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P98072

- ENTK_BOVIN

UniProt

P98072 - ENTK_BOVIN

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Protein

Enteropeptidase

Gene

TMPRSS15

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei841 – 8411Charge relay system1 Publication
Active sitei892 – 8921Charge relay system1 Publication
Active sitei987 – 9871Charge relay system1 Publication

GO - Molecular functioni

  1. scavenger receptor activity Source: InterPro
  2. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.156.

Names & Taxonomyi

Protein namesi
Recommended name:
Enteropeptidase (EC:3.4.21.9)
Alternative name(s):
Enterokinase
Serine protease 7
Transmembrane protease serine 15
Cleaved into the following 2 chains:
Gene namesi
Name:TMPRSS15
Synonyms:ENTK, PRSS7
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi889 – 8891K → A: Prevents the cleavage of trypsinogen. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedSequence Analysis
Chaini2 – 800799Enteropeptidase non-catalytic heavy chainPRO_0000027717Add
BLAST
Chaini801 – 1035235Enteropeptidase catalytic light chainPRO_0000027718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence Analysis
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi194 – 1941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi199 ↔ 212By similarity
Disulfide bondi206 ↔ 225By similarity
Disulfide bondi219 ↔ 236By similarity
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi240 ↔ 269By similarity
Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi456 – 4561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi486 – 4861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi519 – 5191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi540 ↔ 568By similarity
Glycosylationi550 – 5501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi646 – 6461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi659 ↔ 671By similarity
Disulfide bondi666 ↔ 684By similarity
Disulfide bondi678 ↔ 693By similarity
Glycosylationi698 – 6981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi722 – 7221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi741 – 7411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi762 – 7621N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi773 ↔ 783By similarity
Disulfide bondi788 ↔ 912Interchain (between heavy and light chains)
Disulfide bondi826 ↔ 842By similarity
Glycosylationi864 – 8641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi903 – 9031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi926 ↔ 993By similarity
Disulfide bondi957 ↔ 972By similarity
Glycosylationi965 – 9651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi983 ↔ 1011By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Myristate, Zymogen

Proteomic databases

PRIDEiP98072.

Expressioni

Tissue specificityi

Intestinal brush border.

Interactioni

Subunit structurei

Heterodimer of a catalytic (light) chain and a multidomain (heavy) chain linked by a disulfide bond.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000788.

Structurei

Secondary structure

1
1035
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi815 – 8206
Beta strandi823 – 8308
Beta strandi832 – 8387
Helixi840 – 8434
Helixi850 – 8523
Beta strandi853 – 8586
Beta strandi871 – 88010
Turni886 – 8894
Beta strandi894 – 9007
Beta strandi925 – 93511
Beta strandi945 – 9517
Helixi954 – 9607
Beta strandi970 – 9734
Beta strandi990 – 9956
Beta strandi998 – 100710
Beta strandi1009 – 10124
Beta strandi1018 – 10225
Helixi1023 – 10253
Helixi1027 – 10315

