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Reviewed, UniProtKB/Swiss-Prot P97435 (ENTK_MOUSE)

Last modified June 16, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Enteropeptidase
    EC=3.4.21.9
Alternative name(s):
    Enterokinase
    Serine protease 7
Cleaved into the following 2 chains:
    1- Recommended name:
            Enteropeptidase non-catalytic heavy chain
    2- Recommended name:
            Enteropeptidase catalytic light chain
Gene names
Name: Prss7
Synonyms: Entk
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length1069 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

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 By similarity.

Catalytic activity

Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond.

Subunit structure

Heterodimer of a catalytic (light) chain and a multidomain (heavy) chain linked by a disulfide bond By similarity.

Subcellular location

Membrane; Single-pass type II membrane protein Probable.

Post-translational modification

The chains are derived from a single precursor that is cleaved by a trypsin-like protease By similarity.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 CUB domains.

Contains 2 LDL-receptor class A domains.

Contains 1 MAM domain.

Contains 1 peptidase S1 domain.

Contains 1 SEA domain.

Contains 1 SRCR domain.

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Ontologies

Keywords
   Cellular componentMembrane
   DomainRepeat
Signal-anchor
Transmembrane
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionscavenger receptor activity

Inferred from electronic annotation. Source: InterPro

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 829829Enteropeptidase non-catalytic heavy chain
PRO_0000027721
Chain830 – 1069240Enteropeptidase catalytic light chain
PRO_0000027722

Regions

Topological domain1 – 1818Cytoplasmic Potential
Transmembrane19 – 4729Signal-anchor for type II membrane protein Potential
Topological domain48 – 10691022Extracellular Potential
Domain52 – 169118SEA
Domain227 – 26842LDL-receptor class A 1
Domain270 – 379110CUB 1
Domain387 – 549163MAM
Domain569 – 679111CUB 2
Domain686 – 72439LDL-receptor class A 2
Domain723 – 81694SRCR
Domain830 – 1069240Peptidase S1

Sites

Active site8741Charge relay system By similarity
Active site9251Charge relay system By similarity
Active site10211Charge relay system By similarity

Amino acid modifications

Glycosylation1471N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation3731N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Glycosylation5791N-linked (GlcNAc...) Potential
Glycosylation6751N-linked (GlcNAc...) Potential
Glycosylation7271N-linked (GlcNAc...) Potential
Glycosylation7511N-linked (GlcNAc...) Potential
Glycosylation7701N-linked (GlcNAc...) Potential
Glycosylation7911N-linked (GlcNAc...) Potential
Glycosylation8971N-linked (GlcNAc...) Potential
Glycosylation9361N-linked (GlcNAc...) Potential
Glycosylation9991N-linked (GlcNAc...) Potential
Disulfide bond229 ↔ 242 By similarity
Disulfide bond236 ↔ 255 By similarity
Disulfide bond249 ↔ 266 By similarity
Disulfide bond270 ↔ 298 By similarity
Disulfide bond569 ↔ 597 By similarity
Disulfide bond688 ↔ 700 By similarity
Disulfide bond695 ↔ 713 By similarity
Disulfide bond707 ↔ 722 By similarity
Disulfide bond802 ↔ 812 By similarity
Disulfide bond817 ↔ 945Interchain (between heavy and light chains) By similarity
Disulfide bond859 ↔ 875 By similarity
Disulfide bond959 ↔ 1027 By similarity
Disulfide bond991 ↔ 1006 By similarity
Disulfide bond1017 ↔ 1045 By similarity

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Sequences

Sequence LengthMass (Da)Tools
P97435-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: E62549E463743C3D

FASTA1,069118,735
        10         20         30         40         50         60 
MKSSRDEAVG HHSISSFEVM LSALFIMLMV FSIGLIAVSW LAVKESEGDA ALGKSHEVRG 

        70         80         90        100        110        120 
TFKITSGVTY NPNLQDKHSV DFKVLAFDLQ QMIDEIFESS SLKNEYEKSK VFQFEKGSVI 

       130        140        150        160        170        180 
VLFDLFFAQW VSDKNVKEEL IQGIEANISS QLVTLHIDLN SIDITASLSD FTTAVPVTTS 

       190        200        210        220        230        240 
DKLTTSSPMT TSASLGNLST TVAATTSAPL CNLSTATFAT TSGHVSIECQ PGSRPCAHAW 

       250        260        270        280        290        300 
NCVATDLFCD GEVNCPDGSD EDTGLCATAC DGRFLLTGDS GVFQADRYPR PDESGVVCRW 

       310        320        330        340        350        360 
IIRVNQGLSI RMNFGSFIPH YTDVLDIYEG IGPSKILRGS FWETDPGTIR IFSNLVTVTF 

