PEG3_PANPA
ID PEG3_PANPA Reviewed; 1588 AA.
AC A1YGK6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 02-JUN-2021, entry version 66.
DE RecName: Full=Paternally-expressed gene 3 protein;
GN Name=PEG3;
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597;
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; DQ977295; ABM54431.1; -; Genomic_DNA.
DR STRING; 9597.XP_008960468.1; -.
DR eggNOG; KOG1721; Eukaryota.
DR Proteomes; UP000240080; 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_0000285533"
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 263..297
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..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1501
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 1050..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..1500
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1588 AA; 180684 MW; 4FF7B6117370B2DB 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 HDREKPSGSR 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 VTVHKNEPYV YGSSYTHTSF
LTEPLKGAIP FYECKDCGKS FIHSTVLTKH KELHLEEEEE DEAAAAAAAA AQEVEANVHV
PQVVLRIQGS NVEAAEPEVE AXEPEVEAAE PEVEAAEPNG EAEGPDGEAA EPIGEAGQPN
GEAEQPNGDA DEPDGAGIED PEERAEEPEG KAEEPEGDAD EPDGVGIEDP EEGEDQEIQV
EEPYYDCHEC TETFTSSTAF GEHLKTHASM IIFEPANAFG ECSGYIERAS TSTGGANQAD
EKYFKCDVCG QLFNDRLSLA RHQNTHTG
