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P98072 (ENTK_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enteropeptidase

EC=3.4.21.9
Alternative name(s):
Enterokinase
Serine protease 7
Transmembrane protease serine 15
Gene names
Name:TMPRSS15
Synonyms:ENTK, PRSS7
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length1035 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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

Heterodimer of a catalytic (light) chain and a multidomain (heavy) chain linked by a disulfide bond. Ref.4

Subcellular location

Membrane; Single-pass type II membrane protein Probable.

Tissue specificity

Intestinal brush border.

Post-translational modification

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

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P98072-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P98072-2)

The sequence of this isoform differs from the canonical sequence as follows:
     166-192: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 800799Enteropeptidase non-catalytic heavy chain
PRO_0000027717
Chain801 – 1035235Enteropeptidase catalytic light chain
PRO_0000027718

Regions

Topological domain2 – 1817Cytoplasmic Potential
Transmembrane19 – 4729Helical; Signal-anchor for type II membrane protein; Potential
Topological domain48 – 1035988Extracellular Potential
Domain54 – 169116SEA
Domain197 – 23842LDL-receptor class A 1
Domain240 – 350111CUB 1
Domain358 – 520163MAM
Domain540 – 650111CUB 2
Domain657 – 69539LDL-receptor class A 2
Domain694 – 78794SRCR
Domain801 – 1035235Peptidase S1

Sites

Active site8411Charge relay system Ref.4
Active site8921Charge relay system Ref.4
Active site9871Charge relay system Ref.4

Amino acid modifications

Lipidation21N-myristoyl glycine Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1471N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential
Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation2631N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation4041N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Glycosylation4861N-linked (GlcNAc...) Potential
Glycosylation5191N-linked (GlcNAc...) Potential
Glycosylation5501N-linked (GlcNAc...) Potential
Glycosylation6461N-linked (GlcNAc...) Potential
Glycosylation6981N-linked (GlcNAc...) Potential
Glycosylation7221N-linked (GlcNAc...) Potential
Glycosylation7411N-linked (GlcNAc...) Potential
Glycosylation7621N-linked (GlcNAc...) Potential
Glycosylation8641N-linked (GlcNAc...) Potential
Glycosylation9031N-linked (GlcNAc...) Potential
Glycosylation9651N-linked (GlcNAc...) Potential
Disulfide bond199 ↔ 212 By similarity
Disulfide bond206 ↔ 225 By similarity
Disulfide bond219 ↔ 236 By similarity
Disulfide bond240 ↔ 269 By similarity
Disulfide bond540 ↔ 568 By similarity
Disulfide bond659 ↔ 671 By similarity
Disulfide bond666 ↔ 684 By similarity
Disulfide bond678 ↔ 693 By similarity
Disulfide bond773 ↔ 783 By similarity
Disulfide bond788 ↔ 912Interchain (between heavy and light chains) Ref.4
Disulfide bond826 ↔ 842 By similarity
Disulfide bond926 ↔ 993 By similarity
Disulfide bond957 ↔ 972 By similarity
Disulfide bond983 ↔ 1011 By similarity

Natural variations

Alternative sequence166 – 19227Missing in isoform Short.
VSP_005386

Experimental info

Mutagenesis8891K → A: Prevents the cleavage of trypsinogen. Ref.4
Sequence conflict8081R → Y AA sequence Ref.3

Secondary structure

..................................... 1035
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: E207970B08296E13

FASTA1,035114,887
        10         20         30         40         50         60 
MGSKRSVPSR HRSLTTYEVM FAVLFVILVA LCAGLIAVSW LSIQGSVKDA AFGKSHEARG 

        70         80         90        100        110        120 
TLKIISGATY NPHLQDKLSV DFKVLAFDIQ QMIDDIFQSS NLKNEYKNSR VLQFENGSII 

       130        140        150        160        170        180 
VIFDLLFDQW VSDKNVKEEL IQGIEANKSS QLVTFHIDLN SIDITASLEN FSTISPATTS 

       190        200        210        220        230        240 
EKLTTSIPLA TPGNVSIECP PDSRLCADAL KCIAIDLFCD GELNCPDGSD EDNKTCATAC 

       250        260        270        280        290        300 
DGRFLLTGSS GSFEALHYPK PSNNTSAVCR WIIRVNQGLS IQLNFDYFNT YYADVLNIYE 

       310        320        330        340        350        360 
GMGSSKILRA SLWSNNPGII RIFSNQVTAT FLIQSDESDY IGFKVTYTAF NSKELNNYEK 

       370        380        390        400        410        420 
INCNFEDGFC FWIQDLNDDN EWERTQGSTF PPSTGPTFDH TFGNESGFYI STPTGPGGRR 

