ID A0A2K6RJ17_RHIRO Unreviewed; 453 AA.
AC A0A2K6RJ17;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 38.
DE RecName: Full=Serine protease HTRA3 {ECO:0000256|ARBA:ARBA00068962};
DE AltName: Full=High-temperature requirement factor A3 {ECO:0000256|ARBA:ARBA00078689};
DE AltName: Full=Pregnancy-related serine protease {ECO:0000256|ARBA:ARBA00076911};
GN Name=HTRA3 {ECO:0000313|Ensembl:ENSRROP00000041034.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000041034.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000041034.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSRROP00000041034.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Serine protease that cleaves beta-casein/CSN2 as well as
CC several extracellular matrix (ECM) proteoglycans such as decorin/DCN,
CC biglycan/BGN and fibronectin/FN1. Inhibits signaling mediated by TGF-
CC beta family proteins possibly indirectly by degradation of these ECM
CC proteoglycans. May act as a tumor suppressor. Negatively regulates, in
CC vitro, trophoblast invasion during placental development and may be
CC involved in the development of the placenta in vivo. May also have a
CC role in ovarian development, granulosa cell differentiation and
CC luteinization. {ECO:0000256|ARBA:ARBA00059963}.
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 RefSeq; XP_010382720.1; XM_010384418.2.
DR AlphaFoldDB; A0A2K6RJ17; -.
DR STRING; 61622.ENSRROP00000041034; -.
DR Ensembl; ENSRROT00000065527.1; ENSRROP00000041034.1; ENSRROG00000043722.1.
DR GeneID; 104678970; -.
DR KEGG; rro:104678970; -.
DR CTD; 94031; -.
DR GeneTree; ENSGT00940000159570; -.
DR OMA; YDAKAYK; -.
DR OrthoDB; 4217619at2759; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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; 4.10.40.20:FF:000004; HtrA serine peptidase 3; 1.
DR FunFam; 2.30.42.10:FF:000181; Putative serine protease HTRA3; 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:SF14; SERINE PROTEASE HTRA3; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..453
FT /note="Serine protease HTRA3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014417214"
FT DOMAIN 21..84
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 64..128
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 385..426
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 453 AA; 48688 MW; 4692F7F7F5CFEC2A CRC64;
MQARALLLAA LAALALAREP PAAPCPARCD VSRCPSPRCP GGYVPDLCNC CLVCAASEGE
PCGSPLDSPC GESLECVRGL CRCRWTHAVC GTDGHTYANV CALQAASRRA LQLSGTPVRQ
LQKGACPLGL RQLSSPRYKF NFIADVVEKI APAVVHIELF LRHPLFGRNV PLSSGSGFIM
SEAGLIITNA HVVSSNNAAS GRQQLKVQLQ NGDSYEATIK DIDKKSDIAT IKIHPKKKLP
VLLLGHSADL RPGEFVVAIG SPFALQNTVT TGIVSTAQRE GRELGLRDSD MDYIQTDAII
NYGNSGGPLV NLDGEVIGIN TLKVTAGISF AIPSDRITRF LTEFQDKQIK DWKKRFIGIR
MRTITPSLVD ELKASNPDFP EVSSGIYVQE VAPNSPSQRG GIQDGDIIVK VNGRPLVDSS
ELQEAVLTES PLLLEVRRGN DDLLFSIAPE VVM
//
