SXA1_SCHPO
ID SXA1_SCHPO Reviewed; 533 AA.
AC P32834; Q9P7B9; Q9UU52;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Aspartic proteinase sxa1;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=sxa1; ORFNames=SPAC26A3.01, SPAC2E1P5.06;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 308-481.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
CC -!- FUNCTION: Involved in degradation or processing of the mating
CC pheromones. Its loss may cause a persistent response to the pheromones.
CC It may cleave the mating pheromone M-factor. May be involved in
CC processing of zymogens that are required for zygote formation.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; D10198; BAA01046.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB86349.1; -; Genomic_DNA.
DR EMBL; AB027806; BAA87110.1; -; Genomic_DNA.
DR PIR; A42249; A42249.
DR RefSeq; XP_001713079.1; XM_001713027.2.
DR AlphaFoldDB; P32834; -.
DR SMR; P32834; -.
DR BioGRID; 280544; 2.
DR STRING; 4896.SPAC26A3.01.1; -.
DR MEROPS; A01.A91; -.
DR MaxQB; P32834; -.
DR PaxDb; P32834; -.
DR EnsemblFungi; SPAC26A3.01.1; SPAC26A3.01.1:pep; SPAC26A3.01.
DR PomBase; SPAC26A3.01; sxa1.
DR VEuPathDB; FungiDB:SPAC26A3.01; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_033751_0_0_1; -.
DR InParanoid; P32834; -.
DR OMA; LYFMGGV; -.
DR PhylomeDB; P32834; -.
DR Reactome; R-SPO-2132295; MHC class II antigen presentation.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR PRO; PR:P32834; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; TAS:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; HDA:PomBase.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IMP:PomBase.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..533
FT /note="Aspartic proteinase sxa1"
FT /id="PRO_0000025932"
FT DOMAIN 76..434
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 100
FT /note="T -> I (in Ref. 1; BAA01046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 56853 MW; 5B98640743D744EB CRC64;
MKASFFVFAI SALQALQASV ASAYSEVPGK RSVVLNLQHS QYDHVARKLE RTKVLNKRDS
SGYPVLDLEY TDAGGYFANL TLGSNERVYS LTLDTGSPYT WVTAKNITAL SASEIWSDTD
GVDAGRSTSD IRTNACTNYT CFDYSSTTAR RTNSSTIGFL ASYGDNTTVL GYNMVDNAYF
AGLTLPGFEF GLATREYDSS QISVTPGIIG LSVAMTITGI SSDDKVVAFT PPTIVDQLVS
ANVIDTPAFG IYLNEDVGEL IFGGYDKAKI NGSVHWVNIS SSDDSTFYSV NLESITVTNS
TSSNNVQSSK RSSKDIEVNT TVTLDTGTVY IYLPEDTVES IADQYQGIVS EYGYVVIYCD
SFSDSDYISF NFGSDADFHV SVNDLVIYRQ ESTSGDICYL ALFEGDTSSY LLGQYFLQYV
YSIYDWDAQK IGLAALNSNA TSTANHQILN INSALRSVTS GQSVSATPTV SMSIAATSFG
SSLVLTASAS PSSTSVDGSS SSDSSEASGA ASVGVSISAI VLCASTLISL LFA
