel human methyl-CpG-binding endonuclease, interacts with
DNA mismatch repair protein MLH1.";
Proc. Natl. Acad. Sci. U.S.A. 96:3969-3974(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND ALTERNATIVE SPLICING.
PubMed=17143486;
Owen R.M., Baker R.D., Bader S., Dunlop M.G., Nicholl I.D.;
"The identification of a novel alternatively spliced form of the MBD4
DNA glycosylase.";
Oncol. Rep. 17:111-116(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Lung;
Guo J.H., Chen L., Yu L.;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-273; PRO-342;
LYS-346 AND HIS-568.
NIEHS SNPs program;
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
FUNCTION.
PubMed=10930409; DOI=10.1074/jbc.M004535200;
Petronzelli F., Riccio A., Markham G.D., Seeholzer S.H., Stoerker J.,
Genuardi M., Yeung A.T., Matsumoto Y., Bellacosa A.;
"Biphasic kinetics of the human DNA repair protein MED1 (MBD4), a
mismatch-specific DNA N-glycosylase.";
J. Biol. Chem. 275:32422-32429(2000).
[13]
INTERACTION WITH FADD.
PubMed=12702765; DOI=10.1073/pnas.0431215100;
Screaton R.A., Kiessling S., Sansom O.J., Millar C.B., Maddison K.,
Bird A., Clarke A.R., Frisch S.M.;
"Fas-associated death domain protein interacts with methyl-CpG binding
domain protein 4: a potential link between genome surveillance and
apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 100:5211-5216(2003).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318 AND SER-428, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Mismatch-specific DNA N-glycosylase involved in DNA
repair. Has thymine glycosylase activity and is specific for G:T
mismatches within methylated and unmethylated CpG sites. Can also
remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase
activity. Was first identified as methyl-CpG-binding protein.
{ECO:0000269|PubMed:10097147, ECO:0000269|PubMed:10930409}.
-!- SUBUNIT: Interacts with MLH1. {ECO:0000269|PubMed:10097147,
ECO:0000269|PubMed:12702765}.
-!- INTERACTION:
Q13158:FADD; NbExp=6; IntAct=EBI-348011, EBI-494804;
P40692:MLH1; NbExp=6; IntAct=EBI-6448717, EBI-744248;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=O95243-1; Sequence=Displayed;
Name=2;
IsoId=O95243-2; Sequence=VSP_010816;
Name=3;
IsoId=O95243-3; Sequence=VSP_010817, VSP_010818;
Note=No experimental confirmation available.;
Name=5;
IsoId=O95243-5; Sequence=VSP_054846;
Note=No experimental confirmation available.;
Name=4;
IsoId=O95243-6; Sequence=VSP_054845;
Note=Possesses uracil DNA glycosylase but not thymine DNA
glycosylase activity.;
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mbd4/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MBD4ID41312ch3q21.html";
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EMBL; AF072250; AAC68879.1; -; mRNA.
EMBL; AF120999; AAD50374.1; -; Genomic_DNA.
EMBL; AF120997; AAD50374.1; JOINED; Genomic_DNA.
EMBL; AF120998; AAD50374.1; JOINED; Genomic_DNA.
EMBL; AF114784; AAD22195.1; -; mRNA.
EMBL; AM180876; CAJ55826.1; -; mRNA.
EMBL; AF532602; AAP97338.1; -; mRNA.
EMBL; AK303013; BAG64144.1; -; mRNA.
EMBL; CR450305; CAG29301.1; -; mRNA.
EMBL; AF494057; AAM00008.1; -; Genomic_DNA.
EMBL; AL449212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79251.1; -; Genomic_DNA.
EMBL; CH471052; EAW79253.1; -; Genomic_DNA.
EMBL; CH471052; EAW79254.1; -; Genomic_DNA.
EMBL; CH471052; EAW79255.1; -; Genomic_DNA.
EMBL; BC011752; AAH11752.1; -; mRNA.
CCDS; CCDS3058.1; -. [O95243-1]
CCDS; CCDS63766.1; -. [O95243-5]
CCDS; CCDS63767.1; -. [O95243-3]
CCDS; CCDS63768.1; -. [O95243-2]
CCDS; CCDS63769.1; -. [O95243-6]
RefSeq; NP_001263199.1; NM_001276270.1. [O95243-2]
RefSeq; NP_001263200.1; NM_001276271.1. [O95243-5]
RefSeq; NP_001263201.1; NM_001276272.1. [O95243-3]
RefSeq; NP_001263202.1; NM_001276273.1. [O95243-6]
RefSeq; NP_003916.1; NM_003925.2. [O95243-1]
UniGene; Hs.35947; -.
PDB; 2MOE; NMR; -; A=80-148.
PDB; 3IHO; X-ray; 2.70 A; A=437-574.
PDB; 4DK9; X-ray; 2.76 A; A=426-580.
PDB; 4E9E; X-ray; 1.90 A; A=427-580.
PDB; 4E9F; X-ray; 1.79 A; A=427-580.
PDB; 4E9G; X-ray; 2.35 A; A=427-580.
