ENTK_PIG
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 03-AUG-2022, entry version 146.
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.ENSSSCP00000012801; -.
DR MEROPS; S01.156; -.
DR PaxDb; P98074; -.
DR GeneID; 397152; -.
DR KEGG; ssc:397152; -.
DR CTD; 5651; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P98074; -.
DR OrthoDB; 1314811at2759; -.
DR BRENDA; 3.4.21.9; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
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; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 3.10.250.10; -; 1.
DR Gene3D; 3.30.70.960; -; 1.
DR Gene3D; 4.10.400.10; -; 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 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; SSF49854; SSF49854; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR SUPFAM; SSF57424; SSF57424; 2.
DR SUPFAM; SSF82671; SSF82671; 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
