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Protein

Carboxypeptidase sxa2

Gene

sxa2

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

Functioni

Involved in degradation or processing of the mating pheromones. Its loss causes a persistent response to the pheromones. It may be required for stabilization of enzymes that are essential for zygote formation. May degrade the mating pheromone P-factor.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei200 – 2001By similarity
Active sitei434 – 4341By similarity
Active sitei487 – 4871By similarity

GO - Molecular functioni

  • carboxypeptidase activity Source: PomBase
  • serine-type carboxypeptidase activity Source: PomBase

GO - Biological processi

  • conjugation with cellular fusion Source: PomBase
  • negative regulation of conjugation with cellular fusion Source: PomBase
  • negative regulation of induction of conjugation with cellular fusion Source: PomBase
  • negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: PomBase
  • proteolysis involved in cellular protein catabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Protein family/group databases

ESTHERischpo-sxa2. Carboxypeptidase_S10.
MEROPSiS10.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase sxa2 (EC:3.4.16.-)
Gene namesi
Name:sxa2
ORF Names:SPAC1296.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1296.03c.
PomBaseiSPAC1296.03c. sxa2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • extracellular region Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 507485Carboxypeptidase sxa2PRO_0000004288Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence analysis
Glycosylationi45 – 451N-linked (GlcNAc...)Sequence analysis
Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence analysis
Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence analysis
Glycosylationi448 – 4481N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Zymogen

Expressioni

Inductioni

Mating pheromone signaling is required for induction.

Interactioni

Protein-protein interaction databases

BioGridi278197. 8 interactions.
MINTiMINT-4688453.

Structurei

3D structure databases

ProteinModelPortaliP32825.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP32825.
KOiK01288.
OMAiWVEHISK.
OrthoDBiEOG7D867J.
PhylomeDBiP32825.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR033124. Ser_caboxypep_his_AS.
IPR018202. Ser_caboxypep_ser_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 2 hits.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P32825-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLFLKSLF AIIIIELTII HALPTYTVHW KCSIQQANTS SASSNQTVQP
60 70 80 90 100
RQHAAPSSDR IKSLPEFKGS LPELYSGYLE ANSDKSLFYT YAPAVVDSET
110 120 130 140 150
FIVWLQGGPG CAGTLGFFSE NGPIEISQSS PSPSLNPESW TNFANMLWLD
160 170 180 190 200
QPFGTGYSQG QAAYTTTIEE ASSDFVNALK SFYQKFPHLM KKKLYLVGES
210 220 230 240 250
YGSIWSANFA EALLSEPSLN INFMGVGIVS GLTADYETQE QITASIWVEH
260 270 280 290 300
ISKLGYYFNN TSSTISEEFK KRNKECQYDS VLNRLTFPTE QYPIWRPEYN
310 320 330 340 350
FSTSTSLRKR EALDGEDIGN VFNSISGCDL YSLSNFLLYL ENSCVITYDV
360 370 380 390 400
SLDCSFNEYN DPLITYLNRE DVRSSLHATK ASTALTSGEG VFADGCNFDL
410 420 430 440 450
YKKIVSNNVE SVLVEIIPRL TEKYKVSFLA GALDLQILWT GTLLALQNTT
460 470 480 490 500
WNGWQGFTQS PGSLETTNGF TLDERNLAFT LSNSVGHMAP SKDPQMVREW

LENTLLY
Length:507
Mass (Da):56,615
Last modified:October 1, 1993 - v1
Checksum:i0BAF0A46B9E85AC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10199 Genomic DNA. Translation: BAA01047.1.
CU329670 Genomic DNA. Translation: CAB36509.1.
PIRiB42249.
RefSeqiNP_593043.1. NM_001018442.2.

Genome annotation databases

EnsemblFungiiSPAC1296.03c.1; SPAC1296.03c.1:pep; SPAC1296.03c.
GeneIDi2541701.
KEGGispo:SPAC1296.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10199 Genomic DNA. Translation: BAA01047.1.
CU329670 Genomic DNA. Translation: CAB36509.1.
PIRiB42249.
RefSeqiNP_593043.1. NM_001018442.2.

3D structure databases

ProteinModelPortaliP32825.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278197. 8 interactions.
MINTiMINT-4688453.

Protein family/group databases

ESTHERischpo-sxa2. Carboxypeptidase_S10.
MEROPSiS10.012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1296.03c.1; SPAC1296.03c.1:pep; SPAC1296.03c.
GeneIDi2541701.
KEGGispo:SPAC1296.03c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1296.03c.
PomBaseiSPAC1296.03c. sxa2.

Phylogenomic databases

InParanoidiP32825.
KOiK01288.
OMAiWVEHISK.
OrthoDBiEOG7D867J.
PhylomeDBiP32825.

Miscellaneous databases

NextBioi20802794.
PROiP32825.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR033124. Ser_caboxypep_his_AS.
IPR018202. Ser_caboxypep_ser_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 2 hits.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 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.

Entry informationi

Entry nameiSXA2_SCHPO
AccessioniPrimary (citable) accession number: P32825
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: March 16, 2016
This is version 116 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.