ID   DPP4_TRIEQ              Reviewed;         775 AA.
AC   A7UKV8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Dipeptidyl peptidase 4;
DE            EC=3.4.14.5;
DE   AltName: Full=Dipeptidyl peptidase IV;
DE            Short=DPP IV;
DE            Short=DppIV;
DE   Flags: Precursor;
GN   Name=DPP4;
OS   Trichophyton equinum (Horse ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=63418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Brown J.T., Preuett B.L., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between T. tonsurans and T.
RT   equinum.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal
CC       dipeptides sequentially from polypeptides having unsubstituted N-
CC       termini provided that the penultimate residue is proline. Contributes
CC       to pathogenicity (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC         polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC         Pro nor hydroxyproline.; EC=3.4.14.5; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10084};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; EU076573; ABU50383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7UKV8; -.
DR   SMR; A7UKV8; -.
DR   ESTHER; artbc-dpp4; DPP4N_Peptidase_S9.
DR   MEROPS; S09.008; -.
DR   GlyCosmos; A7UKV8; 4 sites, No reported glycans.
DR   VEuPathDB; FungiDB:TEQG_07662; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF162; DIPEPTIDYL PEPTIDASE 4-RELATED; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Virulence.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..775
FT                   /note="Dipeptidyl peptidase 4"
FT                   /id="PRO_0000384088"
FT   ACT_SITE        613
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        690
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        725
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   775 AA;  88010 MW;  753C4CBD7E8D6079 CRC64;
     MKFLSLLLLA GIAQAIVPPR EPRPPTGGGN KLLTYKECVP RATISPRSTS LAWINSDEDG
     QYISQSDDGA LILQNIVTNT NKTLVAADKV PKGYYDYWFK PDLSAVLWAT NYTKQYRHSY
     FANYFILDIE KGSLTPLAQD QAGDIQYAQW SPVDNSIAYV RGNDLYIWNN GTTKRTTENG
     GPDIFNGVPD WVYEEEIFGD RFALWFSPDG EYLAYLRFNE TGVPTYTIPY YKNKQKIAPA
     YPRELEIRYP KVSAKNPTVQ FHLLNIASSQ ESTIPVTAFP ENDLVIGEVA WLSSGHDSVA
     YRAFNRVQDR EKIVSIKVES KESKVIRERD GTDGWIDNLL SMSYIGDVNG KEYYVDISDA
     SGWAHIYLYP VDGGKEIALT KGEWEVVAIL KVDTKKKLIY FTSTKYHSTT RHVYSVSYDT
     NVMTPLVNDK EAAYYTASFS AKGGYYILSY QGPNVPYQEL YSTKDSKKPL KTITSNDALL
     EKLKEYKLPK VSFFEIKLPS GETLNVKQRL PPNFNPHKKY PVLFTPYGGP GAQEVSQAWN
     SLDFKSYITS DPELEYVTWT VDNRGTGYKG RKFRSAVAKR LGFLEAQDQV FAAKELLKNR
     WADKDHIGIW GWSYGGFLTA KTLETDSGVF TFGISTAPVS DFRLYDSMYT ERYMKTVELN
     ADGYSETAVH KVDGFKNLKG HYLIQHGTGD DNVHFQNAAV LSNTLMNGGV TADKLTTQWF
     TDSDHGIRYD MDSTYQYKQL AKMVYDQKQR RPERPPMHQW SKRVLAALFG ERAEE
//