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Zinc finger CCCH-type with G patch domain-containing protein (G patch domain-containing protein 6) (Zinc finger CCCH domain-containing protein 9) (Zinc finger and G patch domain-containing protein)

 ZGPAT_HUMAN             Reviewed;         531 AA.
Q8N5A5; E1P5K1; Q4VXN9; Q5JWI9; Q5JWJ0; Q8NC55; Q8WUV4; Q96JI0;
Q96JU4; Q9H401;
11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
15-MAY-2007, sequence version 3.
25-OCT-2017, entry version 139.
RecName: Full=Zinc finger CCCH-type with G patch domain-containing protein;
AltName: Full=G patch domain-containing protein 6;
AltName: Full=Zinc finger CCCH domain-containing protein 9;
AltName: Full=Zinc finger and G patch domain-containing protein;
Name=ZGPAT; Synonyms=GPATC6, GPATCH6, KIAA1847, ZC3H9, ZC3HDC9, ZIP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ARG-61.
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 8:85-95(2001).
[2]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R.;
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-61.
TISSUE=Thyroid;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-61.
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
ARG-61.
TISSUE=Placenta, and Uterus;
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).
[7]
FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, TISSUE SPECIFICITY, AND
INTERACTION WITH CHD4.
PubMed=19644445; DOI=10.1038/emboj.2009.211;
Li R., Zhang H., Yu W., Chen Y., Gui B., Liang J., Wang Y., Sun L.,
Yang X., Zhang Y., Shi L., Li Y., Shang Y.;
"ZIP: a novel transcription repressor, represses EGFR oncogene and
suppresses breast carcinogenesis.";
EMBO J. 28:2763-2776(2009).
[8]
ALTERNATIVE SPLICING (ISOFORM 4), FUNCTION (ISOFORM 4), AND
SUBCELLULAR LOCATION (ISOFORM 4).
PubMed=20233718; DOI=10.1074/jbc.M110.107508;
Yu W., Li R., Gui B., Shang Y.;
"sZIP, an alternative splice variant of ZIP, antagonizes transcription
repression and growth inhibition by ZIP.";
J. Biol. Chem. 285:14301-14307(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
UBIQUITINATION.
PubMed=24116224; DOI=10.1371/journal.pone.0077320;
Maudet C., Sourisce A., Dragin L., Lahouassa H., Rain J.C.,
Bouaziz S., Ramirez B.C., Margottin-Goguet F.;
"HIV-1 Vpr Induces the Degradation of ZIP and sZIP, Adaptors of the
NuRD Chromatin Remodeling Complex, by Hijacking DCAF1/VprBP.";
PLoS ONE 8:E77320-E77320(2013).
[12]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 120-268 IN COMPLEX WITH ZINC
IONS.
Structural genomics consortium (SGC);
"Crystal structure of the zinc finger of ZGPAT.";
Submitted (FEB-2013) to the PDB data bank.
-!- FUNCTION: Transcription repressor that specifically binds the 5'-
GGAG[GA]A[GA]A-3' consensus sequence. Represses transcription by
recruiting the chromatin multiprotein complex NuRD to target
promoters. Negatively regulates expression of EGFR, a gene
involved in cell proliferation, survival and migration. Its
ability to repress genes of the EGFR pathway suggest it may act as
a tumor suppressor. Able to suppress breast carcinogenesis.
{ECO:0000269|PubMed:19644445}.
-!- FUNCTION: Isoform 4: Antagonizes the transcription repression by
isoform 1 by competing for the binding of the NuRD complex. Does
not bind DNA. {ECO:0000269|PubMed:19644445}.
-!- SUBUNIT: Interacts with CHD4/Mi-2; the interaction is direct.
{ECO:0000269|PubMed:19644445, ECO:0000269|Ref.12}.
