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Database: UniProt
Entry: A0A498NCI0_LABRO
LinkDB: A0A498NCI0_LABRO
Original site: A0A498NCI0_LABRO 
ID   A0A498NCI0_LABRO        Unreviewed;       279 AA.
AC   A0A498NCI0;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Trypsin-2-like protein {ECO:0000313|EMBL:RXN30433.1};
GN   ORFNames=ROHU_005029 {ECO:0000313|EMBL:RXN30433.1};
OS   Labeo rohita (Indian major carp) (Cyprinus rohita).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Labeoninae; Labeonini; Labeo.
OX   NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN30433.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN30433.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN30433.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN30433.1};
RA   Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA   Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA   Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA   Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA   Shah T.M., Rai A., Jena J.K.;
RT   "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RXN30433.1}.
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DR   EMBL; QBIY01011586; RXN30433.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498NCI0; -.
DR   STRING; 84645.A0A498NCI0; -.
DR   Proteomes; UP000290572; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   PANTHER; PTHR24264:SF6; TRYPSINOGEN 1A-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   4: Predicted;
KW   Digestion {ECO:0000256|ARBA:ARBA00022757};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..279
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019735372"
FT   DOMAIN          21..193
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          192..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..248
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   279 AA;  31531 MW;  CB2ABE5B4E7841B3 CRC64;
     MRSLVFLVLL GAAFALDDEK IVGGYECKPY SQPWQVSLNS GYHFCGGSLV NENWVVSAAH
     CYMSRIEVRL GEHNIVITEG SEQFIYSDKV IRHPNYNSWT LDSDIMLIKL SKPATLNQYV
     QPVSLPTGCA TAGTNCSVTG WGNTMSSTAD SNKLQCLEIP ILSNSNCNNS YPGMITNTMF
     CAGYLEGGKD SCQKGESLSM DRRNKKEEEG KKEEEEEGEK EEEGKKEEEE EGGKKEEEEE
     GEKEEEGKKE EEEEGKKEEE EEEEEDKEWK YLMKFEQQS
//
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