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Apaf-1 related killer DARK (Apaf-1/CED-4-related caspase activator Dapaf-1L) (Cell death protein HAC-1) (Death-associated APAF1-related killer, isoform B) (FI21208p1)

 Q7KLI1_DROME            Unreviewed;      1440 AA.
Q7KLI1;
03-OCT-2006, integrated into UniProtKB/TrEMBL.
03-OCT-2006, sequence version 1.
03-JUL-2019, entry version 132.
SubName: Full=Apaf-1 related killer DARK {ECO:0000313|EMBL:AAD45988.1};
SubName: Full=Apaf-1/CED-4-related caspase activator Dapaf-1L {ECO:0000313|EMBL:BAA86939.1};
SubName: Full=Cell death protein HAC-1 {ECO:0000313|EMBL:AAF07207.2};
SubName: Full=Death-associated APAF1-related killer, isoform B {ECO:0000313|EMBL:AAF57916.1};
SubName: Full=FI21208p1 {ECO:0000313|EMBL:AHA95701.1};
Name=Dark {ECO:0000313|EMBL:AAF57916.1,
ECO:0000313|FlyBase:FBgn0263864};
Synonyms=anon-53Fa {ECO:0000313|EMBL:AAF57916.1},
Apaf {ECO:0000313|EMBL:AAF57916.1},
APAF-1 {ECO:0000313|EMBL:AAF57916.1},
Apaf-1 {ECO:0000313|EMBL:AAF57916.1},
apaf-1 {ECO:0000313|EMBL:AAF57916.1},
Apaf-I {ECO:0000313|EMBL:AAF57916.1},
APAF1 {ECO:0000313|EMBL:AAF57916.1},
Apaf1 {ECO:0000313|EMBL:AAF57916.1},
apaf1 {ECO:0000313|EMBL:AAF57916.1},
arc {ECO:0000313|EMBL:AAF57916.1}, ARK {ECO:0000313|EMBL:AAF57916.1},
Ark {ECO:0000313|FlyBase:FBgn0263864},
ark {ECO:0000313|EMBL:AAF57916.1},
Ark-RB {ECO:0000313|EMBL:AHA95701.1},
D-Apaf-1 {ECO:0000313|EMBL:AAF57916.1},
dapaf {ECO:0000313|EMBL:AAF57916.1},
Dapaf-1 {ECO:0000313|EMBL:AAF57916.1},
dAPAF-1 {ECO:0000313|EMBL:AAF57916.1},
dApaf-1 {ECO:0000313|EMBL:AAF57916.1},
dapaf-1 {ECO:0000313|EMBL:AAF57916.1},
dapaf-1L {ECO:0000313|EMBL:AAF57916.1},
dapaf-1S {ECO:0000313|EMBL:AAF57916.1},
dApaf1 {ECO:0000313|EMBL:AAF57916.1},
DARK {ECO:0000313|EMBL:AAF57916.1},
dArk {ECO:0000313|EMBL:AAF57916.1},
dark {ECO:0000313|EMBL:AAF57916.1},
Dmel\CG6829 {ECO:0000313|EMBL:AAF57916.1},
HAC-1 {ECO:0000313|EMBL:AAF57916.1},
Hac-1 {ECO:0000313|EMBL:AAF57916.1},
hac-1 {ECO:0000313|EMBL:AAF57916.1},
HAC1 {ECO:0000313|EMBL:AAF57916.1},
Hac1 {ECO:0000313|EMBL:AAF07207.2},
hac1 {ECO:0000313|EMBL:AAF57916.1},
l(2)SH0173 {ECO:0000313|EMBL:AAF57916.1},
T1 {ECO:0000313|EMBL:AAF57916.1};
ORFNames=CG6829 {ECO:0000313|EMBL:AAF57916.1,
ECO:0000313|FlyBase:FBgn0263864},
Dmel_CG6829 {ECO:0000313|EMBL:AAF57916.1};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000313|EMBL:AAD45988.1};
[1] {ECO:0000313|EMBL:AAF07207.2}
NUCLEOTIDE SEQUENCE.