PDB; 4E9H; X-ray; 3.00 A; A=427-580.
PDB; 4EA4; X-ray; 2.00 A; A=427-574.
PDB; 4EA5; X-ray; 2.14 A; A=427-580.
PDB; 4LG7; X-ray; 2.50 A; A=83-149.
PDB; 4OFA; X-ray; 1.55 A; A=426-580.
PDB; 4OFE; X-ray; 2.15 A; A=426-580.
PDB; 4OFH; X-ray; 2.22 A; A=426-580.
PDB; 5CHZ; X-ray; 1.83 A; A=426-580.
PDBsum; 2MOE; -.
PDBsum; 3IHO; -.
PDBsum; 4DK9; -.
PDBsum; 4E9E; -.
PDBsum; 4E9F; -.
PDBsum; 4E9G; -.
PDBsum; 4E9H; -.
PDBsum; 4EA4; -.
PDBsum; 4EA5; -.
PDBsum; 4LG7; -.
PDBsum; 4OFA; -.
PDBsum; 4OFE; -.
PDBsum; 4OFH; -.
PDBsum; 5CHZ; -.
ProteinModelPortal; O95243; -.
SMR; O95243; -.
BioGrid; 114444; 25.
IntAct; O95243; 16.
MINT; MINT-264766; -.
STRING; 9606.ENSP00000249910; -.
iPTMnet; O95243; -.
PhosphoSitePlus; O95243; -.
EPD; O95243; -.
MaxQB; O95243; -.
PaxDb; O95243; -.
PeptideAtlas; O95243; -.
PRIDE; O95243; -.
TopDownProteomics; O95243-3; -. [O95243-3]
Ensembl; ENST00000249910; ENSP00000249910; ENSG00000129071. [O95243-1]
Ensembl; ENST00000393278; ENSP00000376959; ENSG00000129071. [O95243-6]
Ensembl; ENST00000429544; ENSP00000394080; ENSG00000129071. [O95243-2]
Ensembl; ENST00000503197; ENSP00000424873; ENSG00000129071. [O95243-3]
Ensembl; ENST00000507208; ENSP00000422327; ENSG00000129071. [O95243-5]
GeneID; 8930; -.
KEGG; hsa:8930; -.
UCSC; uc003emh.3; human. [O95243-1]
CTD; 8930; -.
DisGeNET; 8930; -.
EuPathDB; HostDB:ENSG00000129071.9; -.
GeneCards; MBD4; -.
HGNC; HGNC:6919; MBD4.
HPA; HPA002031; -.
MIM; 603574; gene.
neXtProt; NX_O95243; -.
OpenTargets; ENSG00000129071; -.
PharmGKB; PA30663; -.
eggNOG; KOG4161; Eukaryota.
eggNOG; ENOG4111HPQ; LUCA.
GeneTree; ENSGT00530000063687; -.
HOGENOM; HOG000113489; -.
HOVERGEN; HBG052418; -.
InParanoid; O95243; -.
KO; K10801; -.
OMA; TADWRDV; -.
OrthoDB; EOG091G05HO; -.
PhylomeDB; O95243; -.
TreeFam; TF329176; -.
Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1.
EvolutionaryTrace; O95243; -.
GeneWiki; MBD4; -.
GenomeRNAi; 8930; -.
PRO; PR:O95243; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000129071; -.
CleanEx; HS_MBD4; -.
CleanEx; HS_MED1; -.
ExpressionAtlas; O95243; baseline and differential.
Genevisible; O95243; HS.
GO; GO:0000785; C:chromatin; IBA:GO_Central.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0019104; F:DNA N-glycosylase activity; TAS:Reactome.
GO; GO:0004520; F:endodeoxyribonuclease activity; TAS:ProtInc.
GO; GO:0008263; F:pyrimidine-specific mismatch base pair DNA N-glycosylase activity; IDA:MGI.
GO; GO:0003696; F:satellite DNA binding; TAS:ProtInc.
GO; GO:0045008; P:depyrimidination; TAS:Reactome.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IBA:GO_Central.
InterPro; IPR016177; DNA-bd_dom_sf.
InterPro; IPR011257; DNA_glycosylase.
InterPro; IPR017352; MBD4.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
PANTHER; PTHR15074:SF6; PTHR15074:SF6; 1.
Pfam; PF01429; MBD; 1.
PIRSF; PIRSF038005; Methyl_CpG_bd_MBD4; 1.
SMART; SM00391; MBD; 1.
SUPFAM; SSF48150; SSF48150; 1.
SUPFAM; SSF54171; SSF54171; 1.
PROSITE; PS50982; MBD; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; DNA damage;
DNA repair; DNA-binding; Hydrolase; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 580 Methyl-CpG-binding domain protein 4.
/FTId=PRO_0000096264.
