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Protein

Aspartic proteinase sxa1

Gene

sxa1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Involved in degradation or processing of the mating pheromones. Its loss may cause a persistent response to the pheromones. It may cleave the mating pheromone M-factor. May be involved in processing of zymogens that are required for zygote formation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei94 – 941PROSITE-ProRule annotation
Active sitei325 – 3251PROSITE-ProRule annotation

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: UniProtKB-KW
  • peptidase activity Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.A91.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartic proteinase sxa1 (EC:3.4.23.-)
Gene namesi
Name:sxa1
ORF Names:SPAC26A3.01, SPAC2E1P5.06
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC26A3.01.
PomBaseiSPAC26A3.01. sxa1.

Subcellular locationi

GO - Cellular componenti

  • anchored component of external side of plasma membrane Source: PomBase
  • cell surface Source: PomBase
  • endoplasmic reticulum Source: PomBase
  • plasma membrane Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 533510Aspartic proteinase sxa1PRO_0000025932Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence analysis
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence analysis
Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence analysis
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence analysis
Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence analysis
Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence analysis
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence analysis
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence analysis
Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP32834.

Interactioni

Protein-protein interaction databases

MINTiMINT-4688466.

Structurei

3D structure databases

ProteinModelPortaliP32834.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 434359Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP32834.
OMAiRREITIN.
OrthoDBiEOG71VT34.
PhylomeDBiP32834.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 3 hits.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 1 hit.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P32834-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKASFFVFAI SALQALQASV ASAYSEVPGK RSVVLNLQHS QYDHVARKLE
60 70 80 90 100
RTKVLNKRDS SGYPVLDLEY TDAGGYFANL TLGSNERVYS LTLDTGSPYT
110 120 130 140 150
WVTAKNITAL SASEIWSDTD GVDAGRSTSD IRTNACTNYT CFDYSSTTAR
160 170 180 190 200
RTNSSTIGFL ASYGDNTTVL GYNMVDNAYF AGLTLPGFEF GLATREYDSS
210 220 230 240 250
QISVTPGIIG LSVAMTITGI SSDDKVVAFT PPTIVDQLVS ANVIDTPAFG
260 270 280 290 300
IYLNEDVGEL IFGGYDKAKI NGSVHWVNIS SSDDSTFYSV NLESITVTNS
310 320 330 340 350
TSSNNVQSSK RSSKDIEVNT TVTLDTGTVY IYLPEDTVES IADQYQGIVS
360 370 380 390 400
EYGYVVIYCD SFSDSDYISF NFGSDADFHV SVNDLVIYRQ ESTSGDICYL
410 420 430 440 450
ALFEGDTSSY LLGQYFLQYV YSIYDWDAQK IGLAALNSNA TSTANHQILN
460 470 480 490 500
INSALRSVTS GQSVSATPTV SMSIAATSFG SSLVLTASAS PSSTSVDGSS
510 520 530
SSDSSEASGA ASVGVSISAI VLCASTLISL LFA
Length:533
Mass (Da):56,853
Last modified:March 5, 2002 - v2
Checksum:i5B98640743D744EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001T → I in BAA01046 (PubMed:1549128).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10198 Genomic DNA. Translation: BAA01046.1.
CU329670 Genomic DNA. Translation: CAB86349.1.
AB027806 Genomic DNA. Translation: BAA87110.1.
PIRiA42249.
RefSeqiXP_001713079.1. XM_001713027.2.

Genome annotation databases

EnsemblFungiiSPAC26A3.01.1; SPAC26A3.01.1:pep; SPAC26A3.01.
GeneIDi3361468.
KEGGispo:SPAC26A3.01.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10198 Genomic DNA. Translation: BAA01046.1.
CU329670 Genomic DNA. Translation: CAB86349.1.
AB027806 Genomic DNA. Translation: BAA87110.1.
PIRiA42249.
RefSeqiXP_001713079.1. XM_001713027.2.

3D structure databases

ProteinModelPortaliP32834.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4688466.

Protein family/group databases

MEROPSiA01.A91.

Proteomic databases

MaxQBiP32834.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC26A3.01.1; SPAC26A3.01.1:pep; SPAC26A3.01.
GeneIDi3361468.
KEGGispo:SPAC26A3.01.

Organism-specific databases

EuPathDBiFungiDB:SPAC26A3.01.
PomBaseiSPAC26A3.01. sxa1.

Phylogenomic databases

InParanoidiP32834.
OMAiRREITIN.
OrthoDBiEOG71VT34.
PhylomeDBiP32834.

Miscellaneous databases

PROiP32834.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 3 hits.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 1 hit.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Schizosaccharomyces pombe sxa1+ and sxa2+ encode putative proteases involved in the mating response."
    Imai Y., Yamamoto M.
    Mol. Cell. Biol. 12:1827-1834(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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.
  3. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 308-481.
    Strain: ATCC 38364 / 968.

Entry informationi

Entry nameiSXA1_SCHPO
AccessioniPrimary (citable) accession number: P32834
Secondary accession number(s): Q9P7B9, Q9UU52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: March 5, 2002
Last modified: June 8, 2016
This is version 122 of the entry and version 2 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.