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Reviewed, UniProtKB/Swiss-Prot Q24306 (IAP1_DROME)

Last modified November 4, 2008. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Apoptosis 1 inhibitor
Alternative name(s):
    Inhibitor of apoptosis 1
    dIAP1
    Protein thread
Gene names
Name: th
Synonyms: Iap1
ORF Names: CG12284
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Apoptotic suppressor. Overexpression suppresses RPR and W-dependent cell death in the eye. Interaction of th with Nc is required to suppress Nc-mediated cell death; th-mediated ubiquitination of Nc.

Subunit structure

Interacts with Nc; BIR 2 domain interacts with residues 114-125 of Nc. Rpr, W and grim can out compete Nc for binding th therefore removing th-mediated ubiquitination.

Sequence similarities

Belongs to the IAP family.

Contains 2 BIR repeats.

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAM50178.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Apoptosis 1 inhibitor
PRO_0000122367

Regions

Repeat44 – 11067BIR 1
Repeat226 – 29368BIR 2
Zinc finger391 – 42636RING-type

Experimental info

Sequence conflict3191S → T in AAC41609. Ref.1
Sequence conflict324 – 3252VA → DT in AAC41609. Ref.1

Secondary structure

1 .......................................... 438
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q24306-1 [UniParc].

Last modified November 23, 2004. Version 2.
Checksum: 24CA8BC13F5DEF31

FASTA43848,038
        10         20         30         40         50         60 
MASVVADLPS YGPIAFDQVD NNTNATQLFK NNINKTRMND LNREETRLKT FTDWPLDWLD 

        70         80         90        100        110        120 
KRQLAQTGMY FTHAGDKVKC FFCGVEIGCW EQEDQPVPEH QRWSPNCPLL RRRTTNNVPI 

       130        140        150        160        170        180 
NAEALDRILP PISYDICGAN DSTLEMREHA YAEGVIPMSQ LIQSIGMNAV NAAGSVTGTA 

       190        200        210        220        230        240 
APQPRVTVAT HASTATQATG DVQPETCRPS AASGNYFPQY PEYAIETARL RTFEAWPRNL 

       250        260        270        280        290        300 
KQKPHQLAEA GFFYTGVGDR VRCFSCGGGL MDWNDNDEPW EQHALWLSQC RFVKLMKGQL 

       310        320        330        340        350        360 
YIDTVAAKPV LAEEKEESSS IGGVAVASTQ ASEEEQQTSL SSEEAVSGDV APSVAPTAAT 

       370        380        390        400        410        420 
RIFNKIVEAT AVATPSTNSS GSTSIPEEKL CKICYGAEYN TAFLPCGHVV ACAKCASSVT 

       430 
KCPLCRKPFT DVMRVYFS

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References

« Hide 'large scale' references
[1]"Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death."
Hay B.A., Wassarman D.A., Rubin G.M.
Cell 83:1253-1262(1995) [PubMed: 8548811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Eye imaginal disk.
[2]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 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.A., 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.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., 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.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., 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., Woodage T., 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.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-438.
Strain: Berkeley.
Tissue: Head.
[5]"The Drosophila caspase DRONC is regulated by DIAP1."
Meier P., Silke J., Leevers S.J., Evan G.I.
EMBO J. 19:598-611(2000) [PubMed: 10675329] [Abstract]
Cited for: INTERACTION WITH NC.
Tissue: Embryo.
[6]"Structural analysis of a functional DIAP1 fragment bound to grim and hid peptides."
Wu J.W., Cocina A.E., Chai J., Hay B.A., Shi Y.
Mol. Cell 8:95-104(2001) [PubMed: 11511363] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 215-310.
[7]"Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination."
Chai J., Yan N., Huh J.R., Wu J.-W., Li W., Hay B.A., Shi Y.
Nat. Struct. Biol. 10:892-898(2003) [PubMed: 14517550] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 201-324 IN COMPLEX WITH NC, FUNCTION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L49440 mRNA. Translation: AAC41609.1.
AE014296 Genomic DNA. Translation: AAF49548.1.
AE014296 Genomic DNA. Translation: AAN11757.1.
AY119524 mRNA. Translation: AAM50178.1. Sequence problems.
RefSeqNP_524101.2.
NP_730097.1.
NP_730098.1.
UniGeneDm.6466

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JD4X-ray2.70A/B201-323[»]
1JD5X-ray1.90A201-323[»]
1JD6X-ray2.70A201-323[»]
1Q4QX-ray2.10A/B/C/D/E/F/G/H/I/J201-323[»]
1SDZX-ray1.78A30-145[»]
1SE0X-ray1.75A30-145[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ24306.

Protein family/group databases

MEROPSI32.009.

Genome annotation databases

EnsemblCG12284. Drosophila melanogaster. [Contig view]
GeneID39753.
KEGGdme:Dmel_CG12284.

Organism-specific databases

FlyBaseFBgn0003691. th.

Phylogenomic databases

HOGENOMQ24306.

Gene expression databases

ArrayExpressQ24306.
GermOnlineCG12284. Drosophila melanogaster.

Family and domain databases

InterProIPR001370. Prot_inh_I32_IAP.
IPR001841. Znf_RING.
[Graphical view]
PfamPF00653. BIR. 2 hits.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00238. BIR. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEPS01282. BIR_REPEAT_1. 2 hits.
PS50143. BIR_REPEAT_2. 2 hits.
PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio815208.

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Entry information

Entry nameIAP1_DROME
AccessionPrimary (citable) accession number: Q24306
Secondary accession number(s): A4V1Z9 expand/collapse secondary AC list , Q0E8E4, Q8MRM5, Q9VUX5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 23, 2004
Last modified: November 4, 2008
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents