PEG3_BOVIN
ID PEG3_BOVIN Reviewed; 2387 AA.
AC Q6H236;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Paternally-expressed gene 3 protein;
GN Name=PEG3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=15203203; DOI=10.1016/j.ygeno.2004.02.007;
RA Kim J., Bergmann A., Lucas S., Stone R., Stubbs L.;
RT "Lineage-specific imprinting and evolution of the zinc-finger gene ZIM2.";
RL Genomics 84:47-58(2004).
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. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6H236-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6H236-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the cerebellum and at
CC moderate levels in the testis and ovary. {ECO:0000269|PubMed:15203203}.
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; AY427787; AAR97556.1; -; mRNA.
DR AlphaFoldDB; Q6H236; -.
DR STRING; 9913.ENSBTAP00000031689; -.
DR PaxDb; Q6H236; -.
DR PRIDE; Q6H236; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q6H236; -.
DR Proteomes; UP000009136; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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; 5.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 2: Evidence at transcript level;
KW Alternative splicing; Apoptosis; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..2387
FT /note="Paternally-expressed gene 3 protein"
FT /id="PRO_0000249227"
FT DOMAIN 44..126
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT REPEAT 965..973
FT /note="1-1"
FT REPEAT 974..982
FT /note="1-2"
FT REPEAT 983..991
FT /note="3-1"
FT REPEAT 1001..1009
FT /note="2-1"
FT REPEAT 1010..1018
FT /note="4-1"
FT REPEAT 1028..1036
FT /note="3-2"
FT REPEAT 1046..1054
FT /note="2-2"
FT REPEAT 1055..1063
FT /note="4-2"
FT REPEAT 1073..1081
FT /note="3-3"
FT REPEAT 1091..1099
FT /note="1-3"
FT REPEAT 1109..1117
FT /note="2-3"
FT REPEAT 1118..1126
FT /note="4-3"
FT REPEAT 1136..1144
FT /note="1-4"
FT REPEAT 1145..1153
FT /note="2-4"
FT REPEAT 1154..1162
FT /note="2-5"
FT REPEAT 1163..1171
FT /note="1-5"
FT REPEAT 1172..1180
FT /note="1-6"
FT REPEAT 1190..1198
FT /note="2-6"
FT REPEAT 1199..1207
FT /note="1-7"
FT REPEAT 1217..1225
FT /note="4-4"
FT REPEAT 1235..1243
FT /note="1-8"
FT REPEAT 1253..1261
FT /note="2-7"
FT REPEAT 1280..1288
FT /note="2-8"
FT REPEAT 1289..1297
FT /note="1-9"
FT REPEAT 1298..1306
FT /note="2-9"
FT REPEAT 1307..1315
FT /note="2-10"
FT REPEAT 1316..1324
FT /note="1-10"
FT REPEAT 1325..1333
FT /note="2-11"
FT REPEAT 1334..1342
FT /note="1-11"
FT REPEAT 1343..1351
FT /note="2-12"
FT REPEAT 1352..1360
FT /note="1-12"
FT REPEAT 1361..1369
FT /note="1-13"
FT REPEAT 1370..1378
FT /note="1-14"
FT REPEAT 1379..1387
FT /note="2-13"
FT REPEAT 1388..1396
FT /note="1-15"
FT REPEAT 1397..1405
FT /note="1-16"
FT REPEAT 1406..1414
FT /note="1-17"
FT REPEAT 1415..1423
FT /note="1-18"
FT REPEAT 1424..1432
FT /note="1-19"
FT REPEAT 1433..1441
FT /note="1-20"
FT REPEAT 1442..1450
FT /note="1-21"
FT REPEAT 1451..1459
FT /note="1-22"
FT REPEAT 1460..1468
FT /note="1-23"
FT REPEAT 1469..1477
FT /note="1-24"
FT REPEAT 1478..1486
FT /note="1-25"
FT REPEAT 1496..1504
FT /note="1-26"
FT REPEAT 1505..1513
FT /note="1-27"
FT REPEAT 1514..1522
FT /note="1-28"
FT REPEAT 1523..1531
FT /note="1-29"
FT REPEAT 1532..1540
FT /note="1-30"
FT REPEAT 1541..1549
FT /note="1-31"
FT REPEAT 1550..1558
FT /note="1-32"
FT REPEAT 1559..1567
FT /note="1-33"
FT REPEAT 1568..1576
FT /note="1-34"
FT REPEAT 1577..1585
FT /note="1-35"
FT REPEAT 1586..1594
FT /note="1-36"
FT REPEAT 1595..1603
FT /note="1-37"
FT ZN_FING 451..473
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 555..577
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 610..632
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 668..690
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 884..906
