ID T1IR55_STRMM Unreviewed; 448 AA.
AC T1IR55;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Dipeptidyl peptidase 1 {ECO:0000256|ARBA:ARBA00014709};
DE EC=3.4.14.1 {ECO:0000256|ARBA:ARBA00012059};
DE AltName: Full=Cathepsin C {ECO:0000256|ARBA:ARBA00029779};
DE AltName: Full=Cathepsin J {ECO:0000256|ARBA:ARBA00029762};
DE AltName: Full=Dipeptidyl peptidase I {ECO:0000256|ARBA:ARBA00032961};
DE AltName: Full=Dipeptidyl transferase {ECO:0000256|ARBA:ARBA00030778};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR003539-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR003539-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except
CC when Xaa is Arg or Lys, or Yaa or Zaa is Pro.; EC=3.4.14.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000738};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00001923};
CC -!- SUBUNIT: Tetramer of heterotrimers consisting of exclusion domain,
CC heavy- and light chains. {ECO:0000256|ARBA:ARBA00011610}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; AFFK01018464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1IR55; -.
DR STRING; 126957.T1IR55; -.
DR EnsemblMetazoa; SMAR003539-RA; SMAR003539-PA; SMAR003539.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_048219_0_0_1; -.
DR OMA; HWDWRNV; -.
DR OrthoDB; 5475703at2759; -.
DR PhylomeDB; T1IR55; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.80; Cathepsin C, exclusion domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR014882; CathepsinC_exc.
DR InterPro; IPR036496; CathepsinC_exc_dom_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR PANTHER; PTHR12411:SF942; DIPEPTIDYL PEPTIDASE 1; 1.
DR Pfam; PF08773; CathepsinC_exc; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF75001; Dipeptidyl peptidase I (cathepsin C), exclusion domain; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..448
FT /note="Dipeptidyl peptidase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018600511"
FT DOMAIN 221..445
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 448 AA; 50587 MW; B0B3812C06B6273A CRC64;
MAAFFCLLAG LIVVVPSSVA DTPANCTYDD IQGNWIFYET ERSRSTNENC DKIGSVVYKT
QLKLKFPNLV VDDLGNIGFW TIIYNQGFEV VINQRKYFAF SLFKQSGQNA TNYCDQTFPG
WSHDILVRNW ACFMGKKVGL WPEKYISLSK SQVNGMYRTN KGFINEINNK QTLWTAKVYS
HFEKLSHEEL LSMRGGRKSK IIHLPKSSPI SREIEKLTSN LPLVFDWRNV SGVNYISPIR
NQGTCGSCYS FASMAMLEAR LRIYTNNTNQ VIFAPQDVVS CSEYSQGCEG GFPYLIAGKY
AQDFGVIPEN CYPYSGRDEK CSGKKCTRTY VSKYSYVGGF YGGCNEALMR YAIVHNGPVA
VGFQVYPDFM QYSSGIYHHS GVLEKFNPFE LTNHAVLVVG YGEENGVLFW IVKNSWGTGW
GENGFFRIRR GNDECSIESL GMEAVPIP
//