-!- INTERACTION:
Q08117:AES; NbExp=3; IntAct=EBI-10183064, EBI-717810;
Q13155:AIMP2; NbExp=5; IntAct=EBI-10183064, EBI-745226;
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-10183064, EBI-10187270;
Q7L4P6:BEND5; NbExp=3; IntAct=EBI-3439227, EBI-724373;
Q9H2G9:BLZF1; NbExp=3; IntAct=EBI-3439227, EBI-2548012;
Q2TAC2:CCDC57; NbExp=3; IntAct=EBI-3439227, EBI-2808286;
O95273:CCNDBP1; NbExp=4; IntAct=EBI-3439227, EBI-748961;
Q8NHQ1:CEP70; NbExp=7; IntAct=EBI-10183064, EBI-739624;
O43143:DHX15; NbExp=7; IntAct=EBI-10183064, EBI-1237044;
Q8WWB3:DYDC1; NbExp=3; IntAct=EBI-3439227, EBI-740680;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-3439227, EBI-10175124;
Q08379:GOLGA2; NbExp=5; IntAct=EBI-10183064, EBI-618309;
Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-3439227, EBI-747204;
Q86T90:KIAA1328; NbExp=4; IntAct=EBI-10183064, EBI-3437878;
Q9BVG8:KIFC3; NbExp=4; IntAct=EBI-3439227, EBI-2125614;
P19012:KRT15; NbExp=3; IntAct=EBI-3439227, EBI-739566;
Q6A162:KRT40; NbExp=3; IntAct=EBI-10183064, EBI-10171697;
O95751:LDOC1; NbExp=3; IntAct=EBI-10183064, EBI-740738;
Q9BRK4:LZTS2; NbExp=5; IntAct=EBI-10183064, EBI-741037;
Q9UJV3-2:MID2; NbExp=5; IntAct=EBI-10183064, EBI-10172526;
Q8TD10:MIPOL1; NbExp=3; IntAct=EBI-3439227, EBI-2548751;
Q8IXK0:PHC2; NbExp=3; IntAct=EBI-10183064, EBI-713786;
Q9Y2D8:SSX2IP; NbExp=4; IntAct=EBI-3439227, EBI-2212028;
Q96MF2:STAC3; NbExp=3; IntAct=EBI-3439227, EBI-745680;
Q9UBB9:TFIP11; NbExp=5; IntAct=EBI-10183064, EBI-1105213;
Q13625-3:TP53BP2; NbExp=3; IntAct=EBI-10183064, EBI-10175039;
P14373:TRIM27; NbExp=5; IntAct=EBI-10183064, EBI-719493;
Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-3439227, EBI-2130429;
Q96BR9:ZBTB8A; NbExp=3; IntAct=EBI-3439227, EBI-742740;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19644445}.
-!- SUBCELLULAR LOCATION: Isoform 4: Nucleus
{ECO:0000269|PubMed:20233718}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8N5A5-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q8N5A5-2; Sequence=VSP_007754;
Name=3;
IsoId=Q8N5A5-3; Sequence=VSP_038121;
Note=No experimental confirmation available.;
Name=4; Synonyms=sZIP;
IsoId=Q8N5A5-4; Sequence=VSP_053599;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:19644445}.
-!- INDUCTION: Down-regulated in breast carcinomas.
-!- PTM: Ubiquitinated in case of infection by HIV-1, leading to its
degradation. Ubiquitination is mediated by the CUL4A-RBX1-DDB1-
DCAF1/VPRBP complex that is hijacked by HIV-1 via interaction
between HIV-1 Vpr and DCAF1/VPRBP. {ECO:0000269|PubMed:24116224}.
-!- SEQUENCE CAUTION:
Sequence=BAB47476.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAC11317.1; Type=Frameshift; Positions=290; Evidence={ECO:0000305};
Sequence=CAI95713.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AB058750; BAB47476.3; ALT_INIT; mRNA.
EMBL; AK027878; BAB55426.1; -; mRNA.
EMBL; AK074961; BAC11317.1; ALT_FRAME; mRNA.
EMBL; AL121845; CAC03670.1; -; Genomic_DNA.