DOMAIN 76 148 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
ACT_SITE 560 560 {ECO:0000250}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 428 428 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 83 401 RKSVPCGWERVVKQRLFGKTAGRFDVYFISPQGLKFRSKSS
LANYLHKNGETSLKPEDFDFTVLSKRGIKSRYKDCSMAALT
SHLQNQSNNSNWNLRTRSKCKKDVFMPPSSSSELQESRGLS
NFTSTHLLLKEDEGVDDVNFRKVRKPKGKVTILKGIPIKKT
KKGCRKSCSGFVQSDSKRESVCNKADAESEPVAQKSQLDRT
VCISDAGACGETLSVTSEENSLVKKKERSLSSGSNFCSEQK
TSGIINKFCSAKDSEHNEKYEDTFLESEEIGTKVEVVERKE
HLHTDILKRGSEMDNNCSPTRKDFTGEKIFQE -> Q (in
isoform 4).
{ECO:0000303|PubMed:17143486}.
/FTId=VSP_054845.
VAR_SEQ 395 400 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.7}.
/FTId=VSP_010816.
VAR_SEQ 539 540 KY -> AP (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_010817.
VAR_SEQ 541 580 Missing (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_010818.
VAR_SEQ 557 580 HPEDHKLNKYHDWLWENHEKLSLS -> RLTPIHNSAHLVS
EAK (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054846.
VARIANT 61 61 C -> R (in dbSNP:rs2307296).
/FTId=VAR_029306.
VARIANT 273 273 A -> S (in dbSNP:rs10342).
{ECO:0000269|Ref.8}.
/FTId=VAR_019357.
VARIANT 273 273 A -> T (in dbSNP:rs10342).
/FTId=VAR_019514.
VARIANT 342 342 S -> P (in dbSNP:rs2307289).
{ECO:0000269|Ref.8}.
/FTId=VAR_019358.
VARIANT 346 346 E -> K (in dbSNP:rs140693).
{ECO:0000269|Ref.8}.
/FTId=VAR_019359.
VARIANT 358 358 I -> T (in dbSNP:rs2307298).
/FTId=VAR_019515.
VARIANT 568 568 D -> H (in dbSNP:rs2307293).
{ECO:0000269|Ref.8}.
/FTId=VAR_019360.
CONFLICT 51 51 E -> G (in Ref. 6; BAG64144).
{ECO:0000305}.
CONFLICT 359 359 G -> R (in Ref. 6; BAG64144).
{ECO:0000305}.
CONFLICT 387 387 S -> L (in Ref. 6; BAG64144).
{ECO:0000305}.
STRAND 91 96 {ECO:0000244|PDB:4LG7}.
TURN 101 104 {ECO:0000244|PDB:4LG7}.
STRAND 106 111 {ECO:0000244|PDB:4LG7}.
HELIX 121 130 {ECO:0000244|PDB:4LG7}.
HELIX 138 140 {ECO:0000244|PDB:4LG7}.
HELIX 449 452 {ECO:0000244|PDB:4OFA}.
HELIX 456 465 {ECO:0000244|PDB:4OFA}.
TURN 466 468 {ECO:0000244|PDB:4OFA}.
HELIX 471 484 {ECO:0000244|PDB:4OFA}.
HELIX 488 491 {ECO:0000244|PDB:4OFA}.
HELIX 496 503 {ECO:0000244|PDB:4OFA}.
HELIX 504 506 {ECO:0000244|PDB:4OFA}.
HELIX 509 525 {ECO:0000244|PDB:4OFA}.
HELIX 531 533 {ECO:0000244|PDB:4OFA}.
HELIX 539 548 {ECO:0000244|PDB:4OFA}.
HELIX 553 555 {ECO:0000244|PDB:4OFA}.
HELIX 561 577 {ECO:0000244|PDB:4OFA}.
SEQUENCE 580 AA; 66051 MW; BF16FB21A34B8E5F CRC64;
MGTTGLESLS LGDRGAAPTV TSSERLVPDP PNDLRKEDVA MELERVGEDE EQMMIKRSSE
CNPLLQEPIA SAQFGATAGT ECRKSVPCGW ERVVKQRLFG KTAGRFDVYF ISPQGLKFRS
KSSLANYLHK NGETSLKPED FDFTVLSKRG IKSRYKDCSM AALTSHLQNQ SNNSNWNLRT
RSKCKKDVFM PPSSSSELQE SRGLSNFTST HLLLKEDEGV DDVNFRKVRK PKGKVTILKG
IPIKKTKKGC RKSCSGFVQS DSKRESVCNK ADAESEPVAQ KSQLDRTVCI SDAGACGETL
SVTSEENSLV KKKERSLSSG SNFCSEQKTS GIINKFCSAK DSEHNEKYED TFLESEEIGT
KVEVVERKEH LHTDILKRGS EMDNNCSPTR KDFTGEKIFQ EDTIPRTQIE RRKTSLYFSS
KYNKEALSPP RRKAFKKWTP PRSPFNLVQE TLFHDPWKLL IATIFLNRTS GKMAIPVLWK
FLEKYPSAEV ARTADWRDVS ELLKPLGLYD LRAKTIVKFS DEYLTKQWKY PIELHGIGKY
GNDSYRIFCV NEWKQVHPED HKLNKYHDWL WENHEKLSLS


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