ID A4UWM5_ORYLA Unreviewed; 1036 AA.
AC A4UWM5;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Enteropeptidase-1 {ECO:0000313|EMBL:BAF57203.1};
GN Name=EP-1 {ECO:0000313|EMBL:BAF57203.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|EMBL:BAF57203.1};
RN [1] {ECO:0000313|EMBL:BAF57203.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17438297; DOI=10.1073/pnas.0610447104;
RA Ogiwara K., Takahashi T.;
RT "Specificity of the medaka enteropeptidase serine protease and its
RT usefulness as a biotechnological tool for fusion-protein cleavage.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7021-7026(2007).
RN [2] {ECO:0007829|PDB:3W94}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 795-1029, AND DISULFIDE BONDS.
RX PubMed=24481630; DOI=10.1007/s13238-013-0008-x;
RA Xu J., Hu S., Wang X., Zhao Z., Zhang X., Wang H., Zhang D., Guo Y.;
RT "Structure basis for the unique specificity of medaka enteropeptidase light
RT chain.";
RL Protein Cell 5:178-181(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; AB272104; BAF57203.1; -; mRNA.
DR RefSeq; NP_001098368.1; NM_001104898.1.
DR PDB; 3W94; X-ray; 2.00 A; A/B=795-1029.
DR PDBsum; 3W94; -.
DR AlphaFoldDB; A4UWM5; -.
DR SMR; A4UWM5; -.
DR MEROPS; S01.156; -.
DR GeneID; 100125449; -.
DR CTD; 100125449; -.
DR BRENDA; 3.4.21.9; 3199.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd06263; MAM; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR017949; Thaumatin_CS.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF15; TRANSMEMBRANE SERINE PROTEASE 15; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00200; SEA; 1.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS00316; THAUMATIN_1; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3W94};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 39..153
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 229..338
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 349..511
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 532..643
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 795..1029
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 229..256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 652..664
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 659..677
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 671..686
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 820..836
FT /evidence="ECO:0007829|PDB:3W94"
FT DISULFID 920..987
FT /evidence="ECO:0007829|PDB:3W94"
FT DISULFID 951..966
FT /evidence="ECO:0007829|PDB:3W94"
FT DISULFID 977..1005
FT /evidence="ECO:0007829|PDB:3W94"
SQ SEQUENCE 1036 AA; 113392 MW; 1C08D01B016C9630 CRC64;
MKRRLTNLEV LLTVTTSLFA VCCVCLIVVS CIGLKPEGAA QPVQLTGQMV ITAGAAFSEE
LRNSSSHFFK SLAFDVQQLV SDAFGASELR LLYRSFRVLY FRPGSIAVTF DLEFNQQIDL
NEVKQQLGEG LQQIEDGALV IDVDSIQITV KPSSTTPQPT PTTGHITTET MPITGHTTPA
ATPTAASCPP DHSLCWDRST CVLTDVLCDG VSDCPDASDE NSSRCATTCD GQFVLGGPNG
TFRSSETETY RNNSNCRWII RMDGGLSVQV NFHHFETEEY SDVLKLYEGV GPHKQLAAEL
SGPSPPGTVL LLNNQVTVEF TSDGVNDLSG FRASYAAVNT SSLSNQEKLS CSFDQGFCFW
RQLQDSFDTW IRTNVPTFPP LTGPNFDHTF GNSSGFYIVT SLSPGQWLKS FVINSLPLAP
SSHPTCLSFW YHMFGEDVYR LRVLLRPSQP ELTEVVLFHK EGNFGDNWNY AQITLNLSTE
STVVFEAQKE GGNQNDIALD DISLRSEGCG PAPPEPTNVP LPTTAAPIPP DCGGPFDLWE
PNSTFTSPNY PQSYGDRAEC LWTLHAEKGQ NIQLHFLDFD VEATYDVVEV RDGAGLNSTL
LAVLSGSDGP THDLYSTDNQ MTVWFYTDSG GFGRGFRANF TSGVNLGSQA PCANGQFQCQ
TGDCIHGDRQ CDGVADCPDG YDEADCVALQ VNGSHRLHFR LLHSLLTVCA DTWDSELSDF
TCQYLGYRSG EESLQPVLPQ DAAFAVVTVS SNGTLETQVR ETCSSGEVIS LNCSNQPCGQ
RQVYNSKENN GVPRVVGGVN AEKGAWPWMV SLHWRGRHGC GASLIGRDWL LTAAHCVYGK
NTHLQYWSAV LGLHAQSSMN SQEVQIRQVD RIIINKNYNR RTKEADIAMM HLQQPVNFTE
WVLPVCLASE DQHFPAGRRC FIAGWGRDAE GGSLPDILQE AEVPLVDQDE CQRLLPEYTF
TSSMLCAGYP EGGVDSCQGD SGGPLMCLED ARWTLIGVTS FGVGCGRPER PGAYARVSAF
TSWIAETRRS SFSDLD
//
