ID A0A383ZCN0_BALAS Unreviewed; 553 AA.
AC A0A383ZCN0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Ovochymase-2 {ECO:0000313|RefSeq:XP_007172943.1};
GN Name=OVCH2 {ECO:0000313|RefSeq:XP_007172943.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007172943.1};
RN [1] {ECO:0000313|RefSeq:XP_007172943.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007172943.1};
RG RefSeq;
RL Submitted (JAN-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 RefSeq; XP_007172943.1; XM_007172881.1.
DR AlphaFoldDB; A0A383ZCN0; -.
DR STRING; 310752.A0A383ZCN0; -.
DR KEGG; bacu:103007935; -.
DR CTD; 341277; -.
DR InParanoid; A0A383ZCN0; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000261681; Unplaced.
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:UP000261681};
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..553
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016773223"
FT DOMAIN 52..299
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 299..409
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 419..531
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 419..446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 553 AA; 61422 MW; C9A62DB220F1D119 CRC64;
MHMSKNKLIL LLGMICLEQS KSATLSLPKV PTCGQSLVKS RPLNYLNIFS RIVGGRQVEK
GSYPWQVSLK RRQKHVCGGT IISPEWVITA AHCVANRNIA STFNVTAGEY DLSYIEPGEQ
TLTIETIIIH PYFSTKKPMD YDIALLKMAG AFHFDQSVRP VCLPEPGEQF EPGFICTTTG
WGRLNEDGVV PQVLQEVNLP ILTQDECITA LLTLQKPISG RTFLCTGFPD GGRDACQGDS
GGSLMCRNKK GTWTLAGVTS WGLGCGRGWR NNLQKDDQGS PGIFTDLTKV LPWIHKPSCS
EQDRVIRASA GELHFPESPF LYYESKQMCV WTLFVPEGMH VLLNFSHFDA ESCHHNYLSV
YSLEDTLIGK FCGDSLASSV LVGSNAIRLR FISDATDYAV GFNLTYKALK PNYLPDSGCS
SLTILFEEGL IQSLHYPEDY SNMASCNWVF QAPKRHLVKL SFQNLEIEES GDCTSDYVSV
HRDVERKKEI ARLCGFVVPA PVVSISRVMS ISFQSDENMT FRGFQAAVSF IPKTGKKLEA
PTPQVPSLIL LPW
//
