ID Q53HN4_HUMAN Unreviewed; 331 AA.
AC Q53HN4;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 22-FEB-2023, entry version 79.
DE SubName: Full=DNAation factor, 45kDa, alpha polypeptide isoform 1 variant {ECO:0000313|EMBL:BAD96266.1};
DE Flags: Fragment;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD96266.1};
RN [1] {ECO:0000313|EMBL:BAD96266.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Coronary artery {ECO:0000313|EMBL:BAD96266.1};
RX PubMed=8125298; DOI=10.1016/0378-1119(94)90802-8;
RA Maruyama K., Sugano S.;
RT "Oligo-capping: a simple method to replace the cap structure of eukaryotic
RT mRNAs with oligoribonucleotides.";
RL Gene 138:171-174(1994).
RN [2] {ECO:0000313|EMBL:BAD96266.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Coronary artery {ECO:0000313|EMBL:BAD96266.1};
RX PubMed=9373149; DOI=10.1016/S0378-1119(97)00411-3;
RA Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.;
RT "Construction and characterization of a full length-enriched and a 5'-end-
RT enriched cDNA library.";
RL Gene 200:149-156(1997).
RN [3] {ECO:0000313|EMBL:BAD96266.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Coronary artery {ECO:0000313|EMBL:BAD96266.1};
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AK222546; BAD96266.1; -; mRNA.
DR AlphaFoldDB; Q53HN4; -.
DR PeptideAtlas; Q53HN4; -.
DR GO; GO:0060703; F:deoxyribonuclease inhibitor activity; IEA:InterPro.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; IEA:InterPro.
DR Gene3D; 3.10.20.10; -; 1.
DR Gene3D; 1.10.1490.10; C-terminal domain of DFF45/ICAD (DFF-C domain); 2.
DR InterPro; IPR003508; CIDE-N_dom.
DR InterPro; IPR027296; DFF-C.
DR InterPro; IPR017299; DFF45.
DR InterPro; IPR015121; DNA_fragmentation_mid_dom.
DR PANTHER; PTHR12306; CELL DEATH ACTIVATOR CIDE; 1.
DR PANTHER; PTHR12306:SF16; CIDE-N DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02017; CIDE-N; 1.
DR Pfam; PF09033; DFF-C; 1.
DR PIRSF; PIRSF037865; DFF_alpha; 1.
DR SMART; SM00266; CAD; 1.
DR SUPFAM; SSF81783; C-terminal domain of DFF45/ICAD (DFF-C domain); 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR PROSITE; PS51135; CIDE_N; 1.
PE 2: Evidence at transcript level;
KW Apoptosis {ECO:0000256|PROSITE-ProRule:PRU00447};
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 17..96
FT /note="CIDE-N"
FT /evidence="ECO:0000259|PROSITE:PS51135"
FT REGION 305..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..202
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAD96266.1"
SQ SEQUENCE 331 AA; 36594 MW; 31E2842C7D9A548E CRC64;
MEVTGDAGVP ESGEIRTLKP CLLRRNYSRE QHGVAASCLE DLRSKACDIL AIDKSLTPVT
LVLAEDGTIV DDDDYFLCLP SNTKFVALAS NEKWAYNNSD EGTAWISQES FDVDETDSGA
GLKWKNVARQ LKEDLSSIIL LSEEDLQMLV DAPCSDLAQE LRQSCATVQR LQHTLQQVLD
QREEVRQSKQ LLQLYLQALE KEGSLLSKQE ESKAAFGEEV DAVDTGISRE TSSDVALASH
ILTALREKQA PELSLSSQDL ELVTKEDPKA LAVALNWDIK KTETVQEACE RELALRLQQT
QSLHSLRSIS ASKASPPGDL QNPKRARQDP T
//
