ENTK_BOVIN
ID ENTK_BOVIN Reviewed; 1035 AA.
AC P98072;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
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 heavy chain;
DE Contains:
DE RecName: Full=Enteropeptidase catalytic light chain;
DE Flags: Precursor;
GN Name=TMPRSS15; Synonyms=ENTK, PRSS7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Duodenum;
RX PubMed=8052624; DOI=10.1073/pnas.91.16.7588;
RA Kitamoto Y., Yuan X., Wu Q., McCourt D.W., Sadler J.E.;
RT "Enterokinase, the initiator of intestinal digestion, is a mosaic protease
RT composed of a distinctive assortment of domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7588-7592(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 801-1035, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8226855; DOI=10.1016/s0021-9258(19)49464-7;
RA Lavallie E.R., Rehemtulla A., Racie L.A., Diblasio E.A., Ferenz C.,
RA Grant K.L., Light A., McCoy J.M.;
RT "Cloning and functional expression of a cDNA encoding the catalytic subunit
RT of bovine enterokinase.";
RL J. Biol. Chem. 268:23311-23317(1993).
RN [3]
RP PROTEIN SEQUENCE OF 801-827.
RC TISSUE=Intestine;
RX PubMed=1799406; DOI=10.1007/bf01025475;
RA Light A., Janska H.;
RT "The amino-terminal sequence of the catalytic subunit of bovine
RT enterokinase.";
RL J. Protein Chem. 10:475-480(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 788-1035 IN COMPLEX WITH
RP INHIBITOR, ACTIVE SITE, SUBUNIT, INTERCHAIN DISULFIDE BOND, AND MUTAGENESIS
RP OF LYS-889.
RX PubMed=10493881; DOI=10.1006/jmbi.1999.3089;
RA Lu D., Futterer K., Korolev S., Zheng X., Tan K., Waksman G., Sadler J.E.;
RT "Crystal structure of enteropeptidase light chain complexed with an analog
RT of the trypsinogen activation peptide.";
RL J. Mol. Biol. 292:361-373(1999).
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: Heterodimer of a catalytic (light) chain and a multidomain
CC (heavy) chain linked by a disulfide bond.
CC {ECO:0000269|PubMed:10493881}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P98072-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P98072-2; Sequence=VSP_005386;
CC -!- TISSUE SPECIFICITY: Intestinal brush border.
CC -!- PTM: The chains are derived from a single precursor that is cleaved by
CC a trypsin-like protease.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; U09859; AAB40026.1; -; mRNA.
DR EMBL; L19663; AAA16035.1; -; mRNA.
DR PIR; A43090; A43090.
DR RefSeq; NP_776864.1; NM_174439.2. [P98072-1]
DR PDB; 1EKB; X-ray; 2.30 A; A=788-800, B=801-1035.
DR PDBsum; 1EKB; -.
DR AlphaFoldDB; P98072; -.
DR SMR; P98072; -.
DR STRING; 9913.ENSBTAP00000000788; -.
DR MEROPS; S01.156; -.
DR PaxDb; P98072; -.
DR PRIDE; P98072; -.
DR GeneID; 282009; -.
DR KEGG; bta:282009; -.
DR CTD; 5651; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_011803_0_0_1; -.
DR InParanoid; P98072; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF351678; -.
DR BRENDA; 3.4.21.9; 908.
DR EvolutionaryTrace; P98072; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
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:0044256; P:protein digestion; TAS:AgBase.
DR GO; GO:0032023; P:trypsinogen activation; TAS:AgBase.
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 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipoprotein; Membrane; Myristate;
KW Protease; Reference proteome; Repeat; Serine protease; Signal-anchor;
KW Transmembrane; Transmembrane helix; Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..800
FT /note="Enteropeptidase non-catalytic heavy chain"
FT /id="PRO_0000027717"
FT CHAIN 801..1035
FT /note="Enteropeptidase catalytic light chain"
FT /id="PRO_0000027718"
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..1035
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..350
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 358..520
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 540..650
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 657..695
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 694..787
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 801..1035
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 841
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10493881"
FT ACT_SITE 892
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10493881"
FT ACT_SITE 987
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10493881"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
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 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 864
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 903
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 965
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..269
FT /evidence="ECO:0000250"
FT DISULFID 540..568
FT /evidence="ECO:0000250"
FT DISULFID 659..671
FT /evidence="ECO:0000250"
FT DISULFID 666..684
FT /evidence="ECO:0000250"
FT DISULFID 678..693
FT /evidence="ECO:0000250"
FT DISULFID 773..783
FT /evidence="ECO:0000250"
FT DISULFID 788..912
FT /note="Interchain (between heavy and light chains)"
FT DISULFID 826..842
FT /evidence="ECO:0000250"
FT DISULFID 926..993
FT /evidence="ECO:0000250"
FT DISULFID 957..972
FT /evidence="ECO:0000250"
FT DISULFID 983..1011
FT /evidence="ECO:0000250"
FT VAR_SEQ 166..192
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_005386"
FT MUTAGEN 889
FT /note="K->A: Prevents the cleavage of trypsinogen."
