ID A0A9J8CAN8_CYPCA Unreviewed; 446 AA.
AC A0A9J8CAN8;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=HtrA serine peptidase 4 {ECO:0000313|Ensembl:ENSCCRP00000163231.1};
OS Cyprinus carpio carpio.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000163231.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000163231.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000163231.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR AlphaFoldDB; A0A9J8CAN8; -.
DR Ensembl; ENSCCRT00000198848.1; ENSCCRP00000163231.1; ENSCCRG00000059033.1.
DR GeneTree; ENSGT00940000160760; -.
DR Proteomes; UP001108240; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:TreeGrafter.
DR GO; GO:0012501; P:programmed cell death; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00104; KAZAL_FS; 1.
DR FunFam; 2.40.10.120:FF:000002; HtrA serine peptidase 3; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 4.10.40.20; -; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF105; SERINE PROTEASE HTRA4; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00121; IB; 1.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP001108240};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..446
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039952336"
FT DOMAIN 22..92
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 88..136
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 378..433
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 446 AA; 48609 MW; DE69BA409B9DFDB1 CRC64;
MWKLLACVLM ASVLQARDLR TRQTICPNVC DLSRCSSALE SCYFGVVKDR CDCCTVCAAR
EGEYCGERGH AVCGQGMTCE YSTSAIGTCV CDARDPVCGS DGRTYPSICR LKAENRRAEM
SGIPAVIFIQ RGPCETGSRN PNSMRYKFNF IADVVDKIAP AVVHLELFTR LPSSNQDIPV
SSGSGFIVSE DGWIVTNAHV LSNKQHIKVE LKNGMFYDAT IKDVDQKLDI ALIKIDSETP
LPVLLLGRSS DLRPGEFVVA VGSPFSLQNT VTTGIISTTH RGGHELGLQN SDMDYIQTDA
IINYGNSGGP LVNLDGDVIG INTLKVTPGI SFAIPSDRIR QFLADSYDRQ RKGLQISYEL
LIRELKEKES NFPDVSSGVY VYEVIPGTAA FSAGLLNQDV IISINGQSVH STEDVSQAVQ
SDKVLSLVVR RANEEITLTV VPYEVD
//