ID A0A3Q1I8M9_ANATE Unreviewed; 482 AA.
AC A0A3Q1I8M9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Serine protease HTRA1A-like {ECO:0000313|Ensembl:ENSATEP00000013713.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000013713.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000013713.2}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q1I8M9; -.
DR STRING; 64144.ENSATEP00000013713; -.
DR Ensembl; ENSATET00000013931.2; ENSATEP00000013713.2; ENSATEG00000009535.2.
DR GeneTree; ENSGT00940000156955; -.
DR InParanoid; A0A3Q1I8M9; -.
DR OrthoDB; 2159919at2759; -.
DR Proteomes; UP000265040; 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; 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:SF128; SERINE PROTEASE HTRA1A; 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:UP000265040};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..482
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030079776"
FT DOMAIN 31..115
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 106..159
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 367..468
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 482 AA; 51568 MW; DC2443928530B266 CRC64;
VSLVSVMFWS LLCVILAFAS APADAQISNR YVIGCPARCD KSMCPRLPAD CQAGQALDAC
NCCPVCASGE GESCGGSGKL GDPVCGEGLE CSVSGGVAFT ATVRRRSKTG ICVCKATDPV
CGSDGVSYRN ICELKRVSRR AQKLQQPPVL FIQRGACGKA QDNPDSPRHK YNFIADVVER
IAPSVVHIEL YRKMTYSKRE VAVASGSGFV VSEDGQIVTN AHVVANKHRV KVELKSGATY
DAKIKDVDEK SDIALIKIDV PTNLPVLLLG RSSDLRPGEF VVAIGSPFSL QNTVTTGIVS
TTQRGGRELG LRNSDMDYIQ TDAIINYGNS GGPLVNLDGE VIGINTLKVT AGISFAIPSD
KIRQFLAESY DRQSRGMTGA KKKYIGVRMM TLTPALAKEL KTQHRDFPDI TSGAYVMEVI
AKTPAEVGGL KEHDVIISIN GQRVSSATDV STAVKKDDTL RVVVRRGNED AILTVVPIDI
DP
//
