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Paternally-expressed gene 3 protein (Zinc finger and SCAN domain-containing protein 24)

 PEG3_HUMAN              Reviewed;        1588 AA.
Q9GZU2; A7E2B8; B4DIM4; C9JP50; P78418; Q5H9P9; Q7Z7H7; Q8TF75;
Q9GZY2;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
20-JUN-2018, entry version 146.
RecName: Full=Paternally-expressed gene 3 protein;
AltName: Full=Zinc finger and SCAN domain-containing protein 24;
Name=PEG3; Synonyms=KIAA0287, ZSCAN24;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT LEU-1576.
TISSUE=Fetal kidney;
PubMed=11677152; DOI=10.1016/S1071-5576(01)00129-0;
Van den Veyver I.B., Norman B., Tran C.Q., Bourjac J., Slim R.;
"The human homologue (PEG3) of the mouse paternally expressed gene 3
(Peg3) is maternally imprinted but not mutated in women with familial
recurrent hydatidiform molar pregnancies.";
J. Soc. Gynecol. Invest. 8:305-313(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Hippocampus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 4-1588 (ISOFORM 3), AND VARIANT
SER-947.
TISSUE=Liver;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 127-456, AND TISSUE SPECIFICITY.
PubMed=11331620; DOI=10.1093/hmg/10.10.1093;
Hiby S.E., Lough M., Keverne E.B., Surani M.A., Loke Y.W., King A.;
"Paternal monoallelic expression of PEG3 in the human placenta.";
Hum. Mol. Genet. 10:1093-1100(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 781-1588.
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 302-1588 (ISOFORM 1), FUNCTION, AND
TISSUE SPECIFICITY.
PubMed=11260267; DOI=10.1046/j.1365-2443.2001.00412.x;
Kohda T., Asai A., Kuroiwa Y., Kobayashi S., Aisaka K., Nagashima G.,
Yoshida M.C., Kondo Y., Kagiyama N., Kirino T., Kaneko-Ishino T.,
Ishino F.;
"Tumour suppressor activity of human imprinted gene PEG3 in a glioma
cell line.";
Genes Cells 6:237-247(2001).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 974-1588, AND TISSUE SPECIFICITY.
PubMed=9149948;
Kim J., Ashworth L., Branscomb E., Stubbs L.;
"The human homolog of a mouse-imprinted gene, Peg3, maps to a zinc
finger gene-rich region of human chromosome 19q13.4.";
Genome Res. 7:532-540(1997).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 974-1588.
Lamerdin J.E., McCready P.M., Kim J., Skowronski E., Viswanathan V.,
Burkhart-Schultz K., Gordon L., Dias J., Ramirez M., Stilwagen S.,
Phan H., Velasco N., Do L., Regala W., Terry A., Garnes J.,
Danganan L., Erler A., Christensen M., Georgescu A., Avila J., Liu S.,
Attix C., Andreise T., Trankheim M., Amico-Keller G., Coefield J.,
Duarte S., Lucas S., Bruce R., Thomas P., Quan G., Kronmiller B.,
Arellano A., Saunders C., Ow D., Nolan M., Trong S., Kobayashi A.,
Olsen A.S., Carrano A.V.;
"Sequence analysis of a 2 Mb region containing a zinc finger (ZNF)
gene cluster in 19q13.4.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[10]
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).
[11]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 40-130, SCAN DOMAIN, AND
SUBUNIT.
PubMed=23936039; DOI=10.1371/journal.pone.0069538;
Rimsa V., Eadsforth T.C., Hunter W.N.;
"Structure of the SCAN domain of human paternally expressed gene 3
protein.";
PLoS ONE 8:E69538-E69538(2013).
[12]
VARIANT [LARGE SCALE ANALYSIS] HIS-594.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Induces apoptosis in cooperation with SIAH1A. Acts as a
mediator between p53/TP53 and BAX in a neuronal death pathway that
is activated by DNA damage. Acts synergistically with TRAF2 and
inhibits TNF induced apoptosis through activation of NF-kappa-B
(By similarity). Possesses a tumor suppressing activity in glioma
cells. {ECO:0000250, ECO:0000269|PubMed:11260267}.
-!- SUBUNIT: Homodimer. Interacts with SIAH1A and SIAH2. Interacts
with TRAF2 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00187}. Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9GZU2-1; Sequence=Displayed;
Name=2;
IsoId=Q9GZU2-2; Sequence=VSP_020371;
Name=3;
IsoId=Q9GZU2-3; Sequence=VSP_020372, VSP_020373, VSP_020374;
Name=4;
IsoId=Q9GZU2-4; Sequence=VSP_020371, VSP_045527, VSP_045528;
-!- TISSUE SPECIFICITY: Brain, glial cells, astrocytes, embryo,
placenta, testis, ovary and uterus. In the placenta it is found in
the layer of villous cytotrophoblast cells while in the ovary it
is found in the cells of the ovarian stroma including the thecal
layers around the follicles. Expression is highly repressed in
glioma cell lines. {ECO:0000269|PubMed:11260267,
ECO:0000269|PubMed:11331620, ECO:0000269|PubMed:9149948}.
-!- DOMAIN: The SCAN domain enables PEG3 homo- or heterodimerization
to control gene expression in a combinatorial fashion.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB85588.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=CAI45975.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PEG3ID41690ch19q13.html";
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EMBL; AF208980; AAG42324.1; -; Genomic_DNA.
EMBL; AF208974; AAG42324.1; JOINED; Genomic_DNA.
EMBL; AF208975; AAG42324.1; JOINED; Genomic_DNA.
EMBL; AF208976; AAG42324.1; JOINED; Genomic_DNA.
EMBL; AF208977; AAG42324.1; JOINED; Genomic_DNA.
EMBL; AF208978; AAG42324.1; JOINED; Genomic_DNA.
EMBL; AF208979; AAG42324.1; JOINED; Genomic_DNA.
EMBL; AF208980; AAG42325.1; -; Genomic_DNA.
EMBL; AF208974; AAG42325.1; JOINED; Genomic_DNA.
EMBL; AF208975; AAG42325.1; JOINED; Genomic_DNA.
EMBL; AF208976; AAG42325.1; JOINED; Genomic_DNA.
EMBL; AF208977; AAG42325.1; JOINED; Genomic_DNA.
EMBL; AF208978; AAG42325.1; JOINED; Genomic_DNA.
EMBL; AF208979; AAG42325.1; JOINED; Genomic_DNA.
EMBL; AF208967; AAG35739.1; -; mRNA.
EMBL; AF208968; AAG35740.1; -; mRNA.
EMBL; AF208969; AAG35741.1; -; mRNA.
EMBL; AF208970; AAG35742.1; -; mRNA.
EMBL; AK295679; BAG58536.1; -; mRNA.
EMBL; CH471135; EAW72474.1; -; Genomic_DNA.
EMBL; BC052616; AAH52616.1; -; mRNA.
EMBL; BC150272; AAI50273.1; -; mRNA.
EMBL; AB003039; BAB85588.1; ALT_FRAME; mRNA.
EMBL; CR933682; CAI45975.1; ALT_INIT; mRNA.
EMBL; U90336; AAB50011.1; -; mRNA.
EMBL; AC006115; AAC83176.1; -; Genomic_DNA.
CCDS; CCDS12948.1; -. [Q9GZU2-1]
CCDS; CCDS58684.1; -. [Q9GZU2-4]
CCDS; CCDS58685.1; -. [Q9GZU2-2]
RefSeq; NP_001139656.1; NM_001146184.1. [Q9GZU2-1]
RefSeq; NP_001139657.1; NM_001146185.1. [Q9GZU2-2]
RefSeq; NP_001139658.1; NM_001146186.1. [Q9GZU2-1]
RefSeq; NP_001139659.1; NM_001146187.1. [Q9GZU2-4]
RefSeq; NP_006201.1; NM_006210.2. [Q9GZU2-1]
UniGene; Hs.731875; -.
PDB; 4BHX; X-ray; 1.95 A; A/B=40-130.
PDBsum; 4BHX; -.
ProteinModelPortal; Q9GZU2; -.
SMR; Q9GZU2; -.
BioGrid; 111204; 7.
DIP; DIP-38426N; -.
IntAct; Q9GZU2; 4.
STRING; 9606.ENSP00000326581; -.
iPTMnet; Q9GZU2; -.
PhosphoSitePlus; Q9GZU2; -.
BioMuta; PEG3; -.
DMDM; 74762724; -.
MaxQB; Q9GZU2; -.
PaxDb; Q9GZU2; -.
PeptideAtlas; Q9GZU2; -.
PRIDE; Q9GZU2; -.
ProteomicsDB; 80145; -.
ProteomicsDB; 80146; -. [Q9GZU2-2]
ProteomicsDB; 80147; -. [Q9GZU2-3]
Ensembl; ENST00000326441; ENSP00000326581; ENSG00000198300. [Q9GZU2-1]
Ensembl; ENST00000593695; ENSP00000472402; ENSG00000198300. [Q9GZU2-2]
Ensembl; ENST00000598410; ENSP00000473190; ENSG00000198300. [Q9GZU2-4]
Ensembl; ENST00000599534; ENSP00000472395; ENSG00000198300. [Q9GZU2-1]
Ensembl; ENST00000599577; ENSP00000469486; ENSG00000198300. [Q9GZU2-1]
GeneID; 5178; -.
KEGG; hsa:5178; -.
UCSC; uc002qnv.3; human. [Q9GZU2-1]
CTD; 5178; -.