       430        440        450        460        470        480 
ERVGLLTLPL DPTPEQACLS FWYYMYGENV YKLSINISSD QNMEKTIFQK EGNYGQNWNY 

       490        500        510        520        530        540 
GQVTLNETVE FKVSFYGFKN QILSDIALDD ISLTYGICNV SVYPEPTLVP TPPPELPTDC 

       550        560        570        580        590        600 
GGPHDLWEPN TTFTSINFPN SYPNQAFCIW NLNAQKGKNI QLHFQEFDLE NIADVVEIRD 

       610        620        630        640        650        660 
GEGDDSLFLA VYTGPGPVND VFSTTNRMTV LFITDNMLAK QGFKANFTTG YGLGIPEPCK 

       670        680        690        700        710        720 
EDNFQCKDGE CIPLVNLCDG FPHCKDGSDE AHCVRLFNGT TDSSGLVQFR IQSIWHVACA 

       730        740        750        760        770        780 
ENWTTQISDD VCQLLGLGTG NSSVPTFSTG GGPYVNLNTA PNGSLILTPS QQCLEDSLIL 

       790        800        810        820        830        840 
LQCNYKSCGK KLVTQEVSPK IVGGSDSREG AWPWVVALYF DDQQVCGASL VSRDWLVSAA 

       850        860        870        880        890        900 
HCVYGRNMEP SKWKAVLGLH MASNLTSPQI ETRLIDQIVI NPHYNKRRKN NDIAMMHLEM 

       910        920        930        940        950        960 
KVNYTDYIQP ICLPEENQVF PPGRICSIAG WGALIYQGST ADVLQEADVP LLSNEKCQQQ 

       970        980        990       1000       1010       1020 
MPEYNITENM VCAGYEAGGV DSCQGDSGGP LMCQENNRWL LAGVTSFGYQ CALPNRPGVY 

      1030 
ARVPRFTEWI QSFLH 

« Hide

Isoform Short [UniParc].

Checksum: E987B6FAE94E9FF9
Show »

FASTA1,008112,127

References

[1]"Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains."
Kitamoto Y., Yuan X., Wu Q., McCourt D.W., Sadler J.E.
Proc. Natl. Acad. Sci. U.S.A. 91:7588-7592(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Duodenum.
[2]"Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase."
Lavallie E.R., Rehemtulla A., Racie L.A., Diblasio E.A., Ferenz C., Grant K.L., Light A., McCoy J.M.
J. Biol. Chem. 268:23311-23317(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 801-1035, PARTIAL PROTEIN SEQUENCE.
[3]"The amino-terminal sequence of the catalytic subunit of bovine enterokinase."
Light A., Janska H.
J. Protein Chem. 10:475-480(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 801-827.
Tissue: Intestine.
[4]"Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide."
Lu D., Futterer K., Korolev S., Zheng X., Tan K., Waksman G., Sadler J.E.
J. Mol. Biol. 292:361-373(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 788-1035 IN COMPLEX WITH INHIBITOR, ACTIVE SITE, SUBUNIT, INTERCHAIN DISULFIDE BOND, MUTAGENESIS OF LYS-889.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09859 mRNA. Translation: AAB40026.1.
L19663 mRNA. Translation: AAA16035.1.
PIRA43090.
RefSeqNP_776864.1. NM_174439.2. [P98072-1]
UniGeneBt.66152.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EKBX-ray2.30A788-800[»]
B801-1035[»]
ProteinModelPortalP98072.
SMRP98072. Positions 801-1035.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000000788.

Protein family/group databases

MEROPSS01.156.

Proteomic databases

PRIDEP98072.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000000788; ENSBTAP00000000788; ENSBTAG00000000597. [P98072-1]
ENSBTAT00000064206; ENSBTAP00000054149; ENSBTAG00000000597. [P98072-2]
GeneID282009.
KEGGbta:282009.

Organism-specific databases

CTD5651.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00720000108393.
HOGENOMHOG000112380.
HOVERGENHBG005588.
InParanoidP98072.
KOK01316.
OMAFEDGFCF.
OrthoDBEOG7RNK07.
TreeFamTF351678.

Family and domain databases

Gene3D2.60.120.290. 2 hits.
3.10.250.10. 1 hit.
3.30.70.960. 1 hit.
4.10.400.10. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR000859. CUB_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR000998. MAM_dom.
IPR011163. Pept_S1A_enterop.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
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.
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]
SUPFAMSSF49854. SSF49854. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 2 hits.
SSF82671. SSF82671. 1 hit.
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

EvolutionaryTraceP98072.
NextBio20805876.

Entry information

Entry nameENTK_BOVIN
AccessionPrimary (citable) accession number: P98072
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references