ID A0A3B3RVD2_9TELE Unreviewed; 420 AA.
AC A0A3B3RVD2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Hepsin {ECO:0000313|Ensembl:ENSPKIP00000022474.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000022474.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000022474.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B3RVD2; -.
DR STRING; 1676925.ENSPKIP00000022474; -.
DR Ensembl; ENSPKIT00000003139.1; ENSPKIP00000022474.1; ENSPKIG00000006466.1.
DR GeneTree; ENSGT00940000159697; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000261540; Unplaced.
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:0072378; P:blood coagulation, fibrin clot formation; IEA:Ensembl.
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; IPR017448; SRCR-like_dom.
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; SM00202; SR; 1.
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 Serine protease {ECO:0000256|RuleBase:RU363034};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..150
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 162..406
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 420 AA; 46538 MW; BE88E5DDEB4B8231 CRC64;
MSEKNNGSQG ISFLTPCRVI TSFLILFLLV GIGAAAWAVV TFLIKQEETG LYDVQVNSVD
QRLSVFDRMQ GRWRSVCSSS SNELLANISC EEMGFVRALN HSVYSILNGI NNSEDFFCVG
VEELTYGKKF RELLFPCNCD SGLILRVQCQ DCGRRSLTED RIVGGLDARQ GSWPWQVSLQ
YDGVHQCGGS IISDRWIVSA AHCFPERYRH VARWRVLLGS IYKAHTHSSV HTAEVQTVVF
HSSYLPFVDP NVDDNSRDIA VLALTSRLQF TEYIQPVCLP TYGQRLIDGQ MGTVTGWGNT
EYYGQPSDVL QEASVPIISD AVCNAADYYD NQITTSMFCA GYEKGGTDAC QGDSGGPFVS
EDSLSKASRY RLLGVVSWGT GCAMAKKPGV YTKVSRFLPW ISSAMRTFEN VPGVHKMSRT
//
