WAPP_COCPS
ID WAPP_COCPS Reviewed; 309 AA.
AC E9D2Q2; C5PDD2; P42783; Q400X6; Q400Y3; Q400Y4; Q400Y5; Q9C2W3; Q9C2W4;
AC Q9C2W5; Q9C2W6;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Wall-associated proteinase;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN ORFNames=CPSG_03850;
OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=443226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Coccidioides posadasii strain Silveira.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-261, AND VARIANTS SER-222; ASP-247
RP AND ILE-249.
RC STRAIN=RMSCC 1036 / AZ1, RMSCC 1045 / AZ2, RMSCC 2128 / TX1, and
RC RMSCC 757 / Silveira;
RX PubMed=9144263; DOI=10.1073/pnas.94.10.5478;
RA Koufopanou V., Burt A., Taylor J.W.;
RT "Concordance of gene genealogies reveals reproductive isolation in the
RT pathogenic fungus Coccidioides immitis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5478-5482(1997).
RN [3]
RP ERRATUM OF PUBMED:9144263.
RA Koufopanou V., Burt A., Taylor J.W.;
RL Proc. Natl. Acad. Sci. U.S.A. 95:8414-8414(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-261, AND VARIANTS SER-222; ASP-247
RP AND ILE-249.
RC STRAIN=IFM 45809 / Silveira, IFM 45810 / Silveira, IFM 45811, IFM 45812,
RC IFM 45813, IFM 45817, IFM 4935, IFM 4945, IFM 50993, IFM 50994, IFM 51112,
RC IFM 54194, IFM 54195, and IFM 54196;
RX PubMed=16699492; DOI=10.3314/jjmm.47.113;
RA Sano A., Miyaji M., Kamei K., Mikami Y., Nishimura K.;
RT "Reexamination of Coccidioides spp. reserved in the Research Center for
RT Pathogenic Fungi and Microbial Toxicoses, Chiba University, based on a
RT multiple gene analysis.";
RL Nippon Ishinkin Gakkai Zasshi 47:113-117(2006).
CC -!- FUNCTION: May participate in wall plasticization and/or intussusception
CC or in cell wall turnover. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
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DR EMBL; GL636490; EFW19467.1; -; Genomic_DNA.
DR EMBL; AJ408857; CAC29123.1; -; Genomic_DNA.
DR EMBL; AJ408858; CAC29124.1; -; Genomic_DNA.
DR EMBL; AJ408859; CAC29125.1; -; Genomic_DNA.
DR EMBL; AJ408860; CAC29126.1; -; Genomic_DNA.
DR EMBL; AB232726; BAE20270.1; -; Genomic_DNA.
DR EMBL; AB232727; BAE20271.1; -; Genomic_DNA.
DR EMBL; AB232728; BAE20272.1; -; Genomic_DNA.
DR EMBL; AB232729; BAE20273.1; -; Genomic_DNA.
DR EMBL; AB232730; BAE20274.1; -; Genomic_DNA.
DR EMBL; AB232731; BAE20275.1; -; Genomic_DNA.
DR EMBL; AB232732; BAE20276.1; -; Genomic_DNA.
DR EMBL; AB232735; BAE20279.1; -; Genomic_DNA.
DR EMBL; AB232738; BAE20282.1; -; Genomic_DNA.
DR EMBL; AB232739; BAE20283.1; -; Genomic_DNA.
DR EMBL; AB232741; BAE20285.1; -; Genomic_DNA.
DR EMBL; AB232742; BAE20286.1; -; Genomic_DNA.
DR EMBL; AB232743; BAE20287.1; -; Genomic_DNA.
DR EMBL; AB232744; BAE20288.1; -; Genomic_DNA.
DR AlphaFoldDB; E9D2Q2; -.
DR SMR; E9D2Q2; -.
DR EnsemblFungi; EFW19467; EFW19467; CPSG_03850.
DR eggNOG; ENOG502SW3V; Eukaryota.
DR HOGENOM; CLU_900182_0_0_1; -.
DR Proteomes; UP000002497; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Cell wall; Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..309
FT /note="Wall-associated proteinase"
FT /id="PRO_0000409490"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 222
FT /note="R -> S (in strain: IFM 45817, IFM 50993, IFM 54196
FT and RMSCC 1036 / AZ1)"
FT /evidence="ECO:0000269|PubMed:16699492,
FT ECO:0000269|PubMed:9144263"
FT VARIANT 247
FT /note="N -> D (in strain: IFM 45812, IFM 4935, IFM 51112
FT and RMSCC 2128 / TX1)"
FT /evidence="ECO:0000269|PubMed:16699492,
FT ECO:0000269|PubMed:9144263"
FT VARIANT 249
FT /note="V -> I (in strain: IFM 45811, IFM 45812, IFM 45813,
FT IFM 45817, IFM 4935, IFM 4945, IFM 50993, IFM 50994, IFM
FT 51112, IFM 54194, IFM 54195, IFM 54196, RMSCC 1036 / AZ1,
FT RMSCC 1045 / AZ2 and RMSCC 2128 / TX1)"
FT /evidence="ECO:0000269|PubMed:16699492,
FT ECO:0000269|PubMed:9144263"
FT CONFLICT 196
FT /note="G -> A (in Ref. 1; EFW19467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34258 MW; ACEE298EF5EE222D CRC64;
MASPVTVLEN PIPKSGQHLL FFLTSKQQLA LEQRPIESSL GYSAYVDHGV SQGVIVNPSS
IAAAMRSSLI TVYGITKPGT DKQYISVISP TYNLIANRQN QPIETTQKAL AACSDNDRNN
WVYYLNLPQG TAQYAIYELN IQDSTSAPTV YSGPTPSGNS NLAAVYFSPN KDRFIIFSNT
DTRHYLYWVN STLQSGNRIA GTGSVMSASP LAATTITNVQ TRSMTIFLYY MDVNTLLNRI
VGKVTDNEVH WYANQVVEGA PPMKVDTLLT GVVVEEKWNC LYYIPDGDTE FRAFNDTIRD
SFFDEPREG