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Enteropeptidase (EC 3.4.21.9) (Enterokinase) (Serine protease 7) (Transmembrane protease serine 15) [Cleaved into: Enteropeptidase non-catalytic mini chain; Enteropeptidase non-catalytic heavy chain; Enteropeptidase catalytic light chain]

 ENTK_PIG                Reviewed;        1034 AA.
P98074;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 135.
RecName: Full=Enteropeptidase;
EC=3.4.21.9;
AltName: Full=Enterokinase;
AltName: Full=Serine protease 7;
AltName: Full=Transmembrane protease serine 15;
Contains:
RecName: Full=Enteropeptidase non-catalytic mini chain;
Contains:
RecName: Full=Enteropeptidase non-catalytic heavy chain;
Contains:
RecName: Full=Enteropeptidase catalytic light chain;
Flags: Precursor;
Name=TMPRSS15; Synonyms=ENTK, PRSS7;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Duodenal mucosa;
PubMed=8051081;
Matsushima M., Ichinose M., Yahagi N., Kakei N., Tsukada S., Miki K.,
Kurokawa K., Tashiro K., Shiokawa K., Shinomiya K., Umeyama H.,
Inoue H., Takahashi T., Takahashi K.;
"Structural characterization of porcine enteropeptidase.";
J. Biol. Chem. 269:19976-19982(1994).
-!- FUNCTION: Responsible for initiating activation of pancreatic
proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase
A). It catalyzes the conversion of trypsinogen to trypsin which in
turn activates other proenzymes including chymotrypsinogen,
procarboxypeptidases, and proelastases.
-!- CATALYTIC ACTIVITY: Activation of trypsinogen by selective
cleavage of 6-Lys-|-Ile-7 bond.
-!- SUBUNIT: Heterotrimer of a catalytic (light) chain, a multidomain
(heavy) chain, and a mini chain.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}.
-!- PTM: The chains are derived from a single precursor that is
cleaved by a trypsin-like protease.
-!- PTM: The mini chain may be cleaved by elastase.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; D30799; BAA06459.1; -; mRNA.
PIR; A53663; A53663.
RefSeq; NP_001001259.1; NM_001001259.1.
UniGene; Ssc.298; -.
ProteinModelPortal; P98074; -.
SMR; P98074; -.
STRING; 9823.ENSSSCP00000012801; -.
MEROPS; S01.156; -.
PaxDb; P98074; -.
PRIDE; P98074; -.
GeneID; 397152; -.
KEGG; ssc:397152; -.
CTD; 5651; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000112380; -.
HOVERGEN; HBG005588; -.
InParanoid; P98074; -.
KO; K01316; -.
BRENDA; 3.4.21.9; 6170.
Proteomes; UP000008227; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
CDD; cd00041; CUB; 2.
CDD; cd00112; LDLa; 2.
CDD; cd06263; MAM; 1.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.60.120.290; -; 2.
Gene3D; 3.10.250.10; -; 1.
Gene3D; 3.30.70.960; -; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR000859; CUB_dom.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR000998; MAM_dom.
InterPro; IPR011163; Pept_S1A_enterop.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR000082; SEA_dom.
InterPro; IPR036364; SEA_dom_sf.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR001190; SRCR.
InterPro; IPR017448; SRCR-like_dom.
InterPro; IPR036772; SRCR-like_dom_sf.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00431; CUB; 2.
Pfam; PF00057; Ldl_recept_a; 1.
Pfam; PF00629; MAM; 1.
Pfam; PF01390; SEA; 1.
Pfam; PF00530; SRCR; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001138; Enteropeptidase; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00042; CUB; 2.
SMART; SM00192; LDLa; 2.
SMART; SM00137; MAM; 1.
SMART; SM00200; SEA; 1.
SMART; SM00202; SR; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF49854; SSF49854; 2.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF56487; SSF56487; 1.
SUPFAM; SSF57424; SSF57424; 2.
SUPFAM; SSF82671; SSF82671; 1.
PROSITE; PS01180; CUB; 2.
PROSITE; PS01209; LDLRA_1; 2.
PROSITE; PS50068; LDLRA_2; 2.
PROSITE; PS00740; MAM_1; 1.
PROSITE; PS50060; MAM_2; 1.
PROSITE; PS50024; SEA; 1.
PROSITE; PS00420; SRCR_1; 1.
PROSITE; PS50287; SRCR_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome;
Repeat; Serine protease; Signal-anchor; Transmembrane;
Transmembrane helix; Zymogen.
PROPEP 1 51
/FTId=PRO_0000027723.
CHAIN 52 117 Enteropeptidase non-catalytic mini chain.
/FTId=PRO_0000027724.
CHAIN 118 799 Enteropeptidase non-catalytic heavy
chain.
/FTId=PRO_0000027725.
CHAIN 800 1034 Enteropeptidase catalytic light chain.
/FTId=PRO_0000027726.
TOPO_DOM 2 18 Cytoplasmic. {ECO:0000255}.
TRANSMEM 19 47 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 48 1034 Extracellular. {ECO:0000255}.
DOMAIN 54 169 SEA. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
DOMAIN 197 238 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 240 349 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 357 519 MAM. {ECO:0000255|PROSITE-
ProRule:PRU00128}.
DOMAIN 539 649 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 656 694 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 693 786 SRCR. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 800 1034 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 840 840 Charge relay system. {ECO:0000250}.
ACT_SITE 891 891 Charge relay system. {ECO:0000250}.
ACT_SITE 986 986 Charge relay system. {ECO:0000250}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 194 194 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 343 343 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 403 403 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 455 455 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 485 485 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 518 518 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 549 549 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 645 645 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 697 697 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 701 701 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 721 721 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 740 740 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 761 761 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 804 804 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 863 863 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 902 902 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 964 964 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 199 212 {ECO:0000250}.
DISULFID 206 225 {ECO:0000250}.
DISULFID 219 236 {ECO:0000250}.
DISULFID 240 268 {ECO:0000250}.
DISULFID 539 567 {ECO:0000250}.
DISULFID 658 670 {ECO:0000250}.
DISULFID 665 683 {ECO:0000250}.
DISULFID 677 692 {ECO:0000250}.
DISULFID 772 782 {ECO:0000250}.
DISULFID 787 911 Interchain (between heavy and light
chains). {ECO:0000255|PROSITE-
ProRule:PRU00059, ECO:0000255|PROSITE-
ProRule:PRU00124, ECO:0000255|PROSITE-
ProRule:PRU00196, ECO:0000255|PROSITE-
ProRule:PRU00274}.
DISULFID 825 841 {ECO:0000250}.
DISULFID 925 992 {ECO:0000250}.
DISULFID 956 971 {ECO:0000250}.
DISULFID 982 1010 {ECO:0000250}.
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


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