HTRA4_MOUSE
ID HTRA4_MOUSE Reviewed; 483 AA.
AC A2RT60;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Serine protease HTRA4;
DE EC=3.4.21.-;
DE AltName: Full=High-temperature requirement factor A4;
DE Flags: Precursor;
GN Name=Htra4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Serine protease. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; AC156553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466580; EDL32845.1; -; Genomic_DNA.
DR EMBL; BC132380; AAI32381.1; -; mRNA.
DR EMBL; BC145842; AAI45843.1; -; mRNA.
DR CCDS; CCDS40301.1; -.
DR RefSeq; NP_001074656.1; NM_001081187.3.
DR AlphaFoldDB; A2RT60; -.
DR SMR; A2RT60; -.
DR STRING; 10090.ENSMUSP00000081044; -.
DR MEROPS; S01.329; -.
DR PhosphoSitePlus; A2RT60; -.
DR jPOST; A2RT60; -.
DR MaxQB; A2RT60; -.
DR PaxDb; A2RT60; -.
DR PeptideAtlas; A2RT60; -.
DR PRIDE; A2RT60; -.
DR ProteomicsDB; 273323; -.
DR Antibodypedia; 23738; 109 antibodies from 19 providers.
DR DNASU; 330723; -.
DR Ensembl; ENSMUST00000084031; ENSMUSP00000081044; ENSMUSG00000037406.
DR GeneID; 330723; -.
DR KEGG; mmu:330723; -.
DR UCSC; uc009lfp.2; mouse.
DR CTD; 203100; -.
DR MGI; MGI:3036260; Htra4.
DR VEuPathDB; HostDB:ENSMUSG00000037406; -.
DR eggNOG; ENOG502RMZV; Eukaryota.
DR GeneTree; ENSGT00940000160760; -.
DR HOGENOM; CLU_020120_6_2_1; -.
DR InParanoid; A2RT60; -.
DR OMA; NQQWIEV; -.
DR OrthoDB; 630723at2759; -.
DR PhylomeDB; A2RT60; -.
DR TreeFam; TF323480; -.
DR BioGRID-ORCS; 330723; 3 hits in 76 CRISPR screens.
DR PRO; PR:A2RT60; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; A2RT60; protein.
DR Bgee; ENSMUSG00000037406; Expressed in tarsal region and 61 other tissues.
DR Genevisible; A2RT60; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0012501; P:programmed cell death; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR Gene3D; 2.30.42.10; -; 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 Pfam; PF00219; IGFBP; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00121; IB; 1.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..483
FT /note="Serine protease HTRA4"
FT /id="PRO_0000417600"
FT DOMAIN 35..113
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 379..471
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 208..368
FT /note="Serine protease"
FT /evidence="ECO:0000250"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 254
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 332
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
SQ SEQUENCE 483 AA; 51988 MW; D81BA7C2C22C2169 CRC64;
MSFQRLWAVR TQFLLLWLLL PAVPVPWAEA RRSRVSLPCP DACDPTRCPT LPTCSAGLAP
VPDRCGCCRV CAAAEGQECG GARGRPCAPR LRCGAPFSRD PSGGAWLGTC GCAEGAEDAV
VCGSDGRTYP SLCALRKENR AARQRGALPA VPVQKGACEE AGTTRAGRLR RKYNFIAAVV
EKVAPSVVHL QLFRRSPLTN QEIPSSSGSG FIVSEDGLIV TNAHVLTNQQ KIQVELQSGA
RYEATVKDID HKLDLALIKI EPDTELPVLL LGRSSDLRAG EFVVALGSPF SLQNTVTAGI
VSTTQRGGRE LGLKNSDIDY IQTDAIINHG NSGGPLVNLD GDVIGINTLK VTAGISFAIP
SDRIRQFLED YHERQLKGKA PLQKKYLGLR MLPLTLNLLQ EMKRQDPEFP DVSSGVFVYE
VIQGSAAASS GLRDHDVIVS INGQPVTTTT DVIEAVKDND FLSIIVLRGS QTLFLTVTPE
IIN
