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Paternally-expressed gene 3 protein

 PEG3_PANTR              Reviewed;        1588 AA.
A2T7F2;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 1.
23-MAY-2018, entry version 68.
RecName: Full=Paternally-expressed gene 3 protein;
Name=PEG3;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
"Positive selection in transcription factor genes on the human
lineage.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
-!- 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). {ECO:0000250}.
-!- 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}.
-!- DOMAIN: The SCAN domain enables PEG3 homo- or heterodimerization
to control gene expression in a combinatorial fashion.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
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EMBL; DQ977436; ABM92107.1; -; Genomic_DNA.
RefSeq; NP_001129091.1; NM_001135619.1.
UniGene; Ptr.6318; -.
ProteinModelPortal; A2T7F2; -.
SMR; A2T7F2; -.
STRING; 9598.ENSPTRP00000055316; -.
PaxDb; A2T7F2; -.
PRIDE; A2T7F2; -.
GeneID; 469030; -.
KEGG; ptr:469030; -.
CTD; 5178; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
HOGENOM; HOG000001564; -.
HOVERGEN; HBG079943; -.
InParanoid; A2T7F2; -.
KO; K09230; -.
Proteomes; UP000002277; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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.
3: Inferred from homology;
Apoptosis; Complete proteome; Cytoplasm; Metal-binding; Nucleus;
Reference proteome; Repeat; Zinc; Zinc-finger.
CHAIN 1 1588 Paternally-expressed gene 3 protein.
/FTId=PRO_0000285534.
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 454 476 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 507 529 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 565 587 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.
SEQUENCE 1588 AA; 180688 MW; 22528FE9ABDB28E2 CRC64;
MLPPKHLSAT KPKKSWAPNL YELDSDLTKE PDVIIGEGPT DSEFFHQRFR NLIYVEFVGP
RKTLIKLRNL CLDWLQPETH TKEEIIELLV LEQYLTIIPE KLKPWVRAKK PENCEKLVTL
LENYKEMYQP EDDNNSDVTS DDDMTRNRRE SSPPHSVHSF SGDRDWDRRG RSRDMEPRDR
WSHTRNPRSR MPQRDLSLPV VAKTSFEMDR DDDRDSRAYE SRSQDAESYQ NVVDLAEDRK
PHNTIQDNME NYRKLLSLGV QLAEDDGHSH MTQGHSSRSK RSAYPSTSRG LKTMPEAKKS
THRRGICEDE SSHGVIMEKF IKDVSRSSKS GRARESSDRS QRFPRMSDDN WKDISLNKRE
SVIQQRVYEG NAFRGGFRFN STLVSRKRVL ERKRRYHFDT DGKGSIHDQK ACPRKKPFEC
GSEMRKAMSM SSLSSLSSPS FTESQPIDFG AMPYVCDECG RSFSVISEFV EHQIMHTREN
LYEYGESFIH SVAVSEVQKS QVGGKRFECK DCGETFNKSA ALAEHRKIHA RGYLVECKNQ
ECEEAFMPSP TFSELQKIYG KDKFYECRVC KETFLHSSAL IEHQKIHFGD DKDNEREHER
ERERGETFRP SPALNEFQKM YGKEKMYECK VCGETFLHSS SLKEHQKIHT RGNPFENKGK
VCEETFIPGQ SLKKRQKTYN KEKLYDFTDG RDAFMQSSEL SEHQKIHSRK NLFEGRGYEK
SVIHSGPFTE SQKSHTITRP LESDEDEKAF TISSNPYENQ KIPTKENVYE AKSYERSVIH
SLASVEAQKS HSVAGPSKPK VMAESTIQSF DAINHQRVRA GGNTSEGREY SRSVIHSLVA
SKPPRSHNGN ELVESNEKGE SSIYISDLND KRQKIPAREN PCEGGSKNRN YEDSVIQSVS
RAKPQKSVPG EGSGEFKKDG EFSVPSSNVR EYQKARAKKK YIEHRSNETS VIHSLPFGEQ
TFRPRGMLYE CQECGECFAH SSDLTEHQKI HEREKPSGSR NYEWSVIRSL APTDPQTSYA
QEQYAKEQAW NKCKEFRQFF 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 FINPAELADH VTVHKNEPYE YGSSYTHTSF
LTEPLKGAIP FYECKDCGKS FIHSTVLTKH KELHLEEEEE DEAAAAAAAA AQEVEANVHV
PQVVLRIQGS NVEAAEPEVE AAEPEVEAAE PEVEAAEPNG EAEGPDGEAA EPIGEAGQPN
GEAEQPNGDA DEPDGAGIED PEERAEEPEG KAEEPEGDAD EPDGVGIEDP EEGEDQEIQV
EEPYYDCHEC TETFTSSTAF GEHLKTHASM IIFEPANAFG ECSGYIERAS TSTGGANQAD
EKYFKCDVCG QLFNDRLSLA RHQNTHTG


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