ID A0A2Y9DYH4_TRIMA Unreviewed; 420 AA.
AC A0A2Y9DYH4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Serine protease HTRA3 {ECO:0000313|RefSeq:XP_004383610.1};
GN Name=LOC101358420 {ECO:0000313|RefSeq:XP_004383610.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004383610.1};
RN [1] {ECO:0000313|RefSeq:XP_004383610.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_004383610.1; XM_004383553.1.
DR AlphaFoldDB; A0A2Y9DYH4; -.
DR STRING; 127582.A0A2Y9DYH4; -.
DR GeneID; 101358420; -.
DR KEGG; tmu:101358420; -.
DR InParanoid; A0A2Y9DYH4; -.
DR OrthoDB; 2159919at2759; -.
DR Proteomes; UP000248480; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00104; KAZAL_FS; 1.
DR CDD; cd00987; PDZ_serine_protease; 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:SF14; SERINE PROTEASE HTRA3; 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; 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 ECO:0000313|RefSeq:XP_004383610.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480}.
FT DOMAIN 1..51
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 31..95
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 352..393
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT NON_TER 1
FT /evidence="ECO:0000313|RefSeq:XP_004383610.1"
SQ SEQUENCE 420 AA; 45026 MW; 788AD1C776D241F5 CRC64;
CPSPRCPGGY VPDHCNCCLV CAAGEGEPCG SPLDSPCGES LECARGACRC RGAHAVCGTD
GHTYANVCAL QAASRRALQL AGTPVRQLQK GACPSGLHQL NSPRYKFNFI ADVVEKIAPA
VVHIELFLRH PLFGRNVPLS SGSGFIMSEA GLIVTNAHVV SSTNTVSGRQ QLKVQLQNGD
TYEATIKDID KKSDIATIKI HPKRKLPVLL LGHSADLRPG EFVVAIGSPF ALQNTVTTGI
VSTAQRDGKE LGLQDSDMDY IQTDAIINYG NSGGPLVNLD GEVIGINTLK VAAGISFAIP
SDRITRFLTE FQDKHIKDWK KRFIGIRMRT ITPSLVEELK ASNPDFPEVS SGIYVQEVVP
NSPSQRGGIQ DGDLIVKVNG RPLADSSELQ EAVLTESPLL LEVRRGNDDL LFSIAPEVVL
//