EMBL; AL121845; CAI21879.1; -; Genomic_DNA.
EMBL; AL121845; CAI21880.1; -; Genomic_DNA.
EMBL; AL121845; CAI95713.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471077; EAW75223.1; -; Genomic_DNA.
EMBL; CH471077; EAW75226.1; -; Genomic_DNA.
EMBL; BC019338; AAH19338.1; -; mRNA.
EMBL; BC032612; AAH32612.1; -; mRNA.
CCDS; CCDS13534.1; -. [Q8N5A5-1]
CCDS; CCDS13535.1; -. [Q8N5A5-2]
CCDS; CCDS56203.1; -. [Q8N5A5-3]
RefSeq; NP_001076582.1; NM_001083113.1. [Q8N5A5-2]
RefSeq; NP_001182582.1; NM_001195653.1. [Q8N5A5-2]
RefSeq; NP_001182583.1; NM_001195654.1. [Q8N5A5-3]
RefSeq; NP_115916.3; NM_032527.4. [Q8N5A5-1]
RefSeq; NP_852150.2; NM_181485.2. [Q8N5A5-2]
UniGene; Hs.590868; -.
PDB; 4II1; X-ray; 2.65 A; A/B/C/D=120-268.
PDBsum; 4II1; -.
ProteinModelPortal; Q8N5A5; -.
SMR; Q8N5A5; -.
BioGrid; 124150; 61.
IntAct; Q8N5A5; 73.
MINT; MINT-2810381; -.
STRING; 9606.ENSP00000332013; -.
iPTMnet; Q8N5A5; -.
PhosphoSitePlus; Q8N5A5; -.
BioMuta; ZGPAT; -.
DMDM; 147744602; -.
EPD; Q8N5A5; -.
MaxQB; Q8N5A5; -.
PaxDb; Q8N5A5; -.
PeptideAtlas; Q8N5A5; -.
PRIDE; Q8N5A5; -.
DNASU; 84619; -.
Ensembl; ENST00000328969; ENSP00000332013; ENSG00000197114. [Q8N5A5-1]
Ensembl; ENST00000355969; ENSP00000348242; ENSG00000197114. [Q8N5A5-2]
Ensembl; ENST00000357119; ENSP00000349634; ENSG00000197114. [Q8N5A5-3]
Ensembl; ENST00000369967; ENSP00000358984; ENSG00000197114. [Q8N5A5-2]
Ensembl; ENST00000448100; ENSP00000391176; ENSG00000197114. [Q8N5A5-2]
GeneID; 84619; -.
KEGG; hsa:84619; -.
UCSC; uc002ygi.3; human. [Q8N5A5-1]
CTD; 84619; -.
DisGeNET; 84619; -.
EuPathDB; HostDB:ENSG00000197114.11; -.
GeneCards; ZGPAT; -.
H-InvDB; HIX0138076; -.
HGNC; HGNC:15948; ZGPAT.
HPA; HPA056705; -.
neXtProt; NX_Q8N5A5; -.
OpenTargets; ENSG00000197114; -.
PharmGKB; PA134881248; -.
eggNOG; KOG2185; Eukaryota.
eggNOG; ENOG410Z4ZI; LUCA.
GeneTree; ENSGT00390000000732; -.
HOVERGEN; HBG056371; -.
InParanoid; Q8N5A5; -.
OMA; RFKENCR; -.
OrthoDB; EOG091G0FZN; -.
PhylomeDB; Q8N5A5; -.
TreeFam; TF105970; -.
ChiTaRS; ZGPAT; human.
GeneWiki; ZGPAT; -.
GenomeRNAi; 84619; -.
PRO; PR:Q8N5A5; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000197114; -.
CleanEx; HS_ZGPAT; -.
ExpressionAtlas; Q8N5A5; baseline and differential.
Genevisible; Q8N5A5; HS.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 4.10.1000.10; -; 1.
InterPro; IPR000467; G_patch_dom.
InterPro; IPR000571; Znf_CCCH.
