ID A0A3Q1JR34_ANATE Unreviewed; 495 AA.
AC A0A3Q1JR34;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=HtrA serine peptidase 1b {ECO:0000313|Ensembl:ENSATEP00000017351.2};
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:ENSATEP00000017351.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000017351.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; A0A3Q1JR34; -.
DR STRING; 64144.ENSATEP00000017351; -.
DR Ensembl; ENSATET00000017643.2; ENSATEP00000017351.2; ENSATEG00000012049.2.
DR GeneTree; ENSGT00940000156955; -.
DR InParanoid; A0A3Q1JR34; -.
DR OrthoDB; 2159919at2759; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:SF13; SERINE PROTEASE HTRA1; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..495
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030080554"
FT DOMAIN 31..112
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 108..156
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 386..469
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 495 AA; 53234 MW; 1202CBB20C650A67 CRC64;
MCLRFVLCVM SLLASSCSVA EAQGARVSKH PAIGCPETCD KSQCAPIPTD CLAGDVLDRC
DCCPVCASGE GEQCGGTGDH ECAEGLKCVV TDGVEVSATV RRRSKAGRCM CTSSEPVCGS
DGVSYRNICE LKRVSSKATT LQQPPVIFIQ RGSCGKGQQN PDSLRYKYNF IADVVEKIAP
AVVHIELYRK MIYSKRELAV ASGSGFVVSE DGLIVTNAHV VANKHRVKVE LKSGDTFDAK
IKDVDEKADI ALIQIDAPMK LPVLLLGRSA DLRPGEFVVA IGSPFSLQNT VTTGIVSTTQ
RGGKELGLRN SDMDYIQTDA IINVNLPLLS RSSFAVLLQY GNSGGPLVNL DGEVIGINTL
KVTAGISFAI PSDKIRQFLA ESHDRQIKGK THQKKKYIGV KMMSLTPSLT KELKEKLSDF
PDVTSGAFVL EVIRQTPAEA AGLKETDIII SINGERVTSA SDVSDAIKRD ETLRTVVRRG
NEDVILTIVP EEVEP
//
