ID   ENTK_PIG                Reviewed;        1034 AA.
AC   P98074;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Enteropeptidase;
DE            EC=3.4.21.9;
DE   AltName: Full=Enterokinase;
DE   AltName: Full=Serine protease 7;
DE   AltName: Full=Transmembrane protease serine 15;
DE   Contains:
DE     RecName: Full=Enteropeptidase non-catalytic mini chain;
DE   Contains:
DE     RecName: Full=Enteropeptidase non-catalytic heavy chain;
DE   Contains:
DE     RecName: Full=Enteropeptidase catalytic light chain;
DE   Flags: Precursor;
GN   Name=TMPRSS15; Synonyms=ENTK, PRSS7;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Duodenal mucosa;
RX   PubMed=8051081; DOI=10.1016/s0021-9258(17)32116-6;
RA   Matsushima M., Ichinose M., Yahagi N., Kakei N., Tsukada S., Miki K.,
RA   Kurokawa K., Tashiro K., Shiokawa K., Shinomiya K., Umeyama H., Inoue H.,
RA   Takahashi T., Takahashi K.;
RT   "Structural characterization of porcine enteropeptidase.";
RL   J. Biol. Chem. 269:19976-19982(1994).
CC   -!- FUNCTION: Responsible for initiating activation of pancreatic
CC       proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A).
CC       It catalyzes the conversion of trypsinogen to trypsin which in turn
CC       activates other proenzymes including chymotrypsinogen,
CC       procarboxypeptidases, and proelastases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Activation of trypsinogen by selective cleavage of 6-Lys-|-
CC         Ile-7 bond.; EC=3.4.21.9;
CC   -!- SUBUNIT: Heterotrimer of a catalytic (light) chain, a multidomain
CC       (heavy) chain, and a mini chain.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: The chains are derived from a single precursor that is cleaved by
CC       a trypsin-like protease.
CC   -!- PTM: The mini chain may be cleaved by elastase.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; D30799; BAA06459.1; -; mRNA.
DR   PIR; A53663; A53663.
DR   RefSeq; NP_001001259.1; NM_001001259.1.
DR   AlphaFoldDB; P98074; -.
DR   SMR; P98074; -.
DR   STRING; 9823.ENSSSCP00000069010; -.
DR   MEROPS; S01.156; -.
DR   GlyCosmos; P98074; 22 sites, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000012801; -.
DR   GeneID; 397152; -.
DR   KEGG; ssc:397152; -.
DR   CTD; 5651; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; P98074; -.
DR   OrthoDB; 4252799at2759; -.
DR   BRENDA; 3.4.21.9; 6170.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; 3.10.250.10; SRCR-like domain; 1.
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; IPR011163; Pept_S1A_enterop.
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; 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: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; PF00530; SRCR; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001138; Enteropeptidase; 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; 2.
DR   PROSITE; PS50068; LDLRA_2; 2.
DR   PROSITE; PS00740; MAM_1; 1.
DR   PROSITE; PS50060; MAM_2; 1.
DR   PROSITE; PS50024; SEA; 1.
DR   PROSITE; PS00420; SRCR_1; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Membrane; Protease; Reference proteome; Repeat; Serine protease;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Zymogen.