DisGeNET; 5178; -.
EuPathDB; HostDB:ENSG00000198300.12; -.
GeneCards; PEG3; -.
HGNC; HGNC:8826; PEG3.
HPA; HPA026070; -.
MIM; 601483; gene.
neXtProt; NX_Q9GZU2; -.
OpenTargets; ENSG00000198300; -.
PharmGKB; PA33171; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00910000144259; -.
HOGENOM; HOG000001564; -.
HOVERGEN; HBG079943; -.
InParanoid; Q9GZU2; -.
KO; K09230; -.
OMA; AQTSYAE; -.
OrthoDB; EOG091G0V3Z; -.
PhylomeDB; Q9GZU2; -.
TreeFam; TF337075; -.
GeneWiki; PEG3; -.
GenomeRNAi; 5178; -.
PRO; PR:Q9GZU2; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000198300; -.
CleanEx; HS_PEG3; -.
ExpressionAtlas; Q9GZU2; baseline and differential.
Genevisible; Q9GZU2; HS.
GO; GO:0005776; C:autophagosome; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
CDD; cd07936; SCAN; 1.
Gene3D; 1.10.4020.10; -; 1.
InterPro; IPR003309; SCAN_dom.
InterPro; IPR038269; SCAN_sf.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF02023; SCAN; 1.
SMART; SM00431; SCAN; 1.
SMART; SM00355; ZnF_C2H2; 12.
SUPFAM; SSF57667; SSF57667; 12.
PROSITE; PS50804; SCAN_BOX; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Cytoplasm; Metal-binding; Nucleus; Polymorphism; Reference proteome;
Repeat; Zinc; Zinc-finger.
CHAIN 1 1588 Paternally-expressed gene 3 protein.
/FTId=PRO_0000249228.
DOMAIN 46 128 SCAN box. {ECO:0000255|PROSITE-
ProRule:PRU00187}.
REPEAT 1397 1403 2-1.
REPEAT 1404 1410 2-2.
REPEAT 1411 1417 2-3.
REPEAT 1418 1422 1-1.
REPEAT 1425 1429 1-2.
REPEAT 1432 1436 1-3.
REPEAT 1439 1443 1-4.
ZN_FING 452 474 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 505 527 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 563 585 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 627 649 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 969 991 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1107 1129 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1163 1185 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1225 1247 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1282 1304 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1332 1354 C2H2-type 10. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1505 1527 C2H2-type 11. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1564 1586 C2H2-type 12. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 1397 1417 3 X 7 AA repeat of P-E-V-E-A-A-E.
REGION 1418 1443 4 X 5 AA repeat of P-X-G-E-A.
COMPBIAS 1352 1512 Glu-rich.
VAR_SEQ 1 126 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:11677152,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_020371.
VAR_SEQ 161 161 S -> SG (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_045527.
VAR_SEQ 257 257 L -> LG (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_045528.
VAR_SEQ 258 287 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020372.
VAR_SEQ 547 550 SPTF -> NPCL (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020373.
VAR_SEQ 551 1588 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020374.
VARIANT 235 235 A -> T (in dbSNP:rs2191432).
/FTId=VAR_027397.
VARIANT 594 594 R -> H (in a colorectal cancer sample;
somatic mutation; dbSNP:rs754473044).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035562.
VARIANT 624 624 E -> G (in dbSNP:rs36016896).
/FTId=VAR_052725.
VARIANT 839 839 V -> L (in dbSNP:rs7251798).
/FTId=VAR_027398.
VARIANT 947 947 N -> S (in dbSNP:rs35851866).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_052726.
VARIANT 983 983 D -> G (in dbSNP:rs10412932).
/FTId=VAR_027399.
VARIANT 1456 1456 A -> V (in dbSNP:rs34831553).
/FTId=VAR_052727.
VARIANT 1576 1576 R -> H (in dbSNP:rs34051133).
/FTId=VAR_052728.
VARIANT 1576 1576 R -> L. {ECO:0000269|PubMed:11677152}.
/FTId=VAR_027400.
CONFLICT 310 311 SH -> PP (in Ref. 7; BAB85588).
{ECO:0000305}.
CONFLICT 439 439 F -> L (in Ref. 2; BAG58536).
{ECO:0000305}.
CONFLICT 677 677 K -> I (in Ref. 7; BAB85588).
{ECO:0000305}.
CONFLICT 690 690 G -> A (in Ref. 7; BAB85588).
{ECO:0000305}.
CONFLICT 750 750 F -> V (in Ref. 7; BAB85588).
{ECO:0000305}.
CONFLICT 755 755 N -> Y (in Ref. 7; BAB85588).
{ECO:0000305}.
CONFLICT 1117 1117 V -> M (in Ref. 7; BAB85588).
{ECO:0000305}.
