HTR1B_DANRE
ID HTR1B_DANRE Reviewed; 476 AA.
AC A9JRB3;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Serine protease HTRA1B;
DE EC=3.4.21.-;
DE AltName: Full=High-temperature requirement A serine peptidase 1B;
DE Flags: Precursor;
GN Name=htra1b; ORFNames=zgc:172061;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine protease with a variety of targets, including
CC extracellular matrix proteins and proteoglycans. Through cleavage of
CC proteoglycans, may release soluble FGF-glycosaminoglycan complexes that
CC promote the range and intensity of FGF signals in the extracellular
CC space. Regulates the availability of insulin-like growth factors (IGFs)
CC by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-
CC beta family members. Consequently, may regulate many physiological
CC processes. Intracellularly, degrades TSC2, leading to the activation of
CC TSC2 downstream targets (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms homotrimers. In the presence of substrate, may form
CC higher-order multimers in a PDZ-independent manner. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}. Note=Also found associated with the plasma membrane.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; CR450788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC155591; AAI55592.1; -; mRNA.
DR RefSeq; NP_001104652.1; NM_001111182.1.
DR AlphaFoldDB; A9JRB3; -.
DR SMR; A9JRB3; -.
DR STRING; 7955.ENSDARP00000020528; -.
DR PaxDb; A9JRB3; -.
DR PeptideAtlas; A9JRB3; -.
DR Ensembl; ENSDART00000012318; ENSDARP00000020528; ENSDARG00000014907.
DR GeneID; 565082; -.
DR KEGG; dre:565082; -.
DR CTD; 565082; -.
DR ZFIN; ZDB-GENE-080219-7; htra1b.
DR eggNOG; KOG1320; Eukaryota.
DR GeneTree; ENSGT00940000156955; -.
DR HOGENOM; CLU_020120_6_2_1; -.
DR InParanoid; A9JRB3; -.
DR OMA; IGCPDRC; -.
DR OrthoDB; 630723at2759; -.
DR PhylomeDB; A9JRB3; -.
DR TreeFam; TF323480; -.
DR Reactome; R-DRE-1474228; Degradation of the extracellular matrix.
DR PRO; PR:A9JRB3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000014907; Expressed in swim bladder and 15 other tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
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; 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; PF13180; PDZ_2; 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; PS51465; KAZAL_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Growth factor binding; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..476
FT /note="Serine protease HTRA1B"
FT /id="PRO_0000416253"
FT DOMAIN 27..96
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 94..153
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 361..463
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 200..360
FT /note="Serine protease"
FT /evidence="ECO:0000250"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT ACT_SITE 246
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT ACT_SITE 324
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT SITE 166
FT /note="Involved in trimer stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT SITE 168
FT /note="Involved in trimer stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT SITE 274
FT /note="Involved in trimer stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
SQ SEQUENCE 476 AA; 51122 MW; 875E454D6C36E78D CRC64;
MRLLILCASI ILVPLLCDAR IIKRYVIGCP ERCDKSLCPP IPPDCLAGDI LDQCDCCPVC
AAGEGESCGG TGKLGDPECG EGLECAVSDG VGATTTVRRR GKTGVCVCKS SEPVCGSDGV
SYRNICELKR VSNRAQKLQQ PPIIFIQRGA CGKGHEENPD SLRHRYNFIA DVVEKIAPAV
VHIELFRKNV FNREVAVASG SGFVVSEDGL IVTNAHVVAN KHRVKVELKT GTTYDAKIKD
VDEKADIALI KIDAPMKLPV LLLGRSADLR PGEFVVAIGS PFSLQNTVTT GIVSTTQRGG
KELGLRNSDM DYIQTDAIIN YGNSGGPLVN LDGEVIGINT LKVTAGISFA IPSDKIRQFL
AESHDRQAKG KTATKKKYIG VRMMTLTPTL AKELKQRKND FPDVTSGAYV IEVIPKTPAE
VGGLKESDVI ISINGQRITS ASDVSTAIKT DESLRAVVRR GNEDIILTII PEEIDP
