ID W5MGN8_LEPOC Unreviewed; 278 AA.
AC W5MGN8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Granzyme B-like {ECO:0000313|Ensembl:ENSLOCP00000007547.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000007547.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000007547.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AHAT01020379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01020380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MGN8; -.
DR STRING; 7918.ENSLOCP00000007547; -.
DR Ensembl; ENSLOCT00000007555.1; ENSLOCP00000007547.1; ENSLOCG00000006230.1.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00910000144271; -.
DR InParanoid; W5MGN8; -.
DR OMA; DNTFCQG; -.
DR Proteomes; UP000018468; Linkage group LG17.
DR Bgee; ENSLOCG00000006230; Expressed in intestine and 10 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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 InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24271:SF81; GRANZYME B; 1.
DR PANTHER; PTHR24271; KALLIKREIN-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.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 47..277
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 278 AA; 31318 MW; A6A2782F4CEC22DA CRC64;
KWTELLTLLE KELGDHINSL MSYNMFYLFF CFLFILVLCK GAFDSYVIGG KTAEPHSRPY
MASLQVDDHH VCGGFLIRED FVLTAAHCYN NRPLTVVLGA HNIRKKEKSQ QKIEVKKFYK
HGLHSLSPLD FDLMLLKLKA NATLNENVKL LTLPKKEVKV KVNTRCSVAG WGKKTANGNA
ESVLQEATLT IQDNKQCKKI WQKYFNSKNM LCTHFGNGKS GICQGDSGGP LVCNTTPNAS
EVLGVVSYSG PTCDDSSYPH VYMKVHSFLK WINEKMKN
//