CONFLICT 1145 1145 I -> V (in Ref. 7; BAB85588).
{ECO:0000305}.
CONFLICT 1587 1587 T -> M (in Ref. 7; BAB85588).
{ECO:0000305}.
HELIX 42 51 {ECO:0000244|PDB:4BHX}.
TURN 56 58 {ECO:0000244|PDB:4BHX}.
HELIX 60 75 {ECO:0000244|PDB:4BHX}.
HELIX 77 79 {ECO:0000244|PDB:4BHX}.
HELIX 82 97 {ECO:0000244|PDB:4BHX}.
HELIX 100 102 {ECO:0000244|PDB:4BHX}.
HELIX 103 109 {ECO:0000244|PDB:4BHX}.
HELIX 114 121 {ECO:0000244|PDB:4BHX}.
TURN 122 124 {ECO:0000244|PDB:4BHX}.
SEQUENCE 1588 AA; 180827 MW; 7E4F34A01F189F3E CRC64;
MLPPKHLSAT KPKKSWAPNL YELDSDLTKE PDVIIGEGPT DSEFFHQRFR NLIYVEFVGP
RKTLIKLRNL CLDWLQPETR TKEEIIELLV LEQYLTIIPE KLKPWVRAKK PENCEKLVTL
LENYKEMYQP EDDNNSDVTS DDDMTRNRRE SSPPHSVHSF SDRDWDRRGR SRDMEPRDRW
SHTRNPRSRM PPRDLSLPVV AKTSFEMDRE DDRDSRAYES RSQDAESYQN VVDLAEDRKP
HNTIQDNMEN YRKLLSLVQL AEDDGHSHMT QGHSSRSKRS AYPSTSRGLK TMPEAKKSTH
RRGICEDESS HGVIMEKFIK DVSRSSKSGR ARESSDRSQR FPRMSDDNWK DISLNKRESV
IQQRVYEGNA FRGGFRFNST LVSRKRVLER KRRYHFDTDG KGSIHDQKGC PRKKPFECGS
EMRKAMSVSS LSSLSSPSFT ESQPIDFGAM PYVCDECGRS FSVISEFVEH QIMHTRENLY
EYGESFIHSV AVSEVQKSQV GGKRFECKDC GETFNKSAAL AEHRKIHARG YLVECKNQEC
EEAFMPSPTF SELQKIYGKD KFYECRVCKE TFLHSSALIE HQKIHFGDDK DNEREHERER
ERERGETFRP SPALNEFQKM YGKEKMYECK VCGETFLHSS SLKEHQKIHT RGNPFENKGK
VCEETFIPGQ SLKRRQKTYN KEKLCDFTDG RDAFMQSSEL SEHQKIHSRK NLFEGRGYEK
SVIHSGPFTE SQKSHTITRP LESDEDEKAF TISSNPYENQ KIPTKENVYE AKSYERSVIH
SLASVEAQKS HSVAGPSKPK VMAESTIQSF DAINHQRVRA GGNTSEGREY SRSVIHSLVA
SKPPRSHNGN ELVESNEKGE SSIYISDLND KRQKIPAREN PCEGGSKNRN YEDSVIQSVF
RAKPQKSVPG EGSGEFKKDG EFSVPSSNVR EYQKARAKKK YIEHRSNETS VIHSLPFGEQ
TFRPRGMLYE CQECGECFAH SSDLTEHQKI HDREKPSGSR NYEWSVIRSL APTDPQTSYA
QEQYAKEQAR NKCKDFRQFF ATSEDLNTNQ KIYDQEKSHG EESQGENTDG EETHSEETHG
QETIEDPVIQ GSDMEDPQKD DPDDKIYECE DCGLGFVDLT DLTDHQKVHS RKCLVDSREY
THSVIHTHSI SEYQRDYTGE QLYECPKCGE SFIHSSFLFE HQRIHEQDQL YSMKGCDDGF
IALLPMKPRR NRAAERNPAL AGSAIRCLLC GQGFIHSSAL NEHMRLHRED DLLEQSQMAE
EAIIPGLALT EFQRSQTEER LFECAVCGES FVNPAELADH VTVHKNEPYE YGSSYTHTSF
LTEPLKGAIP FYECKDCGKS FIHSTVLTKH KELHLEEEEE DEAAAAAAAA AQEVEANVHV
PQVVLRIQGL NVEAAEPEVE AAEPEVEAAE PEVEAAEPNG EAEGPDGEAA EPIGEAGQPN
GEAEQPNGDA DEPDGAGIED PEERAEEPEG KAEEPEGDAD EPDGVGIEDP EEGEDQEIQV
EEPYYDCHEC TETFTSSTAF SEHLKTHASM IIFEPANAFG ECSGYIERAS TSTGGANQAD
EKYFKCDVCG QLFNDRLSLA RHQNTHTG


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