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Q10714

- ACE_DROME

UniProt

Q10714 - ACE_DROME

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Protein
Angiotensin-converting enzyme
Gene
Ance, Race, CG8827
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.1 Publication

Catalytic activityi

Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.1 Publication

Cofactori

Binds 1 zinc ion per subunit.

Enzyme regulationi

Inhibited by captopril and, to a lesser extent, by lisinopril, trandolaprilat, fosinoprilat and enalaprilat.2 Publications

Kineticsi

  1. KM=33.5 µM for angiotensin I3 Publications
  2. KM=53.4 µM for N-acetyl-Ser-Asp-Lys-Pro
  3. KM=2.59 mM for Hip-His-Leu
  4. KM=10.26 mM for Hip-His-Leu-NH2
  5. KM=372 µM for (Leu5)enkephalin
  6. KM=1.88 mM for (Leu5)enkephalinamide

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi367 – 3671Zinc; catalytic
Active sitei368 – 3681
Metal bindingi371 – 3711Zinc; catalytic
Metal bindingi395 – 3951Zinc; catalytic

GO - Molecular functioni

  1. carboxypeptidase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: UniProtKB-KW
  4. peptidyl-dipeptidase activity Source: FlyBase
  5. protein binding Source: IntAct

GO - Biological processi

  1. metamorphosis Source: FlyBase
  2. proteolysis Source: FlyBase
  3. response to symbiotic bacterium Source: FlyBase
  4. sperm individualization Source: FlyBase
  5. spermatid nucleus differentiation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKQ10714.

Protein family/group databases

MEROPSiM02.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiotensin-converting enzyme (EC:3.4.15.1)
Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
Gene namesi
Name:Ance
Synonyms:Race
ORF Names:CG8827
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0012037. Ance.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: FlyBase
  2. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Male flies are sterile.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717
Add
BLAST
Chaini18 – 615598Angiotensin-converting enzyme
PRO_0000028563Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531N-linked (GlcNAc...) Inferred
Disulfide bondi133 ↔ 141
Glycosylationi196 – 1961N-linked (GlcNAc...) Inferred
Glycosylationi311 – 3111N-linked (GlcNAc...) Inferred
Disulfide bondi336 ↔ 354
Disulfide bondi467 ↔ 612
Disulfide bondi522 ↔ 540

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ10714.
PRIDEiQ10714.

Expressioni

Tissue specificityi

Expressed in vesicular structures in spermatocytes and early spermatids (at protein level).1 Publication

Developmental stagei

Expressed in the amnioserosa during germ band elongation, shortening and heart morphogenesis. Expressed in midgut throughout embryogenesis.

Gene expression databases

BgeeiQ10714.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTP010192EBI-115736,EBI-751728From a different organism.
KNG1P010422EBI-115736,EBI-6378713From a different organism.

Protein-protein interaction databases

BioGridi60835. 2 interactions.
IntActiQ10714. 3 interactions.
MINTiMINT-808657.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 223
Helixi26 – 5126
Helixi56 – 8025
Helixi85 – 873
Helixi91 – 10111
Helixi104 – 1074
Helixi110 – 12920
Turni145 – 1473
Helixi148 – 1558
Helixi159 – 17315
Helixi175 – 1773
Helixi178 – 19417
Helixi200 – 2056
Helixi206 – 2083
Helixi213 – 24331
Turni245 – 2473
Beta strandi250 – 2523
Helixi256 – 2583
Beta strandi259 – 2613
Helixi268 – 2703
Helixi271 – 2744
Beta strandi278 – 2803
Helixi286 – 2916
Helixi296 – 30914
Helixi317 – 3226
Beta strandi329 – 3313
Beta strandi339 – 3424
Beta strandi344 – 3474
Beta strandi349 – 3524
Helixi359 – 37719
Turni378 – 3803
Helixi383 – 3853
Helixi391 – 40515
Helixi408 – 4136
Beta strandi416 – 4194
Helixi424 – 43815
Helixi441 – 45616
Turni457 – 4593
Helixi462 – 4643
Helixi465 – 47713
Helixi492 – 4943
Helixi496 – 4994
Helixi505 – 52420
Turni525 – 5273
Beta strandi530 – 5356
Helixi537 – 5393
Helixi546 – 55611
Turni557 – 5604
Helixi564 – 5729
Helixi580 – 59920
Beta strandi611 – 6133

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J36X-ray2.40A/B14-615[»]
1J37X-ray2.40A/B14-615[»]
1J38X-ray2.60A/B14-615[»]
2X8YX-ray1.90A17-614[»]
2X8ZX-ray1.98A17-614[»]
2X90X-ray1.98A17-614[»]
2X91X-ray1.98A17-614[»]
2X92X-ray2.11A17-615[»]
2X93X-ray1.98A17-615[»]
2X94X-ray1.88A17-615[»]
2X95X-ray1.96A17-615[»]
2X96X-ray1.85A17-614[»]
2X97X-ray1.85A17-614[»]
2XHMX-ray1.96A17-614[»]
3ZQZX-ray2.35A17-614[»]
4AA1X-ray1.99A17-614[»]
4AA2X-ray1.99A17-614[»]
4ASQX-ray1.99A17-614[»]
4ASRX-ray1.90A17-614[»]
4CA7X-ray1.82A17-614[»]
4CA8X-ray1.99A17-614[»]
ProteinModelPortaliQ10714.
SMRiQ10714. Positions 19-614.