       370        380        390        400        410        420 
LIKSDEYDYI GFNATYSTFN NSELNNYEKI DCTFDDGFCF WTQDLDDDNE WERIQVTTFP 

       430        440        450        460        470        480 
CYTGPRFDHT YGNGSGFYIS TPTEQGWRSE RVGLSSLSLD LTSEPVCLHF WYYMCCENVY 

       490        500        510        520        530        540 
NLNIHISSAE TTDKIVFQRK GNYGRNWNYG QVTLNETGEF KVVFNAFRNR GCSTIALDDI 

       550        560        570        580        590        600 
SLTNGICSQS PYPEPTLVPT PPPELPTDCG GPFELWEPNS TFSSPNFPDK YPNQASCIWN 

       610        620        630        640        650        660 
LNAQRGKNIQ LHFQEFDLEN INDVVEVRDG GEFDSLLLAV YTGPGPVKDL FSTTNRMTVI 

       670        680        690        700        710        720 
FTTNMETRRK GFKANFTSGY YLGIPEPCQD DEFQCKDGNC IPLGNLCDSY PHCRDGSDEA 

       730        740        750        760        770        780 
SCVRFLNGTR SNNGLVQFNI HSIWHIACAE NWTTQISNEV CHLLGLGSAN SSMPISSTGG 

       790        800        810        820        830        840 
GPFVRVNQAP NGSLILTPSL QCSQDSLILL QCNHKSCGEK KVTQKVSPKI VGGSDAQAGA 

       850        860        870        880        890        900 
WPWVVALYHR DRSTDRLLCG ASLVSSDWLV SAAHCVYRRN LDPTRWTAVL GLHMQSNLTS 

       910        920        930        940        950        960 
PQVVRRVVDQ IVINPHYDRR RKVNDIAMMH LEFKVNYTDY IQPICLPEEN QIFIPGRTCS 

       970        980        990       1000       1010       1020 
IAGWGYDKIN AGSTVDVLKE ADVPLISNEK CQQQLPEYNI TESMICAGYE EGGIDSCQGD 

      1030       1040       1050       1060 
SGGPLMCQEN NRWFLVGVTS FGVQCALPNH PGVYVRVSQF IEWIHSFLH

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References

[1]"Structure of murine enterokinase (enteropeptidase) and expression in small intestine during development."
Yuan X., Zheng X., Lu D., Rubin D.C., Pung C.Y.M., Sadler J.E.
Am. J. Physiol. 274:G342-G349(1998) [PubMed: 9486188] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Duodenum.
+Additional computationally mapped references.

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Cross-references

Sequence databases

U73378 mRNA. Translation: AAB37317.1.
IPIIPI00125354.
RefSeqNP_032967.1.
UniGeneMm.5184

3D structure databases

HSSPHSSP built from PDB template 1EKB based on UniProtKB P98072.
ModBaseSearch...

Protein family/group databases

MEROPSS01.156.

Genome annotation databases

EnsemblENSMUSG00000022857. Mus musculus. [Contig view]
GeneID19146.
KEGGmmu:19146.

Organism-specific databases

MGIMGI:1197523. Prss7.

Phylogenomic databases

HOGENOMP97435.
HOVERGENP97435.
OMAP97435. IRIFSNQ.

Enzyme and pathway databases

BRENDA3.4.21.9. 244.

Gene expression databases

BgeeP97435.
CleanExMM_PRSS7.
GermOnlineENSMUSG00000022857. Mus musculus.

Family and domain databases

InterProIPR000859. CUB.
IPR002172. LDL_rcpt_classA_cys-rich.
IPR000998. MAM.
IPR011163. Pept_S1A_enterop.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR000082. SEA.
IPR001190. Srcr_rcpt.
IPR017448. Srcr_rcpt-rel.
[Graphical view]
Gene3DG3DSA:2.60.120.290. CUB. 2 hits.
G3DSA:4.10.400.10. LDL_rcpt_classA_cys-rich. 1 hit.
PfamPF00431. CUB. 2 hits.
PF00057. Ldl_recept_a. 1 hit.
PF00629. MAM. 1 hit.
PF01390. SEA. 1 hit.
PF00530. SRCR. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001138. Enteropeptidase. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00261. LDLRECEPTOR.
SMARTSM00042. CUB. 2 hits.
SM00192. LDLa. 2 hits.
SM00137. MAM. 1 hit.
SM00200. SEA. 1 hit.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS01180. CUB. 2 hits.
PS01209. LDLRA_1. 2 hits.
PS50068. LDLRA_2. 2 hits.
PS00740. MAM_1. 1 hit.
PS50060. MAM_2. 1 hit.
PS50024. SEA. 1 hit.
PS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio295786.
SOURCESearch...

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Entry information

Entry nameENTK_MOUSE
AccessionPrimary (citable) accession number: P97435
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: June 16, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents