ID A0A1S3N800_SALSA Unreviewed; 426 AA.
AC A0A1S3N800;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Serine protease hepsin-like {ECO:0000313|RefSeq:XP_014011564.1};
GN Name=LOC106577761 {ECO:0000313|RefSeq:XP_014011564.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014011564.1};
RN [1] {ECO:0000313|RefSeq:XP_014011564.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014011564.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR RefSeq; XP_014011564.1; XM_014156089.1.
DR AlphaFoldDB; A0A1S3N800; -.
DR Ensembl; ENSSSAT00000055880; ENSSSAP00000030580; ENSSSAG00000039705.
DR GeneID; 106577761; -.
DR KEGG; sasa:106577761; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000087266; Chromosome ssa02.
DR Bgee; ENSSSAG00000039705; Expressed in liver and 3 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:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR015352; Hepsin-SRCR_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF14; TRANSMEMBRANE PROTEASE SERINE 3-LIKE; 1.
DR Pfam; PF09272; Hepsin-SRCR; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50287; SRCR_2; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU363034,
KW ECO:0000313|RefSeq:XP_014011564.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..153
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 165..409
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 426 AA; 47192 MW; C88FB059F4B7E935 CRC64;
MTEKKNGSAG VTFLTPCRVA GMCLTVVLLG GIGAAVWAVV TFCIREEDTG LYDVQVNSNP
SSDLRLRVFD SAERRWRHLC SSEANQLLAN ISCEEMGFVS VVNYSVSSIP EGSNDREEFF
CVNEKELTYG KKIKESLYPC DCETGQVLSL LCQDCGRRSL TEDRIVGGVD ARQGSWPWQV
SLQYDGVHQC GGSIISDRWI VSAAHCFPER NRQVSRWRVL LGSIYNKLTH KNVRVLEVKT
VVYHSSYLPF VDPNIDDNSR DIAVLALAQP LHFTDYIQPV CLPHYGQRLI DGQMGTVTGW
GNVGYYGTLA DVLQEANVPI INDAVCNAPD YYDNQITTSM FCAGFEKGGT DACQGDSGGP
FVAEDSLSKA SRYRLLGVVS WGTGCAMAKK PGVYTRVSRF LPWISSAMRT YHNSPGVHKM
ARTWEH
//