Miscellaneous databases

EvolutionaryTraceiQ10714.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M2 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG71044.
GeneTreeiENSGT00520000055576.
InParanoidiQ10714.
KOiK01283.
OMAiWAYGSNI.
OrthoDBiEOG76HQ13.
PhylomeDBiQ10714.

Family and domain databases

InterProiIPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 1 hit.
PfamiPF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q10714-1 [UniParc]FASTAAdd to Basket

« Hide

MRLFLLALLA TLAVTQALVK EEIQAKEYLE NLNKELAKRT NVETEAAWAY    50
GSNITDENEK KKNEISAELA KFMKEVASDT TKFQWRSYQS EDLKRQFKAL 100
TKLGYAALPE DDYAELLDTL SAMESNFAKV KVCDYKDSTK CDLALDPEIE 150
EVISKSRDHE ELAYYWREFY DKAGTAVRSQ FERYVELNTK AAKLNNFTSG 200
AEAWLDEYED DTFEQQLEDI FADIRPLYQQ IHGYVRFRLR KHYGDAVVSE 250
TGPIPMHLLG NMWAQQWSEI ADIVSPFPEK PLVDVSAEME KQGYTPLKMF 300
QMGDDFFTSM NLTKLPQDFW DKSIIEKPTD GRDLVCHASA WDFYLTDDVR 350
IKQCTRVTQD QLFTVHHELG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV 400
LSLSVSTPKH LEKIGLLKDY VRDDEARINQ LFLTALDKIV FLPFAFTMDK 450
YRWSLFRGEV DKANWNCAFW KLRDEYSGIE PPVVRSEKDF DAPAKYHISA 500
DVEYLRYLVS FIIQFQFYKS ACIKAGQYDP DNVELPLDNC DIYGSAAAGA 550
AFHNMLSMGA SKPWPDALEA FNGERIMSGK AIAEYFEPLR VWLEAENIKN 600
NVHIGWTTSN KCVSS 615
Length:615
Mass (Da):70,914
Last modified:September 11, 2007 - v3
Checksum:i9E3691BCC51D6C48
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 514WAYG → GPMR in AAC46902. 1 Publication
Sequence conflicti141 – 1411C → S in AAC46902. 1 Publication
Sequence conflicti293 – 2931G → A in AAB02171. 1 Publication
Sequence conflicti346 – 3461T → I1 Publication
Sequence conflicti346 – 3461T → I in AAB02171. 1 Publication
Sequence conflicti346 – 3461T → I in AAC46902. 1 Publication
Sequence conflicti346 – 3461T → I1 Publication
Sequence conflicti365 – 3651V → E1 Publication
Sequence conflicti402 – 4021S → A1 Publication
Sequence conflicti414 – 4141I → T1 Publication
Sequence conflicti486 – 4861S → T in AAC46902. 1 Publication
Sequence conflicti533 – 5331V → M in AAC46902. 1 Publication
Sequence conflicti547 – 5471A → R in AAB02171. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25344 mRNA. Translation: AAB02171.1.
U34599 mRNA. Translation: AAC46902.1.
AE014134 Genomic DNA. Translation: AAF53353.2.
AE014134 Genomic DNA. Translation: AAN10856.1.
AY061129 mRNA. Translation: AAL28677.1.
RefSeqiNP_477046.1. NM_057698.4.
NP_723852.1. NM_165070.2.
UniGeneiDm.2157.

