ID H3AP08_LATCH Unreviewed; 477 AA.
AC H3AP08;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=HtrA serine peptidase 1 {ECO:0000313|Ensembl:ENSLACP00000011379.1};
GN Name=HTRA1 {ECO:0000313|Ensembl:ENSLACP00000011379.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000011379.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000011379.1}
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}.
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; AFYH01123302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01123303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01123304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01123305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01123306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01123307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01123308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01123309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01123310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01123311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006001804.1; XM_006001742.2.
DR AlphaFoldDB; H3AP08; -.
DR STRING; 7897.ENSLACP00000011379; -.
DR Ensembl; ENSLACT00000011465.1; ENSLACP00000011379.1; ENSLACG00000010012.1.
DR GeneID; 102345424; -.
DR KEGG; lcm:102345424; -.
DR CTD; 565082; -.
DR eggNOG; KOG1320; Eukaryota.
DR GeneTree; ENSGT00940000156955; -.
DR HOGENOM; CLU_020120_6_2_1; -.
DR InParanoid; H3AP08; -.
DR OMA; THGWVLE; -.
DR OrthoDB; 2159919at2759; -.
DR TreeFam; TF323480; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000010012; Expressed in muscle tissue and 6 other cell types or tissues.
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; 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; 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.
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:UP000008672};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..477
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003580084"
FT DOMAIN 26..110
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 107..154
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
SQ SEQUENCE 477 AA; 51063 MW; 79C92155E0A70B56 CRC64;
MMWPVLLCVC WVLASFSAEA RISKRYVVGC PERCDPALCP PLPTDCPSGQ TLDQCGCCSV
CAAGEGEPCG GSGRLGEPLC GDGLECSVSA GVAASLTVRR RGSPGLCVCK SAEPVCGSDG
KTYRTVCELK SASSRAEKLQ QPPVILIQRG ACGQGQEDPN SLRYKYNFIA DVVEKIAPAV
VHIELFRKLP FSKREIAVAS GSGFIVSEDG LIVTNAHVVT NKHRVKVEVK NGATYDAKIK
DVDEKADIAL IKIDPKGKLP VLLLGHSADL RPGEFVVAIG SPFSLQNTVT TGIVSTTQRG
GKELGLRNSD MDYIQTDAII NYGNSGGPLV NLDGEVIGIN TLKVTAGISF AIPSDKIKEF
LTESHDRQSK GKTVNKKKYI GVRMMSLTPS LAKELKERQK DFPDVTSGAY IVEVISKTPA
AFAGLKENDV IISINSQSIR SASDVSDVIK RENTLNVVVR RGNEDIILTV IPEDIEP
//