SCPB_TRIRU
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 03-AUG-2022, entry version 61.
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}.
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DR EMBL; AY497022; AAS76666.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5J6J2; -.
DR SMR; Q5J6J2; -.
DR ESTHER; triru-SCPB; Carboxypeptidase_S10.
DR MEROPS; S10.016; -.
DR VEuPathDB; FungiDB:TERG_08557; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 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