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1859..1881
FT /note="C2H2-type 6; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1924..1946
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1980..2002
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2040..2062
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2097..2119
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2148..2170
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2312..2334
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2363..2385
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 127..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1603
FT /note="37 X 9 AA repeat of P-A-Q-T-X-Y-X-X-E"
FT REGION 1900..1921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2059..2102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2204..2322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1904..1921
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2211..2234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2260..2309
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2387 AA; 264828 MW; 349F29E48C095958 CRC64;
MLPPKSLSAT KPKKWAPNLY ELDSDLSEPD AVPGEGATDS EFFHQRFRNF LYVEFIGPRK
TLLKLRNLCL DWLQPEIRTK EEIIEVLVLE QYLSILPERI KPWVYARKPE TCEKLVALLE
DYEAMYEPED DNSSDTHSEG GMSRRAAESP PPRPALPCCS ERERRRGRSR DMESRDRWPS
VRSPRSRFHQ RDLALPLAER AKEREHRRRD SLLDLDARSE EAVLYQDMVA LTEDRKPQNP
IQDNMENYRK LLSLGVQLAE DDGHSHMTQG HSARSKRSAY PSTSRGLKTA PETKKSAHRR
GICEAESSHG VIMEKFIKDV ARSSRSGRAR ESSERPHRLS RRAGGDWKEA SFSRREAGAS
ERGPEGGAFG GGGFSCGSDL VSKKRALERK RRYHFDAEGQ GPVHDPRGGA RKRPFECGGE
ARRAAKAAGA SSLSAPPAAP SQPLDFGAMP YVCDECGRSF AVISEFVEHQ IVHTRESLYE
YGESFIHSAA VSEAQSRPEG ARRSEGAQAA GLAEHRGGQA QEHLRGSGDE EQDEPFLPSP
TFSELQKMYG KDKFYECKVC KETFLHSSAL IEHQKIHSHE DREKERSTGA VRRTPMLGEL
QRACGKEKRY ECKVCGETFH HSAALREHQK THGRGSPSEG RARAFEETFI PGQSLKRRQK
TYSKEKLYDF REGGDAFGRS SDFMEHQKIH SRKSYFDSRG YEKPLLHSMS MPGSQKSHTI
TRPPEDEDEE KAFTASSSPE DGQEARGYER SAYERAILHS LAAFRPPRGL REDGEPSTYL
SGLRDPPQKT PAWESPYAGG RHSFFRSSVF YRASRPAPLD HLAGEGPSGW QRDGEASGPS
SDGRQHQKAR AKKKNIERKN YDASMMHSLH FGESQTFRPR ERFYECLECG EFFVRSSELA
EHQKIHNRKK LSGSKNYLRS VLRSLSSTDP QTSYQGQSVQ MSYPQEAAQT SYAELAAQTS
YAEEPAQTSY AVEPAQTSYA EEPAQTSYTE APAEASYTEE PAQTSCIEEP AQTSYTNPAA
ETSYAEEPAQ TSYTEAPAEA SYTEEPAQTS CIEEPAQTSY TNPAAETSYT EEPAQTSYTE
APAEASGIEE PAQTNYTEES AEVSYTEEPS QTSCIEEPAQ TSYTDPAAET SYTEEPAQTS
YTQEPAQTSC TEEPAQTSCT EEPAQTSYTQ EPAQTSYTKE PAEASYTEEP AQTSCIEEPA
QTNYTKESAK ASYTEEPAQT SYTDPAAETS YTEEPAQTNY TVESAEASYT EEPSQTSCIE
EPAQTSYTDS AADTSCTEEP AQTSCTEEPA QTSYTQEPAQ TSCTEEPAQT SCTEEPAQTS
YTQEPAQTSC TEEPAQTSYT QEPAQTSCTE EPAQTSYTEE PAQTSYTEEP AQTSYTQEPA
QTSCTEEPAQ TSYTEEPAQT SYTEEPAQTS YTQEPAQTSY TEEPAQTSYT EEPAQTSYAQ
EPAQTSYAEE PAQTSYAEEP AQTSYAEEPA QTSYTQEPAQ TNYTEEPAEA SYTEEPAQTS
YAEEPAQTSY PEEPAQTSYA EEPAQTSYAE EPAQTSYPEE PAQTSYTEEP AQTSYAKEPA
QTSYPEEPAQ TSYAEEPAQT SYAEEPAQTS YAEEPAQTSY SEEPAQTRYT GNELRSDMRK
NQLRPDMPRN QLRPVMPRNQ LRPDMPRNQP RPVILRNQLR PDMPRNQPRP VILRNQLRPD
MLGNQLRPDM PGNQLRPDML REPPAETSYA ELVAQISYAE LVTPTSYAEL AAETGYFEPP
AQTSYTEPAE TNYADPAAQV SFDEPPAEAS YADLAAEISY AELAAETSYA DLAAQISYDE
PPAETSYAEL AAQISYSEPA DQTSYAELAA QTSYSEPLAQ TSYAELTSET SYCEQPVLNE
CKECGECFAT VEDLGRHQKI YAREKFHDGK LFGEPVMQDL GLDGSPEEEL EEQEEPEEPE
DSIYGCKDCG LGFADRADLR DHQKVHGREY LVDSREYTHP AVHMPPVSEY QKDCLGEQLY
ECPACGESFV HSSFLFEHQK VHEQDQFYGH RRYEPFMQPL IVSPRRPQAP QKSAPAGVGP
QCQVCGQDFI HASVLSEHAR GHAGEGLPDQ GQGGAGAAGP GPAPTEPQQD PGEEQRYECE
TCGESFPSQA DLQEHMRVHE KGEPYDYGAA FVHTSFLTEP PKRDWPFYEC KDCGKSFIHS
TILTKHQKLH LQEEGAAAAA AATAQEAEAN VLVPREVLRI QGSNVEAAEP EVEAAEPEVE
AAEPEVEAAE PLGEAEGPEW EAAEPSGEAE QPHAEAEQPD MDADEPDGAG IEDPEERAEE
PEGDDDEPDG AGIEDPEEEG EEQEIQVEEP YYDCGECGET FPSGAAYAEH LTAHASLVIL
EPAGLYGEGA GGPEGGRPDD ELFKCDVCGQ LFSDRLSLAR HQNTHTG
