ID A0A091GJR4_9AVES Unreviewed; 1123 AA.
AC A0A091GJR4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Apoptosis-stimulating of p53 protein 2 {ECO:0000313|EMBL:KFO82640.1};
DE Flags: Fragment;
GN ORFNames=N303_13801 {ECO:0000313|EMBL:KFO82640.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO82640.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO82640.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO82640.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KL448315; KFO82640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GJR4; -.
DR STRING; 55661.A0A091GJR4; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0002039; F:p53 binding; IEA:InterPro.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd17225; RA_ASPP2; 1.
DR CDD; cd11953; SH3_ASPP2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR047163; ASPP1/2.
DR InterPro; IPR048942; ASPP2-like_RA.
DR InterPro; IPR047166; ASPP2_RA.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR24131; APOPTOSIS-STIMULATING OF P53 PROTEIN; 1.
DR PANTHER; PTHR24131:SF8; APOPTOSIS-STIMULATING OF P53 PROTEIN 2; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF21801; ASPP2-like_RA; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 2..85
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REPEAT 965..997
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 998..1030
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1064..1123
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 374..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 127..324
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 380..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO82640.1"
FT NON_TER 1123
FT /evidence="ECO:0000313|EMBL:KFO82640.1"
SQ SEQUENCE 1123 AA; 124767 MW; 92819F7819D6C8DD CRC64;
LFQMFLTVYL SNNEQHFTEV PVTPETTCRD VVELCKEPGE SECHLAEVCC GSERPIADNE
RMLDILQRFR MQRGEVRFFL RHERSPCREA GTGHRSQELA LKRNGVKVPG DRRIENGVSA
PRMDMTLAEL QEMASRQQQQ IEAQQQMLAN KEQRLKFLKQ QDQRQQQQAA EQEKLKRLKE
IAENQEAKLK KVRALKGHVE QKRLSNGKLV EEIEQMNSLF QQKQRELVLA VSKVEELTRQ
LEMLKNGRID GYHDNQSAVA ELDRLYKELQ LRNKLNQEQN AKLQQQRECL NKRNSEVAVM
DKRVNELRER LWKKKAALQQ KENVPVSSDG NLPQPVASAP SRVAAVGPYI QSSTMPRIAS
RPELLVKPAF SDGTQALQVP DGPLKTQTLP NMRAGSSSVI PGAKSSSSAA DWSGSNPDNQ
ISQVSALTSG KGVVTSEGQA EGETFLRDKE KKVRPFSMFD SVDQSAGLGT LRKNQSSEDL
LREAQTANKN ITKVPPPVPT KPKQINLPYF GQASHLQPSD SKLDGNLQKL PLAVLTMGNK
QKPVAQQPSH PSQQIQQRIS VPHAGPSSTQ DQILPSSKQE SPPAAAVRPF TPQPSKETSL
PPFRKPQTVA ASSIYSMYTQ QQTPGKNFQQ AVQSVLTRAQ TRGPHFPSVY GKPVMAGAGV
QNQLPQTENV YSNLQGKPGS PEPEMETAAS AHENHETERI PRPLSPTKLL PFLSNPYRNQ
SDADLEALRK KLSNAPRPLK KRSSITEPEG PNGPNIQKLL YQRTTLAAME TISAPSHPSK
QTTSAASPES PAEIPNPYLN AESEKETAAS IPELAIAEEA ENTPADQSEA VLPSVALDTV
PEGVLDGDEF TQPKMEEPSV EASLPLEAYM EEYPPYPPPP YPSGEPESLG EDSFNMRPPE
VTGQFSLPPG KRTNLRKTGS ERIGHGMRVK FNPLALLLDS SLEGEFDLVQ RIIYEVEDPS
MPNDEGITAL HNAVCAGHTE IVKFLVQFGV NVNAADSDGW TPLHCAASCN NVQVCKFLVE
SGAAVFAMTY SDMQTAADKC EEMEEGYTQC SQFLYGVQEK MGIMNKGVIY GLWDYEAQND
DELSMKEGDC MTILRREDED EIEWWWARLN DKEGYVPRNL LGV
//
