ID CTSD_TRIVH Reviewed; 509 AA.
AC D4D8U6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Probable aspartic-type endopeptidase CTSD;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=CTSD; ORFNames=TRV_03534;
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- FUNCTION: Probable GPI-anchored aspartic-type endopeptidase which
CC contributes to virulence. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; ACYE01000183; EFE41705.1; -; Genomic_DNA.
DR RefSeq; XP_003022323.1; XM_003022277.1.
DR AlphaFoldDB; D4D8U6; -.
DR SMR; D4D8U6; -.
DR MEROPS; A01.077; -.
DR GlyCosmos; D4D8U6; 3 sites, No reported glycans.
DR GeneID; 9580870; -.
DR KEGG; tve:TRV_03534; -.
DR HOGENOM; CLU_013253_10_1_1; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Protease; Signal; Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..485
FT /note="Probable aspartic-type endopeptidase CTSD"
FT /id="PRO_0000397700"
FT PROPEP 486..509
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000397701"
FT DOMAIN 102..408
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 451..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT LIPID 485
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 509 AA; 54631 MW; 2EA12E9D2B261853 CRC64;
MQFLWLCLLS AVTLQFTGTL AFYPIKLPDF TKGLVSNHGS IDRRFFTFPG LYKHAHTGST
TLNIRRGPSN YRRDNNYPAQ IASPPTAPNT LGINNDGYDF SYFSEVKVGS EGQKMWMLID
TGASGTWVFG SDCTSKACGR HNTFGKEDSK TIKVTDEKWG VTYGTGKVSG VIVNDTMSFA
GFELVTPFGS ASTASDDFLN YPMDGILGIG PQDPNAKTPT VVQLLMQQKL LKSNVIGINL
QRASEGATDG QITFGDIDKS KFSGELIYSN VVPDGYQWEI AMDDLIMDGK SLNLKGRTGI
IDTGTSFLIL PPADADLIHS MIPQANKGSG FYTLPCSTKV DIKLSIGGVE YTIQPDDYVG
NETATKGTCN SLIVGRQILG PKQWLVGDVF LKNVYSVFDF DKNRVGLAAR KYAGTKNPPS
STPSPGMFLL HAILCPKTIS VLMLHIDPTS NKAPSGGSPG LPAESGSDST TNGEATNGAT
SSPNSSSSVL TPTWLTLAVF FAIGSSLWS
//
