ID A0A8C8M8H2_ONCTS Unreviewed; 467 AA.
AC A0A8C8M8H2;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOTSP00005073305.1};
GN Name=LOC112223485 {ECO:0000313|Ensembl:ENSOTSP00005073305.1};
OS Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=74940 {ECO:0000313|Ensembl:ENSOTSP00005073305.1, ECO:0000313|Proteomes:UP000694402};
RN [1] {ECO:0000313|Ensembl:ENSOTSP00005073305.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOTSP00005073305.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Serine protease with a variety of targets, including
CC extracellular matrix proteins and proteoglycans. Through cleavage of
CC proteoglycans, may release soluble FGF-glycosaminoglycan complexes that
CC promote the range and intensity of FGF signals in the extracellular
CC space. Regulates the availability of insulin-like growth factors (IGFs)
CC by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-
CC beta family members. Consequently, may regulate many physiological
CC processes. Intracellularly, degrades TSC2, leading to the activation of
CC TSC2 downstream targets. {ECO:0000256|ARBA:ARBA00058100}.
CC -!- SUBUNIT: Forms homotrimers. In the presence of substrate, may form
CC higher-order multimers in a PDZ-independent manner.
CC {ECO:0000256|ARBA:ARBA00063274}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR AlphaFoldDB; A0A8C8M8H2; -.
DR Ensembl; ENSOTST00005079439.2; ENSOTSP00005073305.1; ENSOTSG00005034605.2.
DR GeneTree; ENSGT00940000156955; -.
DR Proteomes; UP000694402; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
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; cd06785; cpPDZ_HtrA-like; 1.
DR CDD; cd00104; KAZAL_FS; 1.
DR FunFam; 2.40.10.120:FF:000002; HtrA serine peptidase 3; 1.
DR FunFam; 3.30.60.30:FF:000026; Insulin-like growth factor-binding protein 7; 1.
DR FunFam; 2.30.42.10:FF:000142; Serine protease HTRA1; 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; 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:SF13; SERINE PROTEASE HTRA1; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF13180; PDZ_2; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Growth factor binding {ECO:0000256|ARBA:ARBA00023183};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000694402};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..467
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034600416"
FT DOMAIN 26..100
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 81..144
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 398..464
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 467 AA; 50347 MW; 0C2AE3AA5A6813E8 CRC64;
LTMFWSVICA TFLLAPLVCE ARTKRYVIGC PDRCDKSLCP PIPADCMAGD ILDQCDCCPV
CASEEGEACG GTGRLGDPEC GEGMECSITD GIGVGVCVCK GSDPVCGSDG VSYQNICELK
RVSNRALKLQ QPPVIFIQRG TCGKGQENPD SLRHRYNFIA DVVEKIAPAV VHIELYRKMV
FSKREVAVAS GSGFVVSEDG LIVTNAHVVA NKHRVKVELK SGATFDAKIK DVDEKADIAL
IKIDVPMKLP VLLLGRSADL RPGEFVVAIG SPFSLQNTVT TGIVSTTQRG GKELGLRNSD
MDYIQTDAII NYGNSGGPLV NLDGEVIGIN TLKVTAGISF AIPSDKIRQF LAESHDRQSK
GKLSTSKKYI GVRMMTLTPM LAKELKERQS DFPDVTSGAY VIEVIPKTPA ETGGLQESDV
IITINSQRIT SASDVSSSIK REDTLRMVVR RGNEDIMLTV VPEEIDP
//
