ID SPCA_TRIRU Reviewed; 652 AA. AC Q5J6J1; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 13-SEP-2023, entry version 69. DE RecName: Full=Carboxypeptidase S1 homolog A; DE EC=3.4.16.6; DE AltName: Full=Serine carboxypeptidase A; DE Short=SPCA; DE Flags: Precursor; GN Name=SCPA; OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton. OX NCBI_TaxID=5551; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=18222721; DOI=10.1016/j.ijmm.2007.11.005; RA Zaugg C., Jousson O., Lechenne B., Staib P., Monod M.; RT "Trichophyton rubrum secreted and membrane-associated carboxypeptidases."; RL Int. J. Med. Microbiol. 298:669-682(2008). CC -!- FUNCTION: Extracellular serine carboxypeptidase that contributes to CC pathogenicity. {ECO:0000250, ECO:0000269|PubMed:18222721}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential release of a C-terminal arginine or lysine CC residue.; EC=3.4.16.6; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 4.5. {ECO:0000269|PubMed:18222721}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI- CC anchor {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY497023; AAS76667.1; -; Genomic_DNA. DR AlphaFoldDB; Q5J6J1; -. DR SMR; Q5J6J1; -. DR ESTHER; triru-SPCA; Carboxypeptidase_S10. DR MEROPS; S10.016; -. DR GlyCosmos; Q5J6J1; 13 sites, No reported glycans. DR VEuPathDB; FungiDB:TERG_04022; -. DR OrthoDB; 1647009at2759; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR001563; Peptidase_S10. DR InterPro; IPR018202; Ser_caboxypep_ser_AS. DR PANTHER; PTHR11802:SF189; CARBOXYPEPTIDASE; 1. DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1. DR Pfam; PF00450; Peptidase_S10; 1. DR PRINTS; PR00724; CRBOXYPTASEC. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1. PE 1: Evidence at protein level; KW Carboxypeptidase; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; KW Hydrolase; Lipoprotein; Membrane; Protease; Signal; Virulence. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..629 FT /note="Carboxypeptidase S1 homolog A" FT /id="PRO_0000384117" FT PROPEP 630..652 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000384118" FT REGION 608..627 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 611..627 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 238 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 458 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 516 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT BINDING 461 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 517 FT /ligand="substrate" FT /evidence="ECO:0000250" FT LIPID 629 FT /note="GPI-anchor amidated glycine" FT /evidence="ECO:0000255" FT CARBOHYD 77 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 132 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 161 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 168 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 184 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 202 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 299 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 347 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 410 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 474 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 492 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 505 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 50..121 FT /evidence="ECO:0000250" FT DISULFID 325..361 FT /evidence="ECO:0000250" FT DISULFID 332..354 FT /evidence="ECO:0000250" SQ SEQUENCE 652 AA; 71825 MW; B5D3E435BAC0A9C5 CRC64; MRFAASIAVA LPVIHAASAQ GFPPPVKGVT VVKSKFDENV KITYKENDIC ETTQGVRSFT GHVHLPPDND DFGVYRNYSI NTFFWFFEAR EDPKNAPLSI WLNGGPGSSS MIGLFQENGP CWVNEDSKST TNNSFSWNNK VNMLYIDQPN QVGFSYDVPT NITYSTINDT ISVADFSNGV PAQNLSTLVG TGSSQNPWAT ANNTVNAARS IWHFAQVWFQ EFPEHKPNNN KISIWTESYG GRYGPSFASY FQEQNEKIKN HTITEEGEMH ILNLDTLGII NGCIDLMFQA ESYAEFPYNN TYGIKAYTKE KRDAILHDIH RPDGCFDKVT KCREAAKEGD PHFYSNNATV NTICADANSA CDKYLMDPFQ ETNLGYYDIA HPLQDPFPPP FYKGFLSQSS VLSDMGSPVN FSQYAQAVGK SFHGVGDYAR PDVRGFTGDI AYLLESGVKV ALVYGDRDYI CNWFGGEQVS LGLNYTGTQD FHRAKYADVK VNSSYVGGVV RQHGNFSFTR VFEAGHEVPG YQPETALKIF ERIMFNKDIS TGEIDIAQKP DYGTTGTEST FHIKNDIPPS PEPTCYLLSA DGTCTPEQLN AIKDGTAVVE NYIIKSPAAS KGNPPPTTTS SPTAAPTAGS AMLKAPVAML AISALTVLAF FL //