Genome annotation databases

EnsemblMetazoaiFBtr0080552; FBpp0080129; FBgn0012037.
FBtr0080553; FBpp0080130; FBgn0012037.
GeneIDi34805.
KEGGidme:Dmel_CG8827.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25344 mRNA. Translation: AAB02171.1 .
U34599 mRNA. Translation: AAC46902.1 .
AE014134 Genomic DNA. Translation: AAF53353.2 .
AE014134 Genomic DNA. Translation: AAN10856.1 .
AY061129 mRNA. Translation: AAL28677.1 .
RefSeqi NP_477046.1. NM_057698.4.
NP_723852.1. NM_165070.2.
UniGenei Dm.2157.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J36 X-ray 2.40 A/B 14-615 [» ]
1J37 X-ray 2.40 A/B 14-615 [» ]
1J38 X-ray 2.60 A/B 14-615 [» ]
2X8Y X-ray 1.90 A 17-614 [» ]
2X8Z X-ray 1.98 A 17-614 [» ]
2X90 X-ray 1.98 A 17-614 [» ]
2X91 X-ray 1.98 A 17-614 [» ]
2X92 X-ray 2.11 A 17-615 [» ]
2X93 X-ray 1.98 A 17-615 [» ]
2X94 X-ray 1.88 A 17-615 [» ]
2X95 X-ray 1.96 A 17-615 [» ]
2X96 X-ray 1.85 A 17-614 [» ]
2X97 X-ray 1.85 A 17-614 [» ]
2XHM X-ray 1.96 A 17-614 [» ]
3ZQZ X-ray 2.35 A 17-614 [» ]
4AA1 X-ray 1.99 A 17-614 [» ]
4AA2 X-ray 1.99 A 17-614 [» ]
4ASQ X-ray 1.99 A 17-614 [» ]
4ASR X-ray 1.90 A 17-614 [» ]
4CA7 X-ray 1.82 A 17-614 [» ]
4CA8 X-ray 1.99 A 17-614 [» ]
ProteinModelPortali Q10714.
SMRi Q10714. Positions 19-614.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 60835. 2 interactions.
IntActi Q10714. 3 interactions.
MINTi MINT-808657.

Protein family/group databases

MEROPSi M02.003.

Proteomic databases

PaxDbi Q10714.
PRIDEi Q10714.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0080552 ; FBpp0080129 ; FBgn0012037 .
FBtr0080553 ; FBpp0080130 ; FBgn0012037 .
GeneIDi 34805.
KEGGi dme:Dmel_CG8827.

Organism-specific databases

CTDi 34805.
FlyBasei FBgn0012037. Ance.

Phylogenomic databases

eggNOGi NOG71044.
GeneTreei ENSGT00520000055576.
InParanoidi Q10714.
KOi K01283.
OMAi WAYGSNI.
OrthoDBi EOG76HQ13.
PhylomeDBi Q10714.

Enzyme and pathway databases

SABIO-RK Q10714.

Miscellaneous databases

EvolutionaryTracei Q10714.
GenomeRNAii 34805.
NextBioi 790306.

Gene expression databases

Bgeei Q10714.

Family and domain databases

InterProi IPR001548. Peptidase_M2.
[Graphical view ]
PANTHERi PTHR10514. PTHR10514. 1 hit.
Pfami PF01401. Peptidase_M2. 1 hit.
[Graphical view ]
PRINTSi PR00791. PEPDIPTASEA.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterisation of putative Drosophila angiotensin converting enzyme cDNA clones."
    Cornell M.J., Coates D., Isaac R.E.
    Biochem. Soc. Trans. 21:243-243(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  2. "Cloning and expression of an evolutionary conserved single-domain angiotensin converting enzyme from Drosophila melanogaster."
    Cornell M.J., Williams T.A., Lamango N.S., Coates D., Corvol P., Soubrier F., Hoheisel J., Lehrach H., Isaac R.E.
    J. Biol. Chem. 270:13613-13619(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  3. Cornell M.J.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. "Race: a Drosophila homologue of the angiotensin converting enzyme."
    Tatei K., Cai H., Ip Y.T., Levine M.
    Mech. Dev. 51:157-168(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Canton-S.
  5. "An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
    Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.
    , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
    Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  6. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  7. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  9. "Drosophila melanogaster angiotensin I-converting enzyme expressed in Pichia pastoris resembles the C domain of the mammalian homologue and does not require glycosylation for secretion and enzymic activity."
    Williams T.A., Michaud A., Houard X., Chauvet M.-T., Soubrier F., Corvol P.
    Biochem. J. 318:125-131(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE SITE, GLYCOSYLATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  10. "The Drosophila melanogaster-related angiotensin-I-converting enzymes Acer and Ance -- distinct enzymic characteristics and alternative expression during pupal development."
    Houard X., Williams T.A., Michaud A., Dani P., Isaac R.E., Shirras A.D., Coates D., Corvol P.
    Eur. J. Biochem. 257:599-606(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  11. "The Drosophila angiotensin-converting enzyme homologue Ance is required for spermiogenesis."
    Hurst D., Rylett C.M., Isaac R.E., Shirras A.D.
    Dev. Biol. 254:238-247(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, FUNCTION, DISRUPTION PHENOTYPE.
  12. "Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril."
    Kim H.M., Shin D.R., Yoo O.J., Lee H., Lee J.-O.
    FEBS Lett. 538:65-70(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 14-615, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 14-615 IN COMPLEX WITH CAPTOPRIL, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 14-615 IN COMPLEX WITH LISINOPRIL.

Entry informationi

Entry nameiACE_DROME
AccessioniPrimary (citable) accession number: Q10714
Secondary accession number(s): A4V0P3
, Q27572, Q9NKE4, Q9TX66, Q9VJV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 11, 2007
Last modified: July 9, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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