PubMed=10619022; DOI=10.1016/S1097-2765(00)80385-8;
Zhou L., Song Z., Tittel J., Steller H.;
"HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in
developmental and radiation-induced apoptosis.";
Mol. Cell 4:745-755(1999).
[2] {ECO:0000313|EMBL:BAA86939.1}
NUCLEOTIDE SEQUENCE.
PubMed=10619023; DOI=10.1016/S1097-2765(00)80386-X;
Kanuka H., Sawamoto K., Inohara N., Matsuno K., Okano H., Miura M.;
"Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-
1/CED-4-related caspase activator.";
Mol. Cell 4:757-769(1999).
[3] {ECO:0000313|EMBL:AAD45988.1}
NUCLEOTIDE SEQUENCE.
PubMed=10559939; DOI=10.1038/12984;
Rodriguez A., Oliver H., Zou H., Chen P., Wang X., Abrams J.M.;
"Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an
evolutionarily conserved death pathway.";
Nat. Cell Biol. 1:272-279(1999).
[4] {ECO:0000313|EMBL:AAD45988.1}
NUCLEOTIDE SEQUENCE.
Rodriquez A., Oliver H., Chen P., Zou H., Wang X., Abrams J.M.;
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:AAF07207.2}
NUCLEOTIDE SEQUENCE.
Zhou L., Song Z., Tittel J., Steller H.;
"HAC-1, a Drosophila homolog of APAF-1 and CED-4, functions in
deveopmental and readiation-induced apoptosis.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J.,
Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[7] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537568;
Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
"Finishing a whole-genome shotgun: release 3 of the Drosophila
melanogaster euchromatic genome sequence.";
Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
[8] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[9] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537573;
Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
Ashburner M., Celniker S.E.;
"The transposable elements of the Drosophila melanogaster euchromatin:
a genomics perspective.";
Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002).
[10] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537574;
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
Karpen G.H.;
"Heterochromatic sequences in a Drosophila whole-genome shotgun
assembly.";
Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
[11] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
Ashburner M., Anxolabehere D.;
"Combined evidence annotation of transposable elements in genome
sequences.";
PLoS Comput. Biol. 1:166-175(2005).
[12] {ECO:0000313|EMBL:AAF57916.1}
NUCLEOTIDE SEQUENCE.
Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
Svirskas R., Rubin G.;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[13] {ECO:0000313|EMBL:AAF57916.1}
NUCLEOTIDE SEQUENCE.
Berkeley Drosophila Genome Project;
Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E.,
Yu C., Rubin G.;
"Drosophila melanogaster release 4 sequence.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[14] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569856; DOI=10.1126/science.1139815;
Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
"The Release 5.1 annotation of Drosophila melanogaster
heterochromatin.";
Science 316:1586-1591(2007).
[15] {ECO:0000313|EMBL:AAF57916.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569867; DOI=10.1126/science.1139816;
Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
Dimitri P., Karpen G.H., Celniker S.E.;
"Sequence finishing and mapping of Drosophila melanogaster
heterochromatin.";
Science 316:1625-1628(2007).
[16] {ECO:0000213|PDB:4V4L}
STRUCTURE BY ELECTRON MICROSCOPY (6.90 ANGSTROMS) OF 1-583.
PubMed=21220123; DOI=10.1016/j.str.2010.10.009;
Yuan S., Yu X., Topf M., Dorstyn L., Kumar S., Ludtke S.J., Akey C.W.;
"Structure of the Drosophila apoptosome at 6.9a resolution.";
Structure 19:128-140(2011).
[17] {ECO:0000313|EMBL:AHA95701.1}
NUCLEOTIDE SEQUENCE.
Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
[18] {ECO:0000313|EMBL:AAF57916.1}
NUCLEOTIDE SEQUENCE.
PubMed=26109357; DOI=.1534/g3.115.018929;
FlyBase Consortium;
Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B.,
St Pierre S.E., Gramates L.S., Zhou P., Schroeder A.J., Falls K.,
Strelets V., Russo S.M., Gelbart W.M.;
"Gene Model Annotations for Drosophila melanogaster: Impact of High-
Throughput Data.";
G3 (Bethesda) 5:1721-1736(2015).
[19] {ECO:0000313|EMBL:AAF57916.1}
NUCLEOTIDE SEQUENCE.
PubMed=26109356; DOI=.1534/g3.115.018937;
FlyBase Consortium;
Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B.,
St Pierre S.E., Zhou P., Schroeder A.J., Falls K., Emmert D.B.,
Russo S.M., Gelbart W.M.;
"Gene Model Annotations for Drosophila melanogaster: The Rule-
Benders.";
G3 (Bethesda) 5:1737-1749(2015).
[20] {ECO:0000213|PDB:3J9K, ECO:0000213|PDB:3J9L}
STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) OF 1-583 IN COMPLEX
WITH ADP.
PubMed=25644603; DOI=10.1101/gad.255877.114;
Pang Y., Bai X.C., Yan C., Hao Q., Chen Z., Wang J.W., Scheres S.H.,
Shi Y.;
"Structure of the apoptosome: mechanistic insights into activation of
an initiator caspase from Drosophila.";
Genes Dev. 29:277-287(2015).
[21] {ECO:0000213|PDB:5JUL}
STRUCTURE BY ELECTRON MICROSCOPY (4.40 ANGSTROMS).
PubMed=27916517; DOI=10.1016/j.str.2016.11.002;
Cheng T.C., Akey I.V., Yuan S., Yu Z., Ludtke S.J., Akey C.W.;
"A Near-Atomic Structure of the Dark Apoptosome Provides Insight into
Assembly and Activation.";
Structure 25:40-52(2017).
[22] {ECO:0000313|EMBL:AAF57916.1}
NUCLEOTIDE SEQUENCE.
FlyBase;
Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-3404349, EBI-3404349;
Q9XYF4:Dronc; NbExp=3; IntAct=EBI-3404349, EBI-108311;
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EMBL; AF162659; AAD45988.1; -; mRNA.
EMBL; AF196306; AAF07207.2; -; mRNA.
EMBL; AE013599; AAF57916.1; -; Genomic_DNA.
EMBL; BT150397; AHA95701.1; -; mRNA.
EMBL; AB027531; BAA86939.1; -; mRNA.
RefSeq; NP_725637.1; NM_166207.3.
PDB; 3J9K; EM; 4.10 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e=1-583.
PDB; 3J9L; EM; 4.00 A; A/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q=1-583.
PDB; 4V4L; EM; 6.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-583.
PDB; 5JUL; EM; 4.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-1440.
PDBsum; 3J9K; -.
PDBsum; 3J9L; -.
PDBsum; 4V4L; -.
PDBsum; 5JUL; -.
IntAct; Q7KLI1; 2.
STRING; 7227.FBpp0086122; -.
EnsemblMetazoa; FBtr0086968; FBpp0086122; FBgn0263864.
GeneID; 36914; -.
KEGG; dme:Dmel_CG6829; -.
UCSC; CG6829-RB; d. melanogaster.
CTD; 36914; -.
FlyBase; FBgn0263864; Dark.
eggNOG; KOG4658; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00940000157710; -.
KO; K02084; -.
OMA; NLGCKIL; -.
ChiTaRS; Dark; fly.
GenomeRNAi; 36914; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0263864; Expressed in 22 organ(s), highest expression level in head mesoderm (Drosophila).
GO; GO:0043293; C:apoptosome; IDA:FlyBase.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0043531; F:ADP binding; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IDA:FlyBase.
GO; GO:0050700; F:CARD domain binding; ISM:FlyBase.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISS:FlyBase.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IDA:FlyBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IPI:FlyBase.
GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IMP:FlyBase.
GO; GO:0006915; P:apoptotic process; TAS:FlyBase.
GO; GO:0021556; P:central nervous system formation; IMP:FlyBase.
GO; GO:0022416; P:chaeta development; IMP:FlyBase.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0035006; P:melanization defense response; IMP:FlyBase.
GO; GO:0002921; P:negative regulation of humoral immune response; IMP:FlyBase.
GO; GO:0070050; P:neuron cellular homeostasis; IGI:FlyBase.
GO; GO:0043065; P:positive regulation of apoptotic process; IGI:FlyBase.
GO; GO:0046672; P:positive regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
GO; GO:0034352; P:positive regulation of glial cell apoptotic process; IMP:FlyBase.