FT   PROPEP          1..51
FT                   /id="PRO_0000027723"
FT   CHAIN           52..117
FT                   /note="Enteropeptidase non-catalytic mini chain"
FT                   /id="PRO_0000027724"
FT   CHAIN           118..799
FT                   /note="Enteropeptidase non-catalytic heavy chain"
FT                   /id="PRO_0000027725"
FT   CHAIN           800..1034
FT                   /note="Enteropeptidase catalytic light chain"
FT                   /id="PRO_0000027726"
FT   TOPO_DOM        2..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..47
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..1034
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          54..169
FT                   /note="SEA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT   DOMAIN          197..238
FT                   /note="LDL-receptor class A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          240..349
FT                   /note="CUB 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          357..519
FT                   /note="MAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT   DOMAIN          539..649
FT                   /note="CUB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          656..694
FT                   /note="LDL-receptor class A 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          693..786
FT                   /note="SRCR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DOMAIN          800..1034
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        840
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        891
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        986
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        518
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        549
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        645
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        697
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        701
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        721
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        740
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        761
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        804
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        863
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        902
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        964
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        199..212
FT                   /evidence="ECO:0000250"
FT   DISULFID        206..225
FT                   /evidence="ECO:0000250"
FT   DISULFID        219..236
FT                   /evidence="ECO:0000250"
FT   DISULFID        240..268
FT                   /evidence="ECO:0000250"
FT   DISULFID        539..567
FT                   /evidence="ECO:0000250"
FT   DISULFID        658..670
FT                   /evidence="ECO:0000250"
FT   DISULFID        665..683
FT                   /evidence="ECO:0000250"
FT   DISULFID        677..692
FT                   /evidence="ECO:0000250"
FT   DISULFID        772..782
FT                   /evidence="ECO:0000250"
FT   DISULFID        787..911
FT                   /note="Interchain (between heavy and light chains)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT                   ECO:0000255|PROSITE-ProRule:PRU00124, ECO:0000255|PROSITE-
FT                   ProRule:PRU00196, ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        825..841
FT                   /evidence="ECO:0000250"
FT   DISULFID        925..992
FT                   /evidence="ECO:0000250"
FT   DISULFID        956..971
FT                   /evidence="ECO:0000250"
FT   DISULFID        982..1010
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1034 AA;  114776 MW;  0388C64CF64CC368 CRC64;
     MGSKRIIPSR HRSLSTYEVM FTALFAILMV LCAGLIAVSW LTIKGSEKDA ALGKSHEARG
     TMKITSGVTY NPNLQDKLSV DFKVLAFDIQ QMIGEIFQSS NLKNEYKNSR VLQFENGSVI
     VIFDLLFAQW VSDENIKEEL IQGIEANKSS QLVAFHIDVN SIDITESLEN YSTTSPSTTS
     DKLTTSSPPA TPGNVSIECL PGSRPCADAL KCIAVDLFCD GELNCPDGSD EDSKICATAC
     DGKFLLTESS GSFDAAQYPK LSEASVVCQW IIRVNQGLSI ELNFSYFNTY SMDVLNIYEG
     VGSSKILRAS LWLMNPGTIR IFSNQVTVTF LIESDENDYI GFNATYTAFN STELNNDEKI
     NCNFEDGFCF WIQDLNDDNE WERIQGTTFP PFTGPNFDHT FGNASGFYIS TPTGPGGRQE
     RVGLLSLPLE PTLEPVCLSF WYYMYGENVY KLSINISNDQ NIEKIIFQKE GNYGENWNYG
     QVTLNETVEF KVAFNAFKNQ FLSDIALDDI SLTYGICNVS LYPEPTLVPT SPPELPTDCG
     GPFELWEPNT TFTSMNFPNN YPNQAFCVWN LNAQKGKNIQ LHFEEFDLEN IADVVEIRDG
     EEDDSLLLAV YTGPGPVEDV FSTTNRMTVL FITNDALTKG GFKANFTTGY HLGIPEPCKE
     DNFQCENGEC VLLVNLCDGF SHCKDGSDEA HCVRFLNGTA NNSGLVQFRI QSIWHTACAE
     NWTTQTSDDV CQLLGLGTGN SSMPFFSSGG GPFVKLNTAP NGSLILTASE QCFEDSLILL
     QCNHKSCGKK QVAQEVSPKI VGGNDSREGA WPWVVALYYN GQLLCGASLV SRDWLVSAAH
     CVYGRNLEPS KWKAILGLHM TSNLTSPQIV TRLIDEIVIN PHYNRRRKDS DIAMMHLEFK
     VNYTDYIQPI CLPEENQVFP PGRICSIAGW GKVIYQGSPA DILQEADVPL LSNEKCQQQM
     PEYNITENMM CAGYEEGGID SCQGDSGGPL MCLENNRWLL AGVTSFGYQC ALPNRPGVYA
     RVPKFTEWIQ SFLH
//