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Reviewed, UniProtKB/Swiss-Prot P98074 (ENTK_PIG)

Last modified March 24, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 3 chains:
    1- Recommended name:
            Enteropeptidase non-catalytic mini chain
    2- Recommended name:
            Enteropeptidase non-catalytic heavy chain
    3- Recommended name:
            Enteropeptidase catalytic light chain
Gene names
Name: PRSS7
Synonyms: ENTK
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length1034 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Catalytic activity

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

Subunit structure

Heterotrimer of a catalytic (light) chain, a multidomain (heavy) chain, and a mini chain.

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.

The mini chain may be cleaved by elastase.

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
Lipoprotein
Myristate
Zymogen
   Technical termDirect protein sequencing
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

Propeptide1 – 5151
PRO_0000027723
Chain52 – 11766Enteropeptidase non-catalytic mini chain
PRO_0000027724
Chain118 – 799682Enteropeptidase non-catalytic heavy chain
PRO_0000027725
Chain800 – 1034235Enteropeptidase catalytic light chain
PRO_0000027726

Regions

Topological domain1 – 1818Cytoplasmic Potential
Transmembrane19 – 4729Signal-anchor for type II membrane protein Potential
Topological domain48 – 1034987Extracellular Potential
Domain52 – 169118SEA
Domain197 – 23842LDL-receptor class A 1
Domain240 – 349110CUB 1
Domain357 – 519163MAM
Domain539 – 649111CUB 2
Domain656 – 69439LDL-receptor class A 2
Domain693 – 78694SRCR
Domain800 – 1034235Peptidase S1

Sites

Active site8401Charge relay system By similarity
Active site8911Charge relay system By similarity
Active site9861Charge relay system By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1471N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential
Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Glycosylation5181N-linked (GlcNAc...) Potential
Glycosylation5491N-linked (GlcNAc...) Potential
Glycosylation6451N-linked (GlcNAc...) Potential
Glycosylation6971N-linked (GlcNAc...) Potential
Glycosylation7011N-linked (GlcNAc...) Potential
Glycosylation7211N-linked (GlcNAc...) Potential
Glycosylation7401N-linked (GlcNAc...) Potential
Glycosylation7611N-linked (GlcNAc...) Potential
Glycosylation8041N-linked (GlcNAc...) Potential
Glycosylation8631N-linked (GlcNAc...) Potential
Glycosylation9021N-linked (GlcNAc...) Potential
Glycosylation9641N-linked (GlcNAc...) Potential
Disulfide bond199 ↔ 212 By similarity
Disulfide bond206 ↔ 225 By similarity
Disulfide bond219 ↔ 236 By similarity
Disulfide bond240 ↔ 268 By similarity
Disulfide bond539 ↔ 567 By similarity
Disulfide bond658 ↔ 670 By similarity
Disulfide bond665 ↔ 683 By similarity
Disulfide bond677 ↔ 692 By similarity
Disulfide bond772 ↔ 782 By similarity
Disulfide bond787 ↔ 911Interchain (between heavy and light chains) By similarity
Disulfide bond825 ↔ 841 By similarity
Disulfide bond925 ↔ 992 By similarity
Disulfide bond956 ↔ 971 By similarity
Disulfide bond982 ↔ 1010 By similarity

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Sequences

Sequence LengthMass (Da)Tools
P98074-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 0388C64CF64CC368

FASTA1,034114,776
        10         20         30         40         50         60 
MGSKRIIPSR HRSLSTYEVM FTALFAILMV LCAGLIAVSW LTIKGSEKDA ALGKSHEARG 

        70         80         90        100        110        120 
TMKITSGVTY NPNLQDKLSV DFKVLAFDIQ QMIGEIFQSS NLKNEYKNSR VLQFENGSVI 

       130        140        150        160        170        180 
VIFDLLFAQW VSDENIKEEL IQGIEANKSS QLVAFHIDVN SIDITESLEN YSTTSPSTTS 

       190        200        210        220        230        240 
DKLTTSSPPA TPGNVSIECL PGSRPCADAL KCIAVDLFCD GELNCPDGSD EDSKICATAC 

       250        260        270        280        290        300 
DGKFLLTESS GSFDAAQYPK LSEASVVCQW IIRVNQGLSI ELNFSYFNTY SMDVLNIYEG 

       310        320        330        340        350        360 
VGSSKILRAS LWLMNPGTIR IFSNQVTVTF LIESDENDYI GFNATYTAFN STELNNDEKI 

       370        380        390        400        410        420 
NCNFEDGFCF WIQDLNDDNE WERIQGTTFP PFTGPNFDHT FGNASGFYIS TPTGPGGRQE 

       430        440        450        460        470        480 
RVGLLSLPLE PTLEPVCLSF WYYMYGENVY KLSINISNDQ NIEKIIFQKE GNYGENWNYG 

       490        500        510        520        530        540 
QVTLNETVEF KVAFNAFKNQ FLSDIALDDI SLTYGICNVS LYPEPTLVPT SPPELPTDCG 

       550        560        570        580        590        600 
GPFELWEPNT TFTSMNFPNN YPNQAFCVWN LNAQKGKNIQ LHFEEFDLEN IADVVEIRDG 

       610        620        630        640        650        660 
EEDDSLLLAV YTGPGPVEDV FSTTNRMTVL FITNDALTKG GFKANFTTGY HLGIPEPCKE 

       670        680        690        700        710        720 
DNFQCENGEC VLLVNLCDGF SHCKDGSDEA HCVRFLNGTA NNSGLVQFRI QSIWHTACAE 

       730        740        750        760        770        780 
NWTTQTSDDV CQLLGLGTGN SSMPFFSSGG GPFVKLNTAP NGSLILTASE QCFEDSLILL 

       790        800        810        820        830        840 
QCNHKSCGKK QVAQEVSPKI VGGNDSREGA WPWVVALYYN GQLLCGASLV SRDWLVSAAH 

       850        860        870        880        890        900 
CVYGRNLEPS KWKAILGLHM TSNLTSPQIV TRLIDEIVIN PHYNRRRKDS DIAMMHLEFK 

       910        920        930        940        950        960 
VNYTDYIQPI CLPEENQVFP PGRICSIAGW GKVIYQGSPA DILQEADVPL LSNEKCQQQM 

       970        980        990       1000       1010       1020 
PEYNITENMM CAGYEEGGID SCQGDSGGPL MCLENNRWLL AGVTSFGYQC ALPNRPGVYA 

      1030 
RVPKFTEWIQ SFLH

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References

[1]"Structural characterization of porcine enteropeptidase."
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.
J. Biol. Chem. 269:19976-19982(1994) [PubMed: 8051081] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Duodenal mucosa.

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Cross-references

Sequence databases

D30799 mRNA. Translation: BAA06459.1.
PIRA53663.
RefSeqNP_001001259.1.
UniGeneSsc.298

3D structure databases

HSSPHSSP built from PDB template 1EKB based on UniProtKB P98072.
SMRP98074. Positions 800-1034.
ModBaseSearch...

Protein family/group databases

MEROPSS01.156.

Genome annotation databases

GeneID397152.
KEGGssc:397152.

Phylogenomic databases

HOVERGENP98074.

Enzyme and pathway databases

BRENDA3.4.21.9. 249.

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...

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Entry information

Entry nameENTK_PIG
AccessionPrimary (citable) accession number: P98074
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: March 24, 2009
This is version 78 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

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