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Protein

Aspartyl aminopeptidase 1

Gene

aap1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Aspartyl aminopeptidase that is able to remove aspartyl residue at N-terminus of angiotensin I. Acts also as a chaperone and efficiently suppressed the thermal aggregation of citrate synthase.1 Publication

Catalytic activityi

Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.1 Publication

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871Zinc 1By similarity
Binding sitei162 – 1621SubstrateBy similarity
Metal bindingi256 – 2561Zinc 1By similarity
Metal bindingi256 – 2561Zinc 2By similarity
Binding sitei292 – 2921SubstrateBy similarity
Metal bindingi293 – 2931Zinc 2By similarity
Metal bindingi337 – 3371Zinc 1By similarity
Binding sitei337 – 3371SubstrateBy similarity
Binding sitei340 – 3401SubstrateBy similarity
Binding sitei365 – 3651SubstrateBy similarity
Binding sitei372 – 3721SubstrateBy similarity
Metal bindingi431 – 4311Zinc 2By similarity

GO - Molecular functioni

  • metalloaminopeptidase activity Source: PomBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • chaperone-mediated protein folding Source: PomBase
  • proteolysis Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Chaperone, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.11.21. 5613.

Protein family/group databases

MEROPSiM18.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartyl aminopeptidase 1 (EC:3.4.11.21)
Gene namesi
Name:aap1
ORF Names:SPAC4F10.02
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC4F10.02.
PomBaseiSPAC4F10.02. aap1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 467467Aspartyl aminopeptidase 1PRO_0000173454Add
BLAST

Proteomic databases

MaxQBiO36014.

Interactioni

Subunit structurei

Tetrahedron-shaped homododecamer built from six homodimers.By similarity

Protein-protein interaction databases

BioGridi280020. 2 interactions.
MINTiMINT-4672902.

Structurei

3D structure databases

ProteinModelPortaliO36014.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M18 family.Curated

Phylogenomic databases

HOGENOMiHOG000253244.
KOiK01267.
OMAiAIHMNRE.
PhylomeDBiO36014.

Family and domain databases

Gene3Di2.30.250.10. 1 hit.
InterProiIPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]
PfamiPF02127. Peptidase_M18. 1 hit.
[Graphical view]
PRINTSiPR00932. AMINO1PTASE.

Sequencei

Sequence statusi: Complete.

O36014-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTATAKSCAL DFLDFVNASP TPYHAVQNLA EHYMSHGFQY LSEKSDWQSK
60 70 80 90 100
IEPGNSYFVT RNKSSIIAFS IGKKWKPGNG FSIIATHTDS PTLRLKPKSQ
110 120 130 140 150
KSAYGYLQVG VEKYGGGIWH TWFDRDLSLA GRVMVEEEDG RVIQYNVHID
160 170 180 190 200
RPLLRIPTLA IHLDPSANSS FSFNMETEFV PLIGLENELA KEETSDNGDK
210 220 230 240 250
YHHPVLLSLL ANEISKSLET TIDPSKIVDF ELILGDAEKA RLGGIHEEFV
260 270 280 290 300
FSPRLDNLGM TFCASQALTK SLENNSLDNE SCVRVVPSFD HEEIGSVSAQ
310 320 330 340 350
GAESTFLPAV LQRICELGKE SSLFSISMVK SFLVSADMAH AMHPNYSSRY
360 370 380 390 400
ENSNTPFLNK GTVIKVNANQ RYTTNSAGIV LLKKVAQLAD VPIQSFVVRN
410 420 430 440 450
DSPCGSTIGP KLAAMTGMRT LDLGNPMLSM HSCREMCGSK DFEYAVVLFS
460
SFFQNFANLE EKIIIDE
Length:467
Mass (Da):51,741
Last modified:January 1, 1998 - v1
Checksum:i4A162926DBE3D086
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 772KP → MI in BAA13937 (PubMed:9501991).Curated
Sequence conflicti262 – 2632FC → SG in BAA13937 (PubMed:9501991).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11706.1.
D89276 mRNA. Translation: BAA13937.1.
PIRiT38806.
T43206.
RefSeqiNP_594745.1. NM_001020172.2.

Genome annotation databases

EnsemblFungiiSPAC4F10.02.1; SPAC4F10.02.1:pep; SPAC4F10.02.
GeneIDi2543605.
KEGGispo:SPAC4F10.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11706.1.
D89276 mRNA. Translation: BAA13937.1.
PIRiT38806.
T43206.
RefSeqiNP_594745.1. NM_001020172.2.

3D structure databases

ProteinModelPortaliO36014.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280020. 2 interactions.
MINTiMINT-4672902.

Protein family/group databases

MEROPSiM18.002.

Proteomic databases

MaxQBiO36014.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC4F10.02.1; SPAC4F10.02.1:pep; SPAC4F10.02.
GeneIDi2543605.
KEGGispo:SPAC4F10.02.

Organism-specific databases

EuPathDBiFungiDB:SPAC4F10.02.
PomBaseiSPAC4F10.02. aap1.

Phylogenomic databases

HOGENOMiHOG000253244.
KOiK01267.
OMAiAIHMNRE.
PhylomeDBiO36014.

Enzyme and pathway databases

BRENDAi3.4.11.21. 5613.

Miscellaneous databases

PROiO36014.

Family and domain databases

Gene3Di2.30.250.10. 1 hit.
InterProiIPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]
PfamiPF02127. Peptidase_M18. 1 hit.
[Graphical view]
PRINTSiPR00932. AMINO1PTASE.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-467.
    Strain: PR745.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. "Aspartyl aminopeptidase of Schizosaccharomyces pombe has a molecular chaperone function."
    Lee S., Kim J.S., Yun C.H., Chae H.Z., Kim K.
    BMB Rep. 42:812-816(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION.

Entry informationi

Entry nameiDNPEP_SCHPO
AccessioniPrimary (citable) accession number: O36014
Secondary accession number(s): P78925
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.