ID M3VY57_FELCA Unreviewed; 565 AA.
AC M3VY57;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Ovochymase 2 {ECO:0000313|Ensembl:ENSFCAP00000002076.5};
GN Name=OVCH2 {ECO:0000313|Ensembl:ENSFCAP00000002076.5,
GN ECO:0000313|VGNC:VGNC:105825};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000002076.5, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000002076.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002076.5,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000002076.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002076.5,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000002076.5}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002076.5};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR EMBL; AANG04002890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3VY57; -.
DR STRING; 9685.ENSFCAP00000002076; -.
DR PaxDb; 9685-ENSFCAP00000002076; -.
DR Ensembl; ENSFCAT00000002251.5; ENSFCAP00000002076.5; ENSFCAG00000002251.5.
DR VGNC; VGNC:105825; OVCH2.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000157791; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; M3VY57; -.
DR OMA; GAFQFDH; -.
DR Proteomes; UP000011712; Chromosome D1.
DR Bgee; ENSFCAG00000002251; Expressed in adult mammalian kidney and 4 other cell types or tissues.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24251:SF16; OVOCHYMASE-2; 1.
DR PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00059}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..565
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023803710"
FT DOMAIN 52..299
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 311..420
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 430..542
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 430..457
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 565 AA; 62531 MW; CC60E41BED08DAF9 CRC64;
MPLSKNRLIL LLGMLCVEQC KSATLSLPKA PTCGQSLVKA QPWNYLNIFS RIVGGSQVEK
GSYPWQVSLK RRQKHICGGT IISAQWVITA AHCIANRNIA STLNVTAGEY DLSHIEPGEQ
TLTIETIIIH PYFSIKKPMD YDIALLKMDG AFHFGQFVGP VCLPEPKEEF EAGFICTTAG
WGRSAEDGVV SQVLQDVNLP ILTQEECVAA LLTLKKPISG QTFLCTGFPD GGRDACQGDS
GGSLMCRNKK GAWTLAGVTS WGLGCGRGWR NNMQEDNQGS PGIFTDLRKV LPWIHKHIQI
GKRRKSSRAS CSEQDRVLRE SQGELRFPES PYLYYESKQL CVWILLAPEK MHVLLNVSHL
DAESCHHTYL SISLEDRLLG KFCGESLPSS VLIGSNSVQL NSVSDATDHA AGFNLTYKAL
KPNYLPDSGC SSFTVLFEEG LIQSLHYPEY YSNMANCEWV FQAPKHYLIK LSFQSLEIEE
NGDCSSDYVA VHRDVEGQEE IARFCGFVAP APVLSSSGVM LISFQSDKNV TYRGFQATVS
FIPGTVHSDL NISRSEDKSL FLETW
//
