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   27-MAR-2024, entry version 189.
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   GlyCosmos; P97435; 16 sites, No reported glycans.
DR   GlyGen; P97435; 16 sites.
DR   iPTMnet; P97435; -.
DR   PhosphoSitePlus; P97435; -.
DR   MaxQB; P97435; -.
DR   PaxDb; 10090-ENSMUSP00000023566; -.
DR   ProteomicsDB; 275916; -.
DR   Antibodypedia; 2519; 257 antibodies from 29 providers.
DR   DNASU; 19146; -.
DR   Ensembl; ENSMUST00000023566.11; ENSMUSP00000023566.5; ENSMUSG00000022857.14.
DR   GeneID; 19146; -.
DR   KEGG; mmu:19146; -.
DR   UCSC; uc007zsy.2; mouse.
DR   AGR; MGI:1197523; -.
DR   CTD; 5651; -.
DR   MGI; MGI:1197523; Tmprss15.
DR   VEuPathDB; HostDB:ENSMUSG00000022857; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000159353; -.
DR   InParanoid; P97435; -.
DR   OMA; THGICNG; -.
DR   OrthoDB; 4252799at2759; -.
DR   PhylomeDB; P97435; -.
DR   TreeFam; TF351678; -.
DR   BioGRID-ORCS; 19146; 4 hits in 79 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 cell types or tissues.
DR   ExpressionAtlas; P97435; baseline and differential.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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; 2.60.120.200; -; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR   Gene3D; 3.30.70.960; SEA domain; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF15; TRANSMEMBRANE SERINE PROTEASE 15; 1.
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; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 2.
DR   SUPFAM; SSF82671; SEA domain; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   SUPFAM; SSF56487; SRCR-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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.
DR   Genevisible; P97435; MM.
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
//