ID SCPB_TRIRU Reviewed; 662 AA. AC Q5J6J2; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 13-SEP-2023, entry version 65. DE RecName: Full=Carboxypeptidase S1 homolog B; DE EC=3.4.16.6; DE AltName: Full=Serine carboxypeptidase B; DE Short=SPCB; DE Flags: Precursor; GN Name=SCPB; 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). RN [2] RP INDUCTION. RX PubMed=19098130; DOI=10.1128/ec.00208-08; RA Zaugg C., Monod M., Weber J., Harshman K., Pradervand S., Thomas J., RA Bueno M., Giddey K., Staib P.; RT "Gene expression profiling in the human pathogenic dermatophyte RT Trichophyton rubrum during growth on proteins."; RL Eukaryot. Cell 8:241-250(2009). CC -!- FUNCTION: Extracellular serine carboxypeptidase that contributes to CC pathogenicity. {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 8.0. {ECO:0000269|PubMed:18222721}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI- CC anchor {ECO:0000305}. CC -!- INDUCTION: Expression is strongly increased during growth on protein- CC rich medium. {ECO:0000269|PubMed:19098130}. 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; AY497022; AAS76666.1; -; Genomic_DNA. DR AlphaFoldDB; Q5J6J2; -. DR SMR; Q5J6J2; -. DR ESTHER; triru-SCPB; Carboxypeptidase_S10. DR MEROPS; S10.016; -. DR GlyCosmos; Q5J6J2; 14 sites, No reported glycans. DR VEuPathDB; FungiDB:TERG_08557; -. DR OMA; FQEFPGY; -. 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..21 FT /evidence="ECO:0000255" FT CHAIN 22..633 FT /note="Carboxypeptidase S1 homolog B" FT /id="PRO_0000384123" FT PROPEP 634..662 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000384124" FT ACT_SITE 240 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 459 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 517 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT BINDING 462 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 518 FT /ligand="substrate" FT /evidence="ECO:0000250" FT LIPID 633 FT /note="GPI-anchor amidated glycine" FT /evidence="ECO:0000255" FT CARBOHYD 130 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 163 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 186 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 200 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 262 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 302 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 311 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 350 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 475 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 493 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 506 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 598 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 612 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 51..123 FT /evidence="ECO:0000250" FT DISULFID 328..364 FT /evidence="ECO:0000250" FT DISULFID 335..357 FT /evidence="ECO:0000250" SQ SEQUENCE 662 AA; 73012 MW; B47308AB5BB82CCB CRC64; MVSFCGVAAC LLTVAGHLAQ AQFPPKPEGV TVLESKFGSG ARITYKEPGL CETTEGVKSY AGYVHLPPGT LRDFGVEQDY PINTFFWFFE ARKDPENAPL GIWMNGGPGS SSMFGMMTEN GPCFVNADSN STRLNPHSWN NEVNMLYIDQ PVQVGLSYDT LANFTRNLVT DEITKLKPGE PIPEQNATFL VGTYASRNMN TTAHGTRHAA MALWHFAQVW FQEFPGYHPR NNKISIATES YGGRYGPAFT AFFEEQNQKI KNGTWKGHEG TMHVLHLDTL MIVNGCIDRL VQWPAYPQMA YNNTYSIEAV NASIHAGMLD ALYRDGGCRD KINHCRSLSS VFDPENLGIN STVNDVCKDA ETFCSNDVRD PYLKFSGRNY YDIGQLDPSP FPAPFYMAWL NQPHVQAALG VPLNWTQSND VVSTAFRAIG DYPRPGWLEN LAYLLENGIK VSLVYGDRDY ACNWFGGELS SLGINYTDTH EFHNAGYAGI QINSSYIGGQ VRQYGNLSFA RVYEAGHEVP SYQPETALQI FHRSLFNKDI ATGTKDTSSR MDGGKFYGTS GPADSFGFKN KPPPQHVHFC HILDTSTCTK EQIQSVENGT AAVRSWIIVD SNSTSLFPEV VGSGEPTPTP MPGGATTLSA HGFLYGVTLW AVIVVAVIEL AM //