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EKBX-ray2.30A788-800[»]
B801-1035[»]
ProteinModelPortaliP98072.
SMRiP98072. Positions 801-1035.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP98072.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1817CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini48 – 1035988ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei19 – 4729Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 169116SEAPROSITE-ProRule annotationAdd
BLAST
Domaini197 – 23842LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini240 – 350111CUB 1PROSITE-ProRule annotationAdd
BLAST
Domaini358 – 520163MAMPROSITE-ProRule annotationAdd
BLAST
Domaini540 – 650111CUB 2PROSITE-ProRule annotationAdd
BLAST
Domaini657 – 69539LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini694 – 78794SRCRPROSITE-ProRule annotationAdd
BLAST
Domaini801 – 1035235Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 CUB domains.PROSITE-ProRule annotation
Contains 2 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 1 MAM domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 1 SEA domain.PROSITE-ProRule annotation
Contains 1 SRCR domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000112380.
HOVERGENiHBG005588.
InParanoidiP98072.
KOiK01316.
OMAiFEDGFCF.
OrthoDBiEOG7RNK07.
TreeFamiTF351678.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
3.10.250.10. 1 hit.
3.30.70.960. 1 hit.
4.10.400.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
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]
PfamiPF00431. 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]
PIRSFiPIRSF001138. Enteropeptidase. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00042. 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]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 2 hits.
SSF82671. SSF82671. 1 hit.
PROSITEiPS01180. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P98072) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGSKRSVPSR HRSLTTYEVM FAVLFVILVA LCAGLIAVSW LSIQGSVKDA
60 70 80 90 100
AFGKSHEARG TLKIISGATY NPHLQDKLSV DFKVLAFDIQ QMIDDIFQSS
110 120 130 140 150
NLKNEYKNSR VLQFENGSII VIFDLLFDQW VSDKNVKEEL IQGIEANKSS
160 170 180 190 200
QLVTFHIDLN SIDITASLEN FSTISPATTS EKLTTSIPLA TPGNVSIECP
210 220 230 240 250
PDSRLCADAL KCIAIDLFCD GELNCPDGSD EDNKTCATAC DGRFLLTGSS
260 270 280 290 300
GSFEALHYPK PSNNTSAVCR WIIRVNQGLS IQLNFDYFNT YYADVLNIYE
310 320 330 340 350
GMGSSKILRA SLWSNNPGII RIFSNQVTAT FLIQSDESDY IGFKVTYTAF
360 370 380 390 400
NSKELNNYEK INCNFEDGFC FWIQDLNDDN EWERTQGSTF PPSTGPTFDH
410 420 430 440 450
TFGNESGFYI STPTGPGGRR ERVGLLTLPL DPTPEQACLS FWYYMYGENV
460 470 480 490 500
YKLSINISSD QNMEKTIFQK EGNYGQNWNY GQVTLNETVE FKVSFYGFKN
510 520 530 540 550
QILSDIALDD ISLTYGICNV SVYPEPTLVP TPPPELPTDC GGPHDLWEPN
560 570 580 590 600
TTFTSINFPN SYPNQAFCIW NLNAQKGKNI QLHFQEFDLE NIADVVEIRD
610 620 630 640 650
GEGDDSLFLA VYTGPGPVND VFSTTNRMTV LFITDNMLAK QGFKANFTTG
660 670 680 690 700
YGLGIPEPCK EDNFQCKDGE CIPLVNLCDG FPHCKDGSDE AHCVRLFNGT
710 720 730 740 750
TDSSGLVQFR IQSIWHVACA ENWTTQISDD VCQLLGLGTG NSSVPTFSTG
760 770 780 790 800
GGPYVNLNTA PNGSLILTPS QQCLEDSLIL LQCNYKSCGK KLVTQEVSPK
810 820 830 840 850
IVGGSDSREG AWPWVVALYF DDQQVCGASL VSRDWLVSAA HCVYGRNMEP
860 870 880 890 900
SKWKAVLGLH MASNLTSPQI ETRLIDQIVI NPHYNKRRKN NDIAMMHLEM
910 920 930 940 950
KVNYTDYIQP ICLPEENQVF PPGRICSIAG WGALIYQGST ADVLQEADVP
960 970 980 990 1000
LLSNEKCQQQ MPEYNITENM VCAGYEAGGV DSCQGDSGGP LMCQENNRWL
1010 1020 1030
LAGVTSFGYQ CALPNRPGVY ARVPRFTEWI QSFLH
Length:1,035
Mass (Da):114,887
Last modified:February 1, 1996 - v1
Checksum:iE207970B08296E13
GO
Isoform Short (identifier: P98072-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,008
Mass (Da):112,127
Checksum:iE987B6FAE94E9FF9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti808 – 8081R → Y AA sequence (PubMed:1799406)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei166 – 19227Missing in isoform Short. CuratedVSP_005386Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09859 mRNA. Translation: AAB40026.1.
L19663 mRNA. Translation: AAA16035.1.
PIRiA43090.
RefSeqiNP_776864.1. NM_174439.2. [P98072-1]
UniGeneiBt.66152.

Genome annotation databases

EnsembliENSBTAT00000000788; ENSBTAP00000000788; ENSBTAG00000000597. [P98072-1]
ENSBTAT00000064206; ENSBTAP00000054149; ENSBTAG00000000597. [P98072-2]
GeneIDi282009.
KEGGibta:282009.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09859 mRNA. Translation: AAB40026.1 .
L19663 mRNA. Translation: AAA16035.1 .
PIRi A43090.
RefSeqi NP_776864.1. NM_174439.2. [P98072-1 ]
UniGenei Bt.66152.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EKB X-ray 2.30 A 788-800 [» ]
B 801-1035 [» ]
ProteinModelPortali P98072.
SMRi P98072. Positions 801-1035.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000000788.

Protein family/group databases

MEROPSi S01.156.

Proteomic databases

PRIDEi P98072.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000000788 ; ENSBTAP00000000788 ; ENSBTAG00000000597 . [P98072-1 ]
ENSBTAT00000064206 ; ENSBTAP00000054149 ; ENSBTAG00000000597 . [P98072-2 ]
GeneIDi 282009.
KEGGi bta:282009.

Organism-specific databases

CTDi 5651.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000118962.
HOGENOMi HOG000112380.
HOVERGENi HBG005588.
InParanoidi P98072.
KOi K01316.
OMAi FEDGFCF.
OrthoDBi EOG7RNK07.
TreeFami TF351678.

Miscellaneous databases

EvolutionaryTracei P98072.
NextBioi 20805876.

Family and domain databases

Gene3Di 2.60.120.290. 2 hits.
3.10.250.10. 1 hit.
3.30.70.960. 1 hit.
4.10.400.10. 2 hits.
InterProi IPR013320. ConA-like_dom.
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 ]
Pfami PF00431. 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 ]
PIRSFi PIRSF001138. Enteropeptidase. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00042. 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 ]
SUPFAMi SSF49854. SSF49854. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 2 hits.
SSF82671. SSF82671. 1 hit.
PROSITEi PS01180. 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 ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiENTK_BOVIN
AccessioniPrimary (citable) accession number: P98072
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3