ID   PEG3_GORGO              Reviewed;        1589 AA.
AC   A1YFC1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Paternally-expressed gene 3 protein;
GN   Name=PEG3;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
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; DQ976560; ABM46839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1YFC1; -.
DR   STRING; 9593.ENSGGOP00000004993; -.
DR   PRIDE; A1YFC1; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; A1YFC1; -.
DR   Proteomes; UP000001519; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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..1589
FT                   /note="Paternally-expressed gene 3 protein"
FT                   /id="PRO_0000285532"
FT   DOMAIN          46..128
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   REPEAT          1398..1404
FT                   /note="2-1"
FT   REPEAT          1405..1411
FT                   /note="2-2"
FT   REPEAT          1412..1418
FT                   /note="2-3"
FT   REPEAT          1419..1423
FT                   /note="1-1"
FT   REPEAT          1426..1430
FT                   /note="1-2"
FT   REPEAT          1433..1437
FT                   /note="1-3"
FT   REPEAT          1440..1444
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         1506..1528
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1565..1587
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          1396..1496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1398..1418
FT                   /note="3 X 7 AA repeat of P-E-V-E-A-A-E"
FT   REGION          1419..1444
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        1399..1422
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1448..1464
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1473..1496
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1589 AA;  180878 MW;  6C8D0B2CCC125490 CRC64;
     MLPPKHLSAT KPKKSWAPNL YELDSDLTKE PDVIIGEGPT DSEFFHQRFR NLIYVEFVGP
     RKTLIKLRNL CLDWLQPETR 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 GCPRKKPFEC
     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 SLKRRQKTYN KEKLYDFTDG RDAFMQSSEL SEHQKIHSRK NLFEGRGYEK
     SVIHSGPFTE SQKSHTITRP LESDEDEKAF TISSNPYENQ KIPTKENVYE AKSYERSVIH
     SLASVEAQKS HSVAGPSKPK VMAESTIQSF DAINHQRVRA GGNTSEGREY NRSVIHSLVA
     SKPPRSHNGN ELVESNEKGE SSIYISDLND KRQKIPAREN PCEGGSKNRN YEDSVIQSVS
     RAKPQKSVPG EGSGEFKKDG EFSVPSSNVR EYQKARAKKK YIEHRSNETS VIHSLPFGEQ
     TFRPRGMLYE CQECGECFAH SSDLTEHQKI HDREKPSGSR NYEWSVIRSL APTDPQTSYA
     QEQYAKEQAR NKCKEFRQFF ATSEDLNTNQ KIYDQEKSHG EESQGENTDG EETHSEETHG
     QETIEDPVIQ SSDMEDPQKD DPDDKIYECE DCGLGFVDLT DLTDHQKVHS RKCLVDSREY
     THSVIHTHSI SEYQRDYTGE QLYECPKCGE SFIHSSFLFE HQRIHEQDQL YSMKGCDDGF
     IALLPMKPRR NRAAERNPAL AGSAIRCLLC GQGFIHSSAL NEHMRLHRED DLLEQSQMVE
     EAIIPGLALT EFQRSQTEER LFECAVCGES FVNPAELADH VTVHKNEPYE YGSSYTHTSF
     LTEPLKGAIP FYECKDCGKS FIHSTVLTKH KELHLEEEEE EDEAAAAAAA AAQEVEANVH
     VPQVVLRIQG SNVEAAEPEV EAAEPEVEAA EPEVEAAEPN GEAEGPDGEA AEPIGEAGQP
     NGEAEQPNGD ADEPDGAGIE DPEERAEEPE GKAEEPEGDA DEPDGVGIED PEEGEDQEIQ
     VEEPYYDCHE CTETFTSSTA FGEHLKTHAS MIIFEPADAF GECSGYIERA STSTGGANQA
     DEKYFKCDVC GQLFNDRLSL ARHQNTHTG