ENTK_MOUSE
ID ENTK_MOUSE Reviewed; 1069 AA.
AC P97435; Q148Y3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
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;
GN Name=Tmprss15; Synonyms=Entk, Prss7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Duodenum;
RX PubMed=9486188; DOI=10.1152/ajpgi.1998.274.2.g342;
RA Yuan X., Zheng X., Lu D., Rubin D.C., Pung C.Y.M., Sadler J.E.;
RT "Structure of murine enterokinase (enteropeptidase) and expression in small
RT intestine during development.";
RL Am. J. Physiol. 274:G342-G349(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; U73378; AAB37317.1; -; mRNA.
DR EMBL; BC117917; AAI17918.1; -; mRNA.
DR EMBL; BC117918; AAI17919.1; -; mRNA.
DR CCDS; CCDS28280.1; -.
DR RefSeq; NP_032967.1; NM_008941.3.
DR RefSeq; NP_849186.2; NM_178855.4.
DR AlphaFoldDB; P97435; -.
DR SMR; P97435; -.
DR STRING; 10090.ENSMUSP00000023566; -.
DR MEROPS; S01.156; -.
DR GlyGen; P97435; 16 sites.
DR iPTMnet; P97435; -.
DR PhosphoSitePlus; P97435; -.
DR MaxQB; P97435; -.
DR PaxDb; P97435; -.
DR PRIDE; P97435; -.
DR ProteomicsDB; 275916; -.
DR Antibodypedia; 2519; 236 antibodies from 29 providers.
DR DNASU; 19146; -.
DR Ensembl; ENSMUST00000023566; ENSMUSP00000023566; ENSMUSG00000022857.
DR GeneID; 19146; -.
DR KEGG; mmu:19146; -.
DR UCSC; uc007zsy.2; mouse.
DR CTD; 5651; -.
DR MGI; MGI:1197523; Tmprss15.
DR VEuPathDB; HostDB:ENSMUSG00000022857; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000159353; -.
DR InParanoid; P97435; -.
DR OMA; PSQQCLQ; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P97435; -.
DR TreeFam; TF351678; -.
DR BioGRID-ORCS; 19146; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Tmprss15; mouse.
DR PRO; PR:P97435; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P97435; protein.
DR Bgee; ENSMUSG00000022857; Expressed in duodenum and 20 other tissues.
DR ExpressionAtlas; P97435; baseline and differential.
DR Genevisible; P97435; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Repeat; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zymogen.
FT CHAIN 1..829
FT /note="Enteropeptidase non-catalytic heavy chain"
FT /id="PRO_0000027721"
FT CHAIN 830..1069
FT /note="Enteropeptidase catalytic light chain"
FT /id="PRO_0000027722"
FT TOPO_DOM 1..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..1069
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 54..169
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 227..268
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 270..379
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 387..549
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 569..679
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 686..724
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 723..816
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 830..1069
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 874
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 925
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 1021
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 936
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 999
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 229..242
FT /evidence="ECO:0000250"
FT DISULFID 236..255
FT /evidence="ECO:0000250"
FT DISULFID 249..266
FT /evidence="ECO:0000250"
FT DISULFID 270..298
FT /evidence="ECO:0000250"
FT DISULFID 569..597
FT /evidence="ECO:0000250"
FT DISULFID 688..700
FT /evidence="ECO:0000250"
FT DISULFID 695..713
FT /evidence="ECO:0000250"
FT DISULFID 707..722
FT /evidence="ECO:0000250"
FT DISULFID 802..812
FT /evidence="ECO:0000250"
FT DISULFID 817..945
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 859..875
FT /evidence="ECO:0000250"
FT DISULFID 959..1027
FT /evidence="ECO:0000250"
FT DISULFID 991..1006
FT /evidence="ECO:0000250"
FT DISULFID 1017..1045
FT /evidence="ECO:0000250"
SQ SEQUENCE 1069 AA; 118735 MW; E62549E463743C3D CRC64;
MKSSRDEAVG HHSISSFEVM LSALFIMLMV FSIGLIAVSW LAVKESEGDA ALGKSHEVRG
TFKITSGVTY NPNLQDKHSV DFKVLAFDLQ QMIDEIFESS SLKNEYEKSK VFQFEKGSVI
VLFDLFFAQW VSDKNVKEEL IQGIEANISS QLVTLHIDLN SIDITASLSD FTTAVPVTTS
DKLTTSSPMT TSASLGNLST TVAATTSAPL CNLSTATFAT TSGHVSIECQ PGSRPCAHAW
NCVATDLFCD GEVNCPDGSD EDTGLCATAC DGRFLLTGDS GVFQADRYPR PDESGVVCRW
IIRVNQGLSI RMNFGSFIPH YTDVLDIYEG IGPSKILRGS FWETDPGTIR IFSNLVTVTF
LIKSDEYDYI GFNATYSTFN NSELNNYEKI DCTFDDGFCF WTQDLDDDNE WERIQVTTFP
CYTGPRFDHT YGNGSGFYIS TPTEQGWRSE RVGLSSLSLD LTSEPVCLHF WYYMCCENVY
NLNIHISSAE TTDKIVFQRK GNYGRNWNYG QVTLNETGEF KVVFNAFRNR GCSTIALDDI
SLTNGICSQS PYPEPTLVPT PPPELPTDCG GPFELWEPNS TFSSPNFPDK YPNQASCIWN
LNAQRGKNIQ LHFQEFDLEN INDVVEVRDG GEFDSLLLAV YTGPGPVKDL FSTTNRMTVI
FTTNMETRRK GFKANFTSGY YLGIPEPCQD DEFQCKDGNC IPLGNLCDSY PHCRDGSDEA
SCVRFLNGTR SNNGLVQFNI HSIWHIACAE NWTTQISNEV CHLLGLGSAN SSMPISSTGG
GPFVRVNQAP NGSLILTPSL QCSQDSLILL QCNHKSCGEK KVTQKVSPKI VGGSDAQAGA
WPWVVALYHR DRSTDRLLCG ASLVSSDWLV SAAHCVYRRN LDPTRWTAVL GLHMQSNLTS
PQVVRRVVDQ IVINPHYDRR RKVNDIAMMH LEFKVNYTDY IQPICLPEEN QIFIPGRTCS
IAGWGYDKIN AGSTVDVLKE ADVPLISNEK CQQQLPEYNI TESMICAGYE EGGIDSCQGD
SGGPLMCQEN NRWFLVGVTS FGVQCALPNH PGVYVRVSQF IEWIHSFLH
