SXA2_SCHPO
ID SXA2_SCHPO Reviewed; 507 AA.
AC P32825;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Carboxypeptidase sxa2;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=sxa2; ORFNames=SPAC1296.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1549128; DOI=10.1128/mcb.12.4.1827-1834.1992;
RA Imai Y., Yamamoto M.;
RT "Schizosaccharomyces pombe sxa1+ and sxa2+ encode putative proteases
RT involved in the mating response.";
RL Mol. Cell. Biol. 12:1827-1834(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Involved in degradation or processing of the mating
CC pheromones. Its loss causes a persistent response to the pheromones. It
CC may be required for stabilization of enzymes that are essential for
CC zygote formation. May degrade the mating pheromone P-factor.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: Mating pheromone signaling is required for induction.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; D10199; BAA01047.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB36509.1; -; Genomic_DNA.
DR PIR; B42249; B42249.
DR RefSeq; NP_593043.1; NM_001018442.2.
DR AlphaFoldDB; P32825; -.
DR SMR; P32825; -.
DR BioGRID; 278197; 8.
DR STRING; 4896.SPAC1296.03c.1; -.
DR ESTHER; schpo-sxa2; Carboxypeptidase_S10.
DR MEROPS; S10.012; -.
DR PaxDb; P32825; -.
DR EnsemblFungi; SPAC1296.03c.1; SPAC1296.03c.1:pep; SPAC1296.03c.
DR GeneID; 2541701; -.
DR KEGG; spo:SPAC1296.03c; -.
DR PomBase; SPAC1296.03c; sxa2.
DR VEuPathDB; FungiDB:SPAC1296.03c; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_537653_0_0_1; -.
DR InParanoid; P32825; -.
DR OMA; VPNAWSW; -.
DR PhylomeDB; P32825; -.
DR PRO; PR:P32825; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005576; C:extracellular region; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004180; F:carboxypeptidase activity; IDA:PomBase.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IDA:PomBase.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IDA:PomBase.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:PomBase.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..507
FT /note="Carboxypeptidase sxa2"
FT /id="PRO_0000004288"
FT REGION 41..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /evidence="ECO:0000250"
FT ACT_SITE 434
FT /evidence="ECO:0000250"
FT ACT_SITE 487
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 507 AA; 56615 MW; 0BAF0A46B9E85AC5 CRC64;
MLSLFLKSLF AIIIIELTII HALPTYTVHW KCSIQQANTS SASSNQTVQP RQHAAPSSDR
IKSLPEFKGS LPELYSGYLE ANSDKSLFYT YAPAVVDSET FIVWLQGGPG CAGTLGFFSE
NGPIEISQSS PSPSLNPESW TNFANMLWLD QPFGTGYSQG QAAYTTTIEE ASSDFVNALK
SFYQKFPHLM KKKLYLVGES YGSIWSANFA EALLSEPSLN INFMGVGIVS GLTADYETQE
QITASIWVEH ISKLGYYFNN TSSTISEEFK KRNKECQYDS VLNRLTFPTE QYPIWRPEYN
FSTSTSLRKR EALDGEDIGN VFNSISGCDL YSLSNFLLYL ENSCVITYDV SLDCSFNEYN
DPLITYLNRE DVRSSLHATK ASTALTSGEG VFADGCNFDL YKKIVSNNVE SVLVEIIPRL
TEKYKVSFLA GALDLQILWT GTLLALQNTT WNGWQGFTQS PGSLETTNGF TLDERNLAFT
LSNSVGHMAP SKDPQMVREW LENTLLY
