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Protein

Enteropeptidase

Gene

TMPRSS15

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei840Charge relay systemBy similarity1
Active sitei891Charge relay systemBy similarity1
Active sitei986Charge relay systemBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.9. 6170.

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 3 chains:
Gene namesi
Name:TMPRSS15
Synonyms:ENTK, PRSS7
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 18CytoplasmicSequence analysisAdd BLAST17
Transmembranei19 – 47Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST29
Topological domaini48 – 1034ExtracellularSequence analysisAdd BLAST987

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000277231 – 51Add BLAST51
ChainiPRO_000002772452 – 117Enteropeptidase non-catalytic mini chainAdd BLAST66
ChainiPRO_0000027725118 – 799Enteropeptidase non-catalytic heavy chainAdd BLAST682
ChainiPRO_0000027726800 – 1034Enteropeptidase catalytic light chainAdd BLAST235

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi116N-linked (GlcNAc...)Sequence analysis1
Glycosylationi147N-linked (GlcNAc...)Sequence analysis1
Glycosylationi170N-linked (GlcNAc...)Sequence analysis1
Glycosylationi194N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi199 ↔ 212By similarity
Disulfide bondi206 ↔ 225By similarity
Disulfide bondi219 ↔ 236By similarity
Disulfide bondi240 ↔ 268By similarity
Glycosylationi283N-linked (GlcNAc...)Sequence analysis1
Glycosylationi343N-linked (GlcNAc...)Sequence analysis1
Glycosylationi350N-linked (GlcNAc...)Sequence analysis1
Glycosylationi403N-linked (GlcNAc...)Sequence analysis1
Glycosylationi455N-linked (GlcNAc...)Sequence analysis1
Glycosylationi485N-linked (GlcNAc...)Sequence analysis1
Glycosylationi518N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi539 ↔ 567By similarity
Glycosylationi549N-linked (GlcNAc...)Sequence analysis1
Glycosylationi645N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi658 ↔ 670By similarity
Disulfide bondi665 ↔ 683By similarity
Disulfide bondi677 ↔ 692By similarity
Glycosylationi697N-linked (GlcNAc...)Sequence analysis1
Glycosylationi701N-linked (GlcNAc...)Sequence analysis1
Glycosylationi721N-linked (GlcNAc...)Sequence analysis1
Glycosylationi740N-linked (GlcNAc...)Sequence analysis1
Glycosylationi761N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi772 ↔ 782By similarity
Disulfide bondi787 ↔ 911Interchain (between heavy and light chains)PROSITE-ProRule annotation
Glycosylationi804N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi825 ↔ 841By similarity
Glycosylationi863N-linked (GlcNAc...)Sequence analysis1
Glycosylationi902N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi925 ↔ 992By similarity
Disulfide bondi956 ↔ 971By similarity
Glycosylationi964N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi982 ↔ 1010By similarity

Post-translational modificationi

The chains are derived from a single precursor that is cleaved by a trypsin-like protease.
The mini chain may be cleaved by elastase.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP98074.
PRIDEiP98074.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000012801.

Structurei

3D structure databases

ProteinModelPortaliP98074.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini54 – 169SEAPROSITE-ProRule annotationAdd BLAST116
Domaini197 – 238LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST42
Domaini240 – 349CUB 1PROSITE-ProRule annotationAdd BLAST110
Domaini357 – 519MAMPROSITE-ProRule annotationAdd BLAST163
Domaini539 – 649CUB 2PROSITE-ProRule annotationAdd BLAST111
Domaini656 – 694LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST39
Domaini693 – 786SRCRPROSITE-ProRule annotationAdd BLAST94
Domaini800 – 1034Peptidase S1PROSITE-ProRule annotationAdd BLAST235

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

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000112380.
HOVERGENiHBG005588.
InParanoidiP98074.
KOiK01316.

Family and domain databases

CDDicd00041. CUB. 2 hits.
cd06263. MAM. 1 hit.
cd00190. Tryp_SPc. 1 hit.
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.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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]

Sequencei

Sequence statusi: Complete.

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

P98074-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSKRIIPSR HRSLSTYEVM FTALFAILMV LCAGLIAVSW LTIKGSEKDA
60 70 80 90 100
ALGKSHEARG TMKITSGVTY NPNLQDKLSV DFKVLAFDIQ QMIGEIFQSS
110 120 130 140 150
NLKNEYKNSR VLQFENGSVI VIFDLLFAQW VSDENIKEEL IQGIEANKSS
160 170 180 190 200
QLVAFHIDVN SIDITESLEN