ID A4UWM6_ORYLA Unreviewed; 1043 AA.
AC A4UWM6;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Enteropeptidase-2 {ECO:0000313|EMBL:BAF57204.1};
DE SubName: Full=Transmembrane serine protease 15 {ECO:0000313|Ensembl:ENSORLP00000037641.1};
GN Name=EP-2 {ECO:0000313|EMBL:BAF57204.1};
GN Synonyms=tmprss15 {ECO:0000313|Ensembl:ENSORLP00000037641.1};
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:BAF57204.1};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000037641.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000037641.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|EMBL:BAF57204.1}
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 [3] {ECO:0000313|Ensembl:ENSORLP00000037641.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000037641.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AB272105; BAF57204.1; -; mRNA.
DR RefSeq; NP_001098369.1; NM_001104899.1.
DR STRING; 8090.ENSORLP00000037641; -.
DR MEROPS; S01.156; -.
DR Ensembl; ENSORLT00000033283.1; ENSORLP00000037641.1; ENSORLG00000023625.1.
DR GeneID; 100125450; -.
DR KEGG; ola:100125450; -.
DR CTD; 5651; -.
DR GeneTree; ENSGT00940000164655; -.
DR OrthoDB; 4252799at2759; -.
DR Proteomes; UP000001038; Chromosome 14.
DR Bgee; ENSORLG00000023625; Expressed in intestine and 6 other cell types or tissues.
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 2: Evidence at transcript level;
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 Reference proteome {ECO:0000313|Proteomes:UP000001038};
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 802..1036
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 150..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 1043 AA; 114016 MW; FDF554704C6B6955 CRC64;
MKRRLTNLEV LLTVTTSLFA VCCVCLIVVS CIGLKPEGAA EPVQLIGQMV ITAGAAFSEE
LRNSSSHLFK SLAFDVQQLV SDAFGASELR LLYRSFRVLY FRPGSIAVTF DLEFNQQIDL
NEVKQQLGEG LQQIEDGALV IDVDSIQITE KPSSTTPEPT STTGHITTET MPITGHTTPA
ATPTAASCPP DHSLCWDRST CVLTDVLCDG VSDCPDASDE NSSRCATTCD GQFVLGGPNG
TFRSSETETY RNNSNCRWII RMDGGLSVQV NFHHFETEEY SDVLKLYEGV GPHKQLAAEL
SGPSPPGTVL LLNNQVTVEF TSDGVNDLSG FRASYVAVNT SSLSNQEKLS CSFDQGFCFW
RQLQDSFDTW IRTNVPTFPP LTGPNFDHTF GNSSGFYIVT SLSPGQWLKS FVINSLPLAP
SSHPTCLSFW YHMFGEDVYR LRVLLRPSQP ELTEVVLFHK EGNFGDNWNY AQITLNLSTE
STVVFEAQKE GGNQNDIALD DISLRSEGCG PAPPEPTNVP LPTTAAPIPP DCGGPFDLWE
PNSTFTSPNY PQSYGDGAEC LWTLHAEKGQ NIQLHFLDFD VEATYDVVEV RDGAGLNSTL
LAVLSGSDGP TRDLYSTDNQ MTVWFYTDSG GFGRGFRANF TSGVNLGSQA PCTNGQFQCQ
TGDCIHGDRQ CDGVADCPDG YDEADCVALQ VNGSHRLHFL LLRSLLTVCA DTWDSELSDF
TCQYLGYRSG EESLQSVLPQ DAAFAVVTVS SNGTLETQVR ETCSSGEVIS LNCSNQPCGQ
RQVYNHGDQS ENSKENNGVP RVVGGVNAEK GAWPWMVSLH WRGRHGCGAS LIGRDWLLTA
AHCVYGKNTH LQYWSAVLGL HAQSSMNSQE VQIRQVDRII INKNYNRRTK EADIAMMHLQ
QPVNFTEWVL PVCLASEGQH FPAGRRCFIA GWGRDAEGGS LPDILQEAEV PLVDQDECQR
LLPEYTFTSS MLCAGYPEGG VDSCQGDSGG PLMCLEDARW TLIGVTSFGV GCGRPERPGA
YARVSAFASW IAETRRSSFS DLD
//
