ID G1NSQ7_MYOLU Unreviewed; 331 AA.
AC G1NSQ7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=DNA fragmentation factor subunit alpha {ECO:0000313|Ensembl:ENSMLUP00000000176.2};
GN Name=DFFA {ECO:0000313|Ensembl:ENSMLUP00000000176.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000000176.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000000176.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000000176.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAPE02050832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006104981.1; XM_006104919.2.
DR AlphaFoldDB; G1NSQ7; -.
DR STRING; 59463.ENSMLUP00000000176; -.
DR Ensembl; ENSMLUT00000000192.2; ENSMLUP00000000176.2; ENSMLUG00000000194.2.
DR GeneID; 102428443; -.
DR KEGG; mlf:102428443; -.
DR CTD; 1676; -.
DR eggNOG; ENOG502RQ19; Eukaryota.
DR GeneTree; ENSGT00390000018596; -.
DR HOGENOM; CLU_086234_0_0_1; -.
DR InParanoid; G1NSQ7; -.
DR OMA; NWDIRKT; -.
DR OrthoDB; 5352007at2759; -.
DR TreeFam; TF102021; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0060703; F:deoxyribonuclease inhibitor activity; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0044183; F:protein folding chaperone; IEA:Ensembl.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; IEA:InterPro.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:Ensembl.
DR GO; GO:1902511; P:negative regulation of apoptotic DNA fragmentation; IEA:Ensembl.
DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
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 4: Predicted;
KW Apoptosis {ECO:0000256|PROSITE-ProRule:PRU00447};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT DOMAIN 17..96
FT /note="CIDE-N"
FT /evidence="ECO:0000259|PROSITE:PS51135"
FT REGION 210..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..202
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 331 AA; 36365 MW; 52515DB3A6425DDE CRC64;
MEVSWGASGP EPGDNQALKP CLLRRNHSRE QYGVAASCLE DLRSKAYDIL AMDKSLAPIT
LVLAEDGTIV DDDDYFLCLP SNTKFVALAG NEKWAYNNSD GGTAWLSQES VDVDETDSGA
ELKWRNVARQ LKEDLSSIVL LSEEDLQVLI DVPCADLAQE LGQSCVTVQG LQNTLQQVLD
QREEARQSRQ LLELYLQALE KEGSILSKQQ ESQAGLGDGG DAVDTGLSRE PSSEIALSSQ
ILTVLKEKPA PELSLSSQDL ELVTKEDPKA LAVALHWDVK KTETVQQACE QELSLRLQQV
QSLHSLRSIS ARRDSLPGEQ QNPKRARQEP A
//
