SPCA_TRIRU
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 03-AUG-2022, entry version 65.
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}.
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DR EMBL; AY497023; AAS76667.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5J6J1; -.
DR SMR; Q5J6J1; -.
DR ESTHER; triru-SPCA; Carboxypeptidase_S10.
DR MEROPS; S10.016; -.
DR PRIDE; Q5J6J1; -.
DR VEuPathDB; FungiDB:TERG_04022; -.
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..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
