Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aspartic proteinase yapsin-1

Gene

yps1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Cleaves at paired basic residues.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei85 – 851By similarity

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: PomBase

GO - Biological processi

  • dibasic protein processing Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.056.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartic proteinase yapsin-1 (EC:3.4.23.-)
Gene namesi
Name:yps1
ORF Names:SPCC1795.09
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1795.09.
PomBaseiSPCC1795.09. yps1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 500483ExtracellularSequence analysisAdd
BLAST
Transmembranei501 – 52121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • anchored component of external side of plasma membrane Source: PomBase
  • cell surface Source: PomBase
  • cell wall Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: PomBase
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • extracellular region Source: UniProtKB-KW
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Endoplasmic reticulum, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 521504Aspartic proteinase yapsin-1PRO_0000255598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence analysis
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence analysis
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence analysis
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence analysis
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence analysis
Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence analysis
Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence analysis
Glycosylationi418 – 4181N-linked (GlcNAc...)Sequence analysis
Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence analysis
Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

BioGridi275503. 14 interactions.
MINTiMINT-4676089.

Structurei

3D structure databases

ProteinModelPortaliO59774.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 409343Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi471 – 4744Poly-Ser

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiO59774.
OrthoDBiEOG71P2M6.
PhylomeDBiO59774.

Family and domain databases

Gene3Di2.40.70.10. 3 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 3 hits.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O59774-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIWILIFFS FIKLVSSLQY TGNGVLALDF VAKTFPNQEN QLEKRDYTYS
60 70 80 90 100
PSGITSFPLD LQSYTYYTTT LSIGRPSISY TVAIDLDMPY TWLTYYNVMA
110 120 130 140 150
FNPAYLGIVN SGTQWSTDEL RYFLCKKESD SCYFGNASSS FHFVTSPSTF
160 170 180 190 200
FIRYDDNITV AGINVQDSLS YSHYQALPDF QFGITLKEYV PSSMLPYKGV
210 220 230 240 250
LGLAASTEIN SIDYSDSISS FSPPTFLEQL VKEDILAYPA FSMYLDNQGN
260 270 280 290 300
GSLLLGAVDT SKYQGQFVAL KQTKLTHYAV SIYSVQFLNS TFFSNYSIIT
310 320 330 340 350
DAYFQTRETY IYLPAELAYS VMDNAGAYLS EGYFALNCDE IDLEAALIFQ
360 370 380 390 400
FGCNSTIKVP ISLLVIGQVS NICLLGIRPS TDSEIVLGLL FFRNAYTFYH
410 420 430 440 450
QSQKMIAIGQ AFYNATSNLS AIVDQHIPGA LTCSQYPTSV ASTQLVQTSH
460 470 480 490 500
FTSTSLSAVN ISESVVYSYT SSSSMPSSAI PSFNISLISQ NAVANAGNSF
510 520
SPLSAMVIMM MSAVFLGLGI I
Length:521
Mass (Da):57,623
Last modified:August 1, 1998 - v1
Checksum:i21F002CF829175EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA18644.1.
PIRiT41134.
RefSeqiNP_588035.1. NM_001023027.2.

Genome annotation databases

EnsemblFungiiSPCC1795.09.1; SPCC1795.09.1:pep; SPCC1795.09.
GeneIDi2538927.
KEGGispo:SPCC1795.09.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA18644.1.
PIRiT41134.
RefSeqiNP_588035.1. NM_001023027.2.

3D structure databases

ProteinModelPortaliO59774.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275503. 14 interactions.
MINTiMINT-4676089.

Protein family/group databases

MEROPSiA01.056.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1795.09.1; SPCC1795.09.1:pep; SPCC1795.09.
GeneIDi2538927.
KEGGispo:SPCC1795.09.

Organism-specific databases

EuPathDBiFungiDB:SPCC1795.09.
PomBaseiSPCC1795.09. yps1.

Phylogenomic databases

InParanoidiO59774.
OrthoDBiEOG71P2M6.
PhylomeDBiO59774.

Miscellaneous databases

PROiO59774.

Family and domain databases

Gene3Di2.40.70.10. 3 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 3 hits.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
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 proteases with shared functions to the proprotein processing protease Krp1 in the fission yeast Schizosaccharomyces pombe."
    Ladds G., Davey J.
    Mol. Microbiol. 38:839-853(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION IN CELL WALL.
  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].

Entry informationi

Entry nameiYPS1_SCHPO
AccessioniPrimary (citable) accession number: O59774
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: August 1, 1998
Last modified: June 8, 2016
This is version 96 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.