ID A0A094MHA0_ANTCR Unreviewed; 1125 AA.
AC A0A094MHA0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Apoptosis-stimulating of p53 protein 2 {ECO:0000313|EMBL:KFZ52293.1};
DE Flags: Fragment;
GN ORFNames=N321_05641 {ECO:0000313|EMBL:KFZ52293.1};
OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC Caprimulgidae; Antrostomus.
OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ52293.1, ECO:0000313|Proteomes:UP000053620};
RN [1] {ECO:0000313|EMBL:KFZ52293.1, ECO:0000313|Proteomes:UP000053620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ52293.1};
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; KL339972; KFZ52293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094MHA0; -.
DR Proteomes; UP000053620; 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 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; 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; 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:UP000053620};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
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..1125
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 87..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..716
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..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..859
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 563..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:KFZ52293.1"
FT NON_TER 1125
FT /evidence="ECO:0000313|EMBL:KFZ52293.1"
SQ SEQUENCE 1125 AA; 124883 MW; 12AA345F0C0AF814 CRC64;
LFQMFLTVYL SNNEQHFTEV PVTPETTCRD VVELCKEPGE SECHLAEVWC GSERPVADNE
RMLDILQRFG MQRSEVRFFL RHERSPCQEA GTGQRSQDPA LKRNGVKVPG DRRIENGVSA
PRMDMTLSEL QEMASRQQQQ IEAQQQMLAN KEQRLKFLKQ QDQRQQQQAA EQEKLKRLKE
IAENQEAKLK KVRALKGHVE QKRLSNGKLV EEIEQMNSLF QQKQRELVLA VSKVEELTRQ
LEMLKNGRID GYHDNQSAVA ELDRLYKELQ LRNKLNQEQN AKLQQQRECL NKRNSEVAVM
DKRVNELRER LWKKKAALQQ KENVPVSSNG NLPQPVASAP SRVAAVGPYI QSSTMPRIAS
RPELLVKPAF SDGTQPLQVP DGPLKTQTLP NMRAGSRSVV PSAKPSPSAT DWSSSNADNH
ISQGTALTSG KGIVTSEGQA EGETFLRDKE KKVRPFSMFD SVDQSAGLGT LRKNQSSEDL
LREAQGANKN VTKVPPPVPT KPKQINLPYF GQATHLQPSD TKLDGNPQKL PLAIATMGSK
QKTVAQQPSH PSQQIQQRIS VPLAGPSSSQ DQILPSSKQE SPPAAAVRPF TPQPSKETSL
PPFRKPPTVA ASSIYSMYTQ QQTPGKNFQQ AVQSALTRAQ TRGPHFPSVY GKPVMAGAGV
PNQLPQMENI YSNLQGKPGS PEPEMETTAS AHENHETERI PRPLSPTKLL PFLSNPYRNQ
SDADLEALRK KLSNAPRPLK KRSSITEPEG PNGPNIQKLL YQRTTLAAME TISAPSHPSK
QTSTAASPES PAEIPNPYLS AESEKETAAS MPEPSIAEEA ENTPADQSEA VLPSVALDTV
PEGASDGEEL AQQKMEEPSQ EASLPLEVYM 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 LGVSP
//
