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Database: UniProt/TrEMBL
Entry: L5KQU0_PTEAL
LinkDB: L5KQU0_PTEAL
Original site: L5KQU0_PTEAL 
ID   L5KQU0_PTEAL            Unreviewed;       247 AA.
AC   L5KQU0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   31-JAN-2018, entry version 28.
DE   SubName: Full=Anionic trypsin {ECO:0000313|EMBL:ELK13777.1};
GN   ORFNames=PAL_GLEAN10019030 {ECO:0000313|EMBL:ELK13777.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera;
OC   Pteropodidae; Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13777.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y.,
RA   Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y.,
RA   Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G.,
RA   Wang L.F., Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the
RT   evolution of flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|SAAS:SAAS00559343}.
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DR   EMBL; KB030581; ELK13777.1; -; Genomic_DNA.
DR   RefSeq; XP_006910523.1; XM_006910461.1.
DR   MEROPS; S01.120; -.
DR   GeneID; 102897268; -.
DR   KEGG; pale:102897268; -.
DR   InParanoid; L5KQU0; -.
DR   KO; K01312; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000010552};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00037407};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     15       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        16    247       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012677878.
FT   DOMAIN       25    245       Peptidase S1. {ECO:0000259|PROSITE:
FT                                PS50240}.
SQ   SEQUENCE   247 AA;  26342 MW;  C51320C171CD2330 CRC64;
     MNPLLILAVV GAAVAFSTDD DDDKIVGGYT CKEGSVPYQV SLNSGYHFCG GSLISNQWVV
     SAAHCYKSRI QVRLGEYNIE EVEGNEQFIN SAKVIRHPSY SSQTLDNDIM LIKLSSTATL
     NSRVSTISLP SSCASTGTQC LVSGWGNTLS SGSNYPELLQ CLNVPVLSQA KCEAAYPGQI
     TSNMFCAGYL EGGKDSCQGD SGGPVVCSNK LQGIVSWGYG CAQKNKPGVY TKVCKFVDWI
     KKTVASN
//
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