ID A0A091FX48_9AVES Unreviewed; 1091 AA.
AC A0A091FX48;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Apoptosis-stimulating of p53 protein 1 {ECO:0000313|EMBL:KFO74840.1};
GN ORFNames=N303_15466 {ECO:0000313|EMBL:KFO74840.1};
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:KFO74840.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO74840.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO74840.1};
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; KL447555; KFO74840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091FX48; -.
DR STRING; 55661.A0A091FX48; -.
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:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0045786; P:negative regulation of cell cycle; IEA:InterPro.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd17224; RA_ASPP1; 1.
DR CDD; cd11954; SH3_ASPP1; 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; IPR028319; ASPP1_RA.
DR InterPro; IPR048942; ASPP2-like_RA.
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:SF5; APOPTOSIS-STIMULATING OF P53 PROTEIN 1; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF21801; ASPP2-like_RA; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
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; 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 REPEAT 921..953
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 954..986
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1020..1082
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 80..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..190
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 215..242
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 266..310
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 87..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..868
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1091 AA; 121108 MW; 42C82E9D00AEAC9E CRC64;
MILTVFLSNN EQILTEVPIT PETTCRDVVE FCKEPGEGSC HLAEVWRGNE RPIPFDHMMY
DHLQKWGPRR EEVKFFLRHE ESPAESNEQS GRQAQNQRNG INIPVEKRTE NGVGNPRVEL
TLSELQDMAA RQQQQIENQQ QMLVAKEQRL RYLKQQERRQ QQSVSESEKL QKLKERVETQ
ETKLKKIRAM RGQVDYSKIM NGNLSTEIEH ISAMFQEKQQ ELQAAVLKVD QLTQQLEDLR
KGKLNGFQSY NGQMTGPAAV ELKKLYQELQ IRNRLNQEQN SKLQQQKELL NKRNMEVAMM
DKRINELRER LYKKKVEARQ KENIPLNRIN GSSSPQSSLS ASGRVAAVGP YIQVPSAGTY
AVPVDPVKPQ SLTIASSSTH GRSKSANDGN WPVLKQSSTP VVKPPQISNT DWKESSMDTA
LKQGTISSQP LPTSVLGSTD KLGLDLGKVP PTIPGVSKQL PQNYGTYPSP VPLGTGSTNS
LERRKDGSLP RPGTNITNRQ RPVPLPPPSN VHQPSSSQQI QQRISVPPSP TYQPSSSPLF
PGADGRPELP LTVAIRPFLA DKGSRPQSPR KGPQTVNSSS IYSMYLQQAT PPKNYQQAVY
NTLNKSVKAV YGKPVLQSGS TSPSPLPFLH GSLPAQTSSQ PQSQPQTEVS EKDQELENAP
PPSENSNVEN IPRPLSPTKL TPIVHSPLRY QSDADLEALR RKLANAPRPL KKRSSITEPE
GPSGPNIQKL LYQRFNTLAG GIESAPFYQP SNPQDFIGIL ADVDNGNTST NGNIEEPISV
QPTVPLPDEP PPSSDANDNE LPSPATEELI STETTNQTSE TTEDNNNNLA IVPSTEQSSS
PMPEVSSPVE EEAPLPPTLP PPLPPTKRTN LKKPNSERTG HGLRVKFNPL ALLLDASLEG
EFDLVQRIIY EVDDPSKPND EGITPLHNAV CAGHHHIVKF LLDFGVNVNA ADSDGWTPLH
CAASCNSVHL CKLLVESGAA IFASTISDIE TAADKCEEME EGYIQCSQFL YGVQEKLGVM
NKGVVYALWD YEAQNNDELS FHEGDAITIL RRKDDNETEW WWARLNDKEG YVPKNLLGLY
PRIKPRQRTL A
//
