ID   DPP4_ARTBC              Reviewed;         778 AA.
AC   D4APE2;
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 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; ORFNames=ARB_06110;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
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: 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:0000269|PubMed:21247460}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; ABSU01000004; EFE35153.1; -; Genomic_DNA.
DR   RefSeq; XP_003015798.1; XM_003015752.1.
DR   AlphaFoldDB; D4APE2; -.
DR   SMR; D4APE2; -.
DR   STRING; 663331.D4APE2; -.
DR   ESTHER; artbc-dpp4; DPP4N_Peptidase_S9.
DR   GlyCosmos; D4APE2; 3 sites, No reported glycans.
DR   GeneID; 9526080; -.
DR   KEGG; abe:ARB_06110; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_2_1; -.
DR   OMA; SLMFAKF; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
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   1: Evidence at protein level;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal; Virulence.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..778
FT                   /note="Probable dipeptidyl peptidase 4"
FT                   /id="PRO_0000397808"
FT   ACT_SITE        616
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        693
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        728
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   778 AA;  88399 MW;  CD21E4B0654123B7 CRC64;
     MKTSQFLSLL LLAGIAQAIV PPREPRPPTG GGNKLLTYKE CVPRATISPR STSLAWINSD
     EDGQYISQSD DGALILQNIV TNTNKTLVAA DKVPKGYYDY WFKPDLSAVL WATNYTKQYR
     HSYFANYFIL DIEKGSLTPL SQDQAGDIQY AQWSPMDNSI AYVRGNDLYI WNNGKTKRIT
     ENGGPDIFNG VPDWVYEEEI FGDRFALWFS PDGEYLAYLR FNETGVPTYT IPYYKNKQKI
     APAYPRELEI RYPKVSAKNP TVQFHLLNIA SSQETTIPVT AFPENDLVIG EVAWLSSGHD
     SVAYRAFNRV QDREKIVSVK VESKESKVIR ERDGTDGWID NLLSMSYIGD VNGKEYYVDI
     SDASGWAHIY LYPVDGGKEI ALTTGEWEVV AILKVDTKKK LIYFTSTKYH STTRHVYSVS
     YDTKVMTPLV NDKEAAYYTA SFSAKGGYYI LSYQGPNVPY QELYSTKDSK KPLKTITSND
     ALLEKLKEYK LPKVSFFEIK LPSGETLNVK QRLPPNFNPH KKYPVLFTPY GGPGAQEVSQ
     AWNSLDFKSY ITSDPELEYV TWTVDNRGTG YKGRKFRSAV AKRLGFLEPQ DQVFAAKELL
     KNRWADKDHI GIWGWSYGGF LTAKTLETDS GVFTFGISTA PVSDFRLYDS MYTERYMKTV
     ELNADGYSET AVHKVDGFKN LKGHYLIQHG TGDDNVHFQN AAVLSNTLMN GGVTADKLTT
     QWFTDSDHGI RYDMDSTYQY KQLAKMVYDQ KQRKPERPPM HQWSKRVLAA LFGERAEE
//