GO; GO:0012501; P:programmed cell death; IDA:FlyBase.
GO; GO:0051291; P:protein heterooligomerization; IDA:FlyBase.
GO; GO:0051260; P:protein homooligomerization; IDA:FlyBase.
GO; GO:0046668; P:regulation of retinal cell programmed cell death; NAS:FlyBase.
GO; GO:0010332; P:response to gamma radiation; IDA:FlyBase.
GO; GO:0042594; P:response to starvation; IMP:FlyBase.
GO; GO:0033353; P:S-adenosylmethionine cycle; IMP:FlyBase.
GO; GO:0035071; P:salivary gland cell autophagic cell death; IMP:FlyBase.
GO; GO:0035070; P:salivary gland histolysis; IMP:FlyBase.
GO; GO:1901053; P:sarcosine catabolic process; IMP:FlyBase.
GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
GO; GO:0070328; P:triglyceride homeostasis; IMP:FlyBase.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR002182; NB-ARC.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF00931; NB-ARC; 1.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50978; SSF50978; 2.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:3J9K, ECO:0000213|PDB:3J9L,
ECO:0000213|PDB:4V4L, ECO:0000213|PDB:5JUL};
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Reference proteome {ECO:0000313|Proteomes:UP000000803}.
DOMAIN 135 303 NB-ARC. {ECO:0000259|Pfam:PF00931}.
REGION 1269 1289 Disordered. {ECO:0000256|MobiDB-
lite:Q7KLI1}.
SEQUENCE 1440 AA; 165619 MW; 74EFEAD06E54FA74 CRC64;
MDFETGEHQY QYKDILSVFE DAFVDNFDCK DVQDMPKSIL SKEEIDHIIM SKDAVSGTLR
LFWTLLSKQE EMVQKFVEEV LRINYKFLMS PIKTEQRQPS MMTRMYIEQR DRLYNDNQVF
AKYNVSRLQP YLKLRQALLE LRPAKNVLID GVLGSGKTWV ALDVCLSYKV QCKMDFKIFW
LNLKNCNSPE TVLEMLQKLL YQIDPNWTSR SDHSSNIKLR IHSIQAELRR LLKSKPYENC
LLVLLNVQNA KAWNAFNLSC KILLTTRFKQ VTDFLSAATT THISLDHHSM TLTPDEVKSL
LLKYLDCRPQ DLPREVLTTN PRRLSIIAES IRDGLATWDN WKHVNCDKLT TIIESSLNVL
EPAEYRKMFD RLSVFPPSAH IPTILLSLIW FDVIKSDVMV VVNKLHKYSL VEKQPKESTI
SIPSIYLELK VKLENEYALH RSIVDHYNIP KTFDSDDLIP PYLDQYFYSH IGHHLKNIEH
PERMTLFRMV FLDFRFLEQK IRHDSTAWNA SGSILNTLQQ LKFYKPYICD NDPKYERLVN
AILDFLPKIE ENLICSKYTD LLRIALMAED EAIFEEAHKQ VQRFDDRVWF TNHGRFHQHR
QIINLGDNEG RHAVYLHNDF CLIALASGQI LLTDVSLEGE DTYLLRDESD SSDILRMAVF
NQQKHLITLH CNGSVKLWSL WPDCPGRRHS GGSKQQLVNS VVKRFIGSYA NLKIVAFYLN
EDAGLPEANI QLHVAFINGD VSILNWDEQD QEFKLSHVPV LKTMQSGIRC FVQVLKRYYV
VCTSNCTLTV WDLTNGSSNT LELHVFNVEN DTPLALDVFD ERSKTATVLL IFKYSVWRLN
FLPGLSVSLQ SEAVQLPEGS FITCGKRSTD GRYLLLGTSE GLIVYDLKIS DPVLRSNVSE
HIECVDIYEL FDPVYKYIVL CGAKGKQVVH VHTLRSVSGS NSHQNREIAW VHSADEISVM
TKACLEPNVY LRSLMDMTRE RTQLLAVDSK ERIHLIKPAI SRISEWSTIT PTHAASNCKI
NAISAFNDEQ IFVGYVDGVI IDVIHDTALP QQFIEEPIDY LKQVSPNILV ASAHSAQKTV
IFQLEKIDPL QPNDQWPLMM DVSTKYASLQ EGQYIILFSD HGVCHLDIAN PSAFVKPKDS
EEYIVGFDLK NSLLFLAYEN NIIDVFRLIF SCNQLRYEQI CEEEIAQKAK ISYLVATDDG
TMLAMGFENG TLELFAVENR KVQLIYSIEE VHEHCIRQLL FSPCKLLLIS CAEQLCFWNV
THMRNNQLER EQKRRRSRRH KQHSVTQEDA VDAAPIAADI DVDVTFVADE FHPVNRGTAE
LWRNKRGNAI RPELLACVKF VGNEARQFFT DAHFSHFYAI DDEGVYYHLQ LLELSRLQPP
PDPVTLDIAN QYEDLKNLRI LDSPLMQDSD SEGADVVGNL VLEKNGGVAR ATPILEEASS


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ant-401 Mouse Anti Human Natural killer cell p44-related protein 20
