HTRA1_XENTR
ID HTRA1_XENTR Reviewed; 460 AA.
AC A4IHA1; A0JM19;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Serine protease HTRA1;
DE EC=3.4.21.-;
DE AltName: Full=High-temperature requirement A serine peptidase 1;
DE AltName: Full=Serine protease 11;
DE Flags: Precursor;
GN Name=htra1; Synonyms=htra, prss11;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine protease with a variety of targets, including
CC extracellular matrix proteins and proteoglycans such as biglycan,
CC syndecan-4 and glypican-4. Through cleavage of proteoglycans, may
CC release soluble FGF-glycosaminoglycan complexes that promote the range
CC and intensity of FGF signals in the extracellular space. Consequently,
CC facilitates inductive processes in the developing embryo, such as
CC posteriorization, mesoderm induction and neuronal differentiation.
CC Regulates the availability of insulin-like growth factors (IGFs) by
CC cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta
CC 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: Cell membrane {ECO:0000250|UniProtKB:Q92743}.
CC Secreted {ECO:0000250|UniProtKB:Q92743}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q92743}. Note=Predominantly secreted. Also found
CC associated with the plasma membrane. {ECO:0000250|UniProtKB:Q92743}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI25706.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI35435.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAMC01093882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01093885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125705; AAI25706.1; ALT_INIT; mRNA.
DR EMBL; BC135434; AAI35435.1; ALT_INIT; mRNA.
DR RefSeq; NP_001072730.2; NM_001079262.2.
DR AlphaFoldDB; A4IHA1; -.
DR SMR; A4IHA1; -.
DR STRING; 8364.ENSXETP00000033992; -.
DR MEROPS; S01.277; -.
DR PaxDb; A4IHA1; -.
DR DNASU; 780187; -.
DR GeneID; 780187; -.
DR KEGG; xtr:780187; -.
DR CTD; 5654; -.
DR Xenbase; XB-GENE-487699; htra1.
DR eggNOG; KOG1320; Eukaryota.
DR HOGENOM; CLU_020120_6_2_1; -.
DR InParanoid; A4IHA1; -.
DR OrthoDB; 630723at2759; -.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000015580; Expressed in skeletal muscle tissue and 9 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:0005886; C:plasma membrane; 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; 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; PS51465; KAZAL_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Disulfide bond; Growth factor binding; Hydrolase;
KW Membrane; Protease; Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..460
FT /note="Serine protease HTRA1"
FT /id="PRO_0000416255"
FT DOMAIN 22..88
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 74..136
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 344..447
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 183..343
FT /note="Serine protease"
FT ACT_SITE 199
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT ACT_SITE 307
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT SITE 148
FT /note="Involved in trimer stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT SITE 150
FT /note="Involved in trimer stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT SITE 257
FT /note="Involved in trimer stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT DISULFID 89..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 98..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CONFLICT 381
FT /note="V -> L (in Ref. 1; AAI35435)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="H -> Q (in Ref. 1; AAI25706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 48897 MW; E9B74E6E53FDBFE2 CRC64;
MAMLWLAVLL TCGAPAALLP TSGVGCPSRC DPASCAPAPT NCPAGETALR CGCCPVCAAA
EWERCGEGPE DPLCASGLRC VKNGGVARCQ CPSNLPVCGS DGKTYPSLCR LQAESKAAQG
KGSAAIIPIQ RGDCQQGQRD PDSPRYKYNF IADVVEKIAP AVVHIELFRM LPFFKREVPA
ASGSGFIVSE DGLILTNAHV VTNKHRLKVE RSDGSTYDAQ IIDVDEKADI ALIKIKAKGK
LPVLLLGRSE DLRPGEFVVA IGSPFSLQNT VTTGIVSTAQ RGGKELGLRN SDMDYIQTDA
IINYGNSGGP LVNLDGEVIG INTLKVTAGI SFAIPSDKIR KFLAESHNRQ STGQGTKKKK
YLGIRMMSLS QGKLKELKEQ VKDFPENTSG AYIVEVIPDT PAEEAGLKEG DIIISIGGKS
VTSSSDVSDA IKKEGTTLHL VIRRGNEDIP ISVTPKEIEF