FT /evidence="ECO:0000269|PubMed:10493881"
FT CONFLICT 808
FT /note="R -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 815..820
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 823..830
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 832..838
FT /evidence="ECO:0007829|PDB:1EKB"
FT HELIX 840..843
FT /evidence="ECO:0007829|PDB:1EKB"
FT HELIX 850..852
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 853..858
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 871..880
FT /evidence="ECO:0007829|PDB:1EKB"
FT TURN 886..889
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 894..900
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 925..935
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 945..951
FT /evidence="ECO:0007829|PDB:1EKB"
FT HELIX 954..960
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 970..973
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 990..995
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 998..1007
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 1009..1012
FT /evidence="ECO:0007829|PDB:1EKB"
FT STRAND 1018..1022
FT /evidence="ECO:0007829|PDB:1EKB"
FT HELIX 1023..1025
FT /evidence="ECO:0007829|PDB:1EKB"
FT HELIX 1027..1031
FT /evidence="ECO:0007829|PDB:1EKB"
SQ SEQUENCE 1035 AA; 114887 MW; E207970B08296E13 CRC64;
MGSKRSVPSR HRSLTTYEVM FAVLFVILVA LCAGLIAVSW LSIQGSVKDA AFGKSHEARG
TLKIISGATY NPHLQDKLSV DFKVLAFDIQ QMIDDIFQSS NLKNEYKNSR VLQFENGSII
VIFDLLFDQW VSDKNVKEEL IQGIEANKSS QLVTFHIDLN SIDITASLEN FSTISPATTS
EKLTTSIPLA TPGNVSIECP PDSRLCADAL KCIAIDLFCD GELNCPDGSD EDNKTCATAC
DGRFLLTGSS GSFEALHYPK PSNNTSAVCR WIIRVNQGLS IQLNFDYFNT YYADVLNIYE
GMGSSKILRA SLWSNNPGII RIFSNQVTAT FLIQSDESDY IGFKVTYTAF NSKELNNYEK
INCNFEDGFC FWIQDLNDDN EWERTQGSTF PPSTGPTFDH TFGNESGFYI STPTGPGGRR
ERVGLLTLPL DPTPEQACLS FWYYMYGENV YKLSINISSD QNMEKTIFQK EGNYGQNWNY
GQVTLNETVE FKVSFYGFKN QILSDIALDD ISLTYGICNV SVYPEPTLVP TPPPELPTDC
GGPHDLWEPN TTFTSINFPN SYPNQAFCIW NLNAQKGKNI QLHFQEFDLE NIADVVEIRD
GEGDDSLFLA VYTGPGPVND VFSTTNRMTV LFITDNMLAK QGFKANFTTG YGLGIPEPCK
EDNFQCKDGE CIPLVNLCDG FPHCKDGSDE AHCVRLFNGT TDSSGLVQFR IQSIWHVACA
ENWTTQISDD VCQLLGLGTG NSSVPTFSTG GGPYVNLNTA PNGSLILTPS QQCLEDSLIL
LQCNYKSCGK KLVTQEVSPK IVGGSDSREG AWPWVVALYF DDQQVCGASL VSRDWLVSAA
HCVYGRNMEP SKWKAVLGLH MASNLTSPQI ETRLIDQIVI NPHYNKRRKN NDIAMMHLEM
KVNYTDYIQP ICLPEENQVF PPGRICSIAG WGALIYQGST ADVLQEADVP LLSNEKCQQQ
MPEYNITENM VCAGYEAGGV DSCQGDSGGP LMCQENNRWL LAGVTSFGYQ CALPNRPGVY
ARVPRFTEWI QSFLH
