ID ENTK_BOVIN STANDARD; PRT; 1035 AA. AC P98072; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE ENTEROPEPTIDASE PRECURSOR (EC 3.4.21.9) (ENTEROKINASE). GN PRSS7 OR ENTK. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=DUODENUM; RX MEDLINE=94329561; PubMed=8052624; RA Kitamoto Y., Yuan X., Wu Q., McCourt D.W., Sadler J.E.; RT "Enterokinase, the initiator of intestinal digestion, is a mosaic RT protease composed of a distinctive assortment of domains."; RL Proc. Natl. Acad. Sci. U.S.A. 91:7588-7592(1994). RN [2] RP SEQUENCE OF 801-1035 FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=94043122; PubMed=8226855; 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 RT subunit of bovine enterokinase."; RL J. Biol. Chem. 268:23311-23317(1993). RN [3] RP SEQUENCE OF 801-827. RC TISSUE=INTESTINE; RX MEDLINE=92189715; PubMed=1799406; 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). CC -!- FUNCTION: RESPONSIBLE FOR INITIATING ACTIVATION OF PANCREATIC CC PROTEOLYTIC PROENZYMES (TRYPSIN, CHYMOTRYPSIN AND CARBOXYPEPTIDASE CC A). IT CATALYZES THE CONVERSION OF TRYPSINOGEN TO TRYPSIN WHICH IN CC TURN ACTIVATES OTHER PROENZYMES INCLUDING CHYMOTRYPSINOGEN, CC PROCARBOXYPEPTIDASES, AND PROELASTASES. CC -!- CATALYTIC ACTIVITY: SELECTIVE CLEAVAGE OF 6-LYS-|-ILE-7 BOND IN CC TRYPSINOGEN. CC -!- SUBUNIT: HETERODIMER OF A CATALYTIC (LIGHT) CHAIN AND A CC MULTIDOMAIN (HEAVY) CHAIN LINKED BY A DISULFIDE BOND. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN (PROBABLE). CC -!- TISSUE SPECIFICITY: INTESTINAL BRUSH BORDER. CC -!- PTM: THE CHAINS ARE DERIVED FROM A SINGLE PRECURSOR THAT IS CC CLEAVED BY A TRYPSIN-LIKE PROTEASE. CC -!- SIMILARITY: CONTAINS 2 LDL-RECEPTOR CLASS A DOMAINS. CC -!- SIMILARITY: CONTAINS 2 CUB DOMAINS. CC -!- SIMILARITY: CONTAINS 1 SRCR DOMAIN. CC -!- SIMILARITY: CONTAINS 1 MAM DOMAIN. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1; ALSO KNOWN AS THE CC TRYPSIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U09859; AAB40026.1; -. DR EMBL; L19663; AAA16035.1; -. DR PIR; A61436; A61436. DR HSSP; P00763; 1DPO. DR MEROPS; S01.156; -. DR INTERPRO; IPR000082; -. DR INTERPRO; IPR000859; -. DR INTERPRO; IPR000998; -. DR INTERPRO; IPR001190; -. DR INTERPRO; IPR001254; -. DR INTERPRO; IPR001314; -. DR INTERPRO; IPR002172; -. DR PFAM; PF00431; CUB; 2. DR PFAM; PF00629; MAM; 1. DR PFAM; PF01390; SEA; 1. DR PFAM; PF00530; SRCR; 1. DR PFAM; PF00057; ldl_recept_a; 2. DR PFAM; PF00089; trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR PROSITE; PS01180; CUB; 2. DR PROSITE; PS00740; MAM_1; 1. DR PROSITE; PS50060; MAM_2; 1. DR PROSITE; PS01209; LDLRA_1; 2. DR PROSITE; PS50068; LDLRA_2; 2. KW Signal-anchor; Glycoprotein; Myristate; Hydrolase; KW Serine protease; Zymogen; Transmembrane; Repeat; Alternative splicing. FT CHAIN 1 800 NON-CATALYTIC CHAIN (HEAVY CHAIN). FT CHAIN 801 1035 CATALYTIC CHAIN (LIGHT CHAIN). FT TRANSMEM 19 47 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN). FT DOMAIN 197 238 LDL-RECEPTOR CLASS A 1. FT DOMAIN 240 350 CUB. FT DOMAIN 358 520 MAM. FT DOMAIN 540 650 CUB. FT DOMAIN 657 695 LDL-RECEPTOR CLASS A 2. FT DOMAIN 694 787 SRCR. FT ACT_SITE 841 841 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 892 892 CHARGE RELAY SYSTEM (BY SIMILARITY). FT ACT_SITE 987 987 CHARGE RELAY SYSTEM (BY SIMILARITY). FT LIPID 2 2 MYRISTATE (POTENTIAL). FT DISULFID 199 212 BY SIMILARITY. FT DISULFID 206 225 BY SIMILARITY. FT DISULFID 219 236 BY SIMILARITY. FT DISULFID 659 671 BY SIMILARITY. FT DISULFID 666 684 BY SIMILARITY. FT DISULFID 678 693 BY SIMILARITY. FT DISULFID 788 912 INTERCHAIN (BY SIMILARITY). FT DISULFID 826 842 BY SIMILARITY. FT DISULFID 926 993 BY SIMILARITY. FT DISULFID 957 972 BY SIMILARITY. FT DISULFID 983 1011 BY SIMILARITY. FT CARBOHYD 116 116 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 147 147 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 170 170 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 194 194 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 233 233 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 263 263 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 264 264 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 404 404 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 456 456 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 486 486 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 519 519 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 550 550 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 646 646 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 698 698 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 722 722 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 741 741 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 762 762 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 864 864 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 903 903 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 965 965 N-LINKED (GLCNAC...) (POTENTIAL). FT VARSPLIC 166 192 MISSING (IN SHORT ISOFORM). FT CONFLICT 808 808 R -> Y (IN REF. 3). 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 //