InterPro; IPR036855; Znf_CCCH_sf.
Pfam; PF01585; G-patch; 1.
SMART; SM00443; G_patch; 1.
SMART; SM00356; ZnF_C3H1; 1.
SUPFAM; SSF90229; SSF90229; 1.
PROSITE; PS50174; G_PATCH; 1.
PROSITE; PS50103; ZF_C3H1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 531 Zinc finger CCCH-type with G patch
domain-containing protein.
/FTId=PRO_0000213894.
DOMAIN 333 379 G-patch. {ECO:0000255|PROSITE-
ProRule:PRU00092}.
ZN_FING 175 201 C3H1-type. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
COMPBIAS 119 128 Poly-Glu.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDM1}.
VAR_SEQ 1 343 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_053599.
VAR_SEQ 282 310 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_038121.
VAR_SEQ 291 310 Missing (in isoform 2).
{ECO:0000303|PubMed:11347906,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007754.
VARIANT 61 61 S -> R (in dbSNP:rs1291212).
{ECO:0000269|PubMed:11347906,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5}.
/FTId=VAR_025539.
CONFLICT 184 184 L -> Q (in Ref. 3; BAB55426).
{ECO:0000305}.
CONFLICT 188 188 C -> R (in Ref. 3; BAC11317).
{ECO:0000305}.
CONFLICT 344 344 M -> V (in Ref. 3; BAB55426).
{ECO:0000305}.
CONFLICT 433 433 G -> R (in Ref. 6; AAH19338).
{ECO:0000305}.
CONFLICT 519 519 Q -> R (in Ref. 3; BAB55426).
{ECO:0000305}.
STRAND 133 138 {ECO:0000244|PDB:4II1}.
STRAND 146 157 {ECO:0000244|PDB:4II1}.
STRAND 163 171 {ECO:0000244|PDB:4II1}.
HELIX 175 177 {ECO:0000244|PDB:4II1}.
HELIX 183 185 {ECO:0000244|PDB:4II1}.
STRAND 195 197 {ECO:0000244|PDB:4II1}.
STRAND 200 203 {ECO:0000244|PDB:4II1}.
HELIX 204 206 {ECO:0000244|PDB:4II1}.
STRAND 223 227 {ECO:0000244|PDB:4II1}.
STRAND 233 244 {ECO:0000244|PDB:4II1}.
STRAND 246 252 {ECO:0000244|PDB:4II1}.
STRAND 258 260 {ECO:0000244|PDB:4II1}.
HELIX 262 264 {ECO:0000244|PDB:4II1}.
SEQUENCE 531 AA; 57359 MW; 36572156BABDA876 CRC64;
MDEESLESAL QTYRAQLQQV ELALGAGLDS SEQADLRQLQ GDLKELIELT EASLVSVRKS
SLLAALDEER PGRQEDAEYQ AFREAITEAV EAPAAARGSG SETVPKAEAG PESAAGGQEE
EEGEDEEELS GTKVSAPYYS SWGTLEYHNA MVVGTEEAED GSAGVRVLYL YPTHKSLKPC
PFFLEGKCRF KENCRFSHGQ VVSLDELRPF QDPDLSSLQA GSACLAKHQD GLWHAARITD
VDNGYYTVKF DSLLLREAVV EGDGILPPLR TEATESDSDS DGTGDSSYAR VVGSDAVDSA
QSSALCPSLA VVGSDAVDSG TCSSAFAGWE VHTRGIGSRL LTKMGYEFGK GLGRHAEGRV
EPIHAVVLPR GKSLDQCVET LQKQTRVGKA GTNKPPRCRG RGARPGGRPA PRNVFDFLNE
KLQGQAPGAL EAGAAPAGRR SKDMYHASKS AKRALSLRLF QTEEKIERTQ RDIRSIQEAL
ARNAGRHSVA SAQLQEKLAG AQRQLGQLRA QEAGLQQEQR KADTHKKMTE F


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