YPS1_SCHPO
ID YPS1_SCHPO Reviewed; 521 AA.
AC O59774;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Aspartic proteinase yapsin-1;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=yps1; ORFNames=SPCC1795.09;
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 [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 [2]
RP FUNCTION, AND SUBCELLULAR LOCATION IN CELL WALL.
RX PubMed=11115118; DOI=10.1046/j.1365-2958.2000.02180.x;
RA Ladds G., Davey J.;
RT "Identification of proteases with shared functions to the proprotein
RT processing protease Krp1 in the fission yeast Schizosaccharomyces pombe.";
RL Mol. Microbiol. 38:839-853(2000).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Cleaves at paired basic residues.
CC {ECO:0000269|PubMed:11115118}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein. Secreted, cell wall.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA18644.1; -; Genomic_DNA.
DR PIR; T41134; T41134.
DR RefSeq; NP_588035.1; NM_001023027.2.
DR AlphaFoldDB; O59774; -.
DR SMR; O59774; -.
DR BioGRID; 275503; 18.
DR STRING; 4896.SPCC1795.09.1; -.
DR MEROPS; A01.056; -.
DR PaxDb; O59774; -.
DR EnsemblFungi; SPCC1795.09.1; SPCC1795.09.1:pep; SPCC1795.09.
DR GeneID; 2538927; -.
DR KEGG; spo:SPCC1795.09; -.
DR PomBase; SPCC1795.09; yps1.
DR VEuPathDB; FungiDB:SPCC1795.09; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_522916_0_0_1; -.
DR InParanoid; O59774; -.
DR OMA; ELRYFLC; -.
DR PhylomeDB; O59774; -.
DR PRO; PR:O59774; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; TAS:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; TAS:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:PomBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47965; PTHR47965; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Cell wall; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Membrane; Protease; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..521
FT /note="Aspartic proteinase yapsin-1"
FT /id="PRO_0000255598"
FT TOPO_DOM 18..500
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 67..409
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 85
FT /evidence="ECO:0000250"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 521 AA; 57623 MW; 21F002CF829175EC CRC64;
MRIWILIFFS FIKLVSSLQY TGNGVLALDF VAKTFPNQEN QLEKRDYTYS PSGITSFPLD
LQSYTYYTTT LSIGRPSISY TVAIDLDMPY TWLTYYNVMA FNPAYLGIVN SGTQWSTDEL
RYFLCKKESD SCYFGNASSS FHFVTSPSTF FIRYDDNITV AGINVQDSLS YSHYQALPDF
QFGITLKEYV PSSMLPYKGV LGLAASTEIN SIDYSDSISS FSPPTFLEQL VKEDILAYPA
FSMYLDNQGN GSLLLGAVDT SKYQGQFVAL KQTKLTHYAV SIYSVQFLNS TFFSNYSIIT
DAYFQTRETY IYLPAELAYS VMDNAGAYLS EGYFALNCDE IDLEAALIFQ FGCNSTIKVP
ISLLVIGQVS NICLLGIRPS TDSEIVLGLL FFRNAYTFYH QSQKMIAIGQ AFYNATSNLS
AIVDQHIPGA LTCSQYPTSV ASTQLVQTSH FTSTSLSAVN ISESVVYSYT SSSSMPSSAI
PSFNISLISQ NAVANAGNSF SPLSAMVIMM MSAVFLGLGI I