ant-402 Mouse Anti Human Natural killer cell p30-related protein 20
ant-402 Mouse Anti Human Natural killer cell p30-related protein 100
ant-401 Mouse Anti Human Natural killer cell p44-related protein 5
ant-401 Mouse Anti Human Natural killer cell p44-related protein 100
ant-402 Mouse Anti Human Natural killer cell p30-related protein 5
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ant-401 Mouse Anti Human Natural killer cell p44-related protein NKp44 5
ant-402 Mouse Anti Human Natural killer cell p30-related protein NKp30 5
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Pathways :
WP731: Sterol regulatory element binding protein related
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP2080: TFs Regulate miRNAs related to cardiac hypertrophy
WP1559: TFs Regulate miRNAs related to cardiac hypertrophy
WP1937: Transport of vitamins, nucleosides, and related molecules
WP1497: Hedgehog-related genes
WP201: Ptf1a related regulatory pathway
WP1770: One carbon metabolism and related pathways
WP367: Programmed Cell Death
WP2371: Parkinsons Disease Pathway
WP656: p53 signal pathway
WP655: p53 pathway
WP2256: Integrated Pancreatic Cancer Pathway
WP45: G1 to S cell cycle control
WP908: B Cell Receptor Signaling Pathway
WP1011: T Cell Receptor Signaling Pathway
WP1493: Carbon assimilation C4 pathway
WP1694: Pyrimidine metabolism
WP2059: Alzheimers Disease
WP274: B Cell Receptor Signaling Pathway
WP74: Integrin-mediated cell adhesion
WP1185: Integrin-mediated cell adhesion
WP1657: Glycerolipid metabolism
WP1888: Post-translational protein modification

Related Genes :
[NLRP1 CARD7 DEFCAP KIAA0926 NAC NALP1] NACHT, LRR and PYD domains-containing protein 1 (Caspase recruitment domain-containing protein 7) (Death effector filament-forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain)
[ced-3 C48D1.2] Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]
[NLRP3 C1orf7 CIAS1 NALP3 PYPAF1] NACHT, LRR and PYD domains-containing protein 3 (Angiotensin/vasopressin receptor AII/AVP-like) (Caterpiller protein 1.1) (CLR1.1) (Cold-induced autoinflammatory syndrome 1 protein) (Cryopyrin) (PYRIN-containing APAF1-like protein 1)
[Nlrp3 Cias1 Mmig1 Nalp3 Pypaf1] NACHT, LRR and PYD domains-containing protein 3 (Cold autoinflammatory syndrome 1 protein homolog) (Cryopyrin) (Mast cell maturation-associated-inducible protein 1) (PYRIN-containing APAF1-like protein 1)
[ced-10 rac-1 C09G12.8] Ras-related protein ced-10 (CErac1) (Cell death protein 10) (Cell-corpse engulfment protein ced-10) (Ras-related protein rac-1)
[DNM1L DLP1 DRP1] Dynamin-1-like protein (EC 3.6.5.5) (Dnm1p/Vps1p-like protein) (DVLP) (Dynamin family member proline-rich carboxyl-terminal domain less) (Dymple) (Dynamin-like protein) (Dynamin-like protein 4) (Dynamin-like protein IV) (HdynIV) (Dynamin-related protein 1)
[Nlrp3 Nalp3 Pypaf1] NACHT, LRR and PYD domains-containing protein 3 (Cold autoinflammatory syndrome 1 protein homolog) (Cryopyrin) (Mast cell maturation-associated-inducible protein 1) (PYRIN-containing APAF1-like protein 1)
