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PEG3_PANTR
ID   PEG3_PANTR              Reviewed;        1588 AA.
AC   A2T7F2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Paternally-expressed gene 3 protein;
GN   Name=PEG3;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT   "Positive selection in transcription factor genes on the human lineage.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Induces apoptosis in cooperation with SIAH1A. Acts as a
CC       mediator between p53/TP53 and BAX in a neuronal death pathway that is
CC       activated by DNA damage. Acts synergistically with TRAF2 and inhibits
CC       TNF induced apoptosis through activation of NF-kappa-B (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with SIAH1A and SIAH2. Interacts with
CC       TRAF2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC       Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The SCAN domain enables PEG3 homo- or heterodimerization to
CC       control gene expression in a combinatorial fashion. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; DQ977436; ABM92107.1; -; Genomic_DNA.
DR   RefSeq; NP_001129091.1; NM_001135619.1.
DR   AlphaFoldDB; A2T7F2; -.
DR   STRING; 9598.ENSPTRP00000055316; -.
DR   PaxDb; A2T7F2; -.
DR   GeneID; 469030; -.
DR   KEGG; ptr:469030; -.
DR   CTD; 5178; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; A2T7F2; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   CDD; cd07936; SCAN; 1.
DR   Gene3D; 1.10.4020.10; -; 1.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 9.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   SUPFAM; SSF57667; SSF57667; 9.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE   3: Inferred from homology;
KW   Apoptosis; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1588
FT                   /note="Paternally-expressed gene 3 protein"
FT                   /id="PRO_0000285534"
FT   DOMAIN          46..128
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   REPEAT          1397..1403
FT                   /note="2-1"
FT   REPEAT          1404..1410
FT                   /note="2-2"
FT   REPEAT          1411..1417
FT                   /note="2-3"
FT   REPEAT          1418..1422
FT                   /note="1-1"
FT   REPEAT          1425..1429
FT                   /note="1-2"
FT   REPEAT          1432..1436
FT                   /note="1-3"
FT   REPEAT          1439..1443
FT                   /note="1-4"
FT   ZN_FING         454..476
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         507..529
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         565..587
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         627..649
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         969..991
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1107..1129
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1163..1185
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1225..1247
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1282..1304
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1332..1354
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1505..1527
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1564..1586
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          128..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          838..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1056..1104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1395..1495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1397..1417
FT                   /note="3 X 7 AA repeat of P-E-V-E-A-A-E"
FT   REGION          1418..1443
FT                   /note="4 X 5 AA repeat of P-X-G-E-A"
FT   COMPBIAS        139..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..878
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..904
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1056..1083
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1398..1421
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1447..1463
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1472..1495
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   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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