[Dredd DCP2 CG7486] Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10]
[CASP8 MCH5] Caspase-8 (CASP-8) (EC 3.4.22.61) (Apoptotic cysteine protease) (Apoptotic protease Mch-5) (CAP4) (FADD-homologous ICE/ced-3-like protease) (FADD-like ICE) (FLICE) (ICE-like apoptotic protease 5) (MORT1-associated ced-3 homolog) (MACH) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]
[NLRC4 CARD12 CLAN CLAN1 IPAF UNQ6189/PRO20215] NLR family CARD domain-containing protein 4 (CARD, LRR, and NACHT-containing protein) (Clan protein) (Caspase recruitment domain-containing protein 12) (Ice protease-activating factor) (Ipaf)
[Ceacam1 Bgp Bgp1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)
[Bok Mtd] Bcl-2-related ovarian killer protein (Apoptosis activator Mtd) (Protein matador)
[PYCARD ASC CARD5 TMS1] Apoptosis-associated speck-like protein containing a CARD (hASC) (Caspase recruitment domain-containing protein 5) (PYD and CARD domain-containing protein) (Target of methylation-induced silencing 1)
[Nlrp6 Nalp6 Navr Pypaf5] NACHT, LRR and PYD domains-containing protein 6 (Angiotensin II/vasopressin receptor) (Non-angiotensin-vasopressin receptor) (Non-AVR) (PYRIN-containing APAF1-like protein 5-like)
[ced-1 Y47H9C.4] Cell death abnormality protein 1
[ced-9 T07C4.8] Apoptosis regulator ced-9 (Cell death protein 9)
[Ceacam1] Carcinoembryonic antigen-related cell adhesion molecule 1 (ATP-dependent taurocolate-carrier protein) (Cell-CAM 105) (C-CAM 105) (Ecto-ATPase) (GP110) (pp120) (CD antigen CD66a)
[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[DAPK2] Death-associated protein kinase 2 (DAP kinase 2) (EC 2.7.11.1) (DAP-kinase-related protein 1) (DRP-1)
[ced-8 F08F1.5] Cell death abnormality protein 8
[ced-4 C35D10.9] Cell death protein 4
[MCL1 BCL2L3] Induced myeloid leukemia cell differentiation protein Mcl-1 (Bcl-2-like protein 3) (Bcl2-L-3) (Bcl-2-related protein EAT/mcl1) (mcl1/EAT)
[RERE ARG ARP ATN1L KIAA0458] Arginine-glutamic acid dipeptide repeats protein (Atrophin-1-like protein) (Atrophin-1-related protein)
[CEACAM1 BGP BGP1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (CD antigen CD66a)
[BOK BCL2L9] Bcl-2-related ovarian killer protein (hBOK) (Bcl-2-like protein 9) (Bcl2-L-9)
[gag-pol] Gag-Pol polyprotein (Pr180gag-pol) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-pol); Protease p14 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p80 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[CASP2 ICH1 NEDD2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[CASP10 MCH4] Caspase-10 (CASP-10) (EC 3.4.22.63) (Apoptotic protease Mch-4) (FAS-associated death domain protein interleukin-1B-converting enzyme 2) (FLICE2) (ICE-like apoptotic protease 4) [Cleaved into: Caspase-10 subunit p23/17; Caspase-10 subunit p12]
[Bok] Bcl-2-related ovarian killer protein
[Cd244 2b4 Nmrk] Natural killer cell receptor 2B4 (NK cell type I receptor protein 2B4) (NKR2B4) (Non-MHC restricted killing associated) (SLAM family member 4) (SLAMF4) (Signaling lymphocytic activation molecule 4) (CD antigen CD244)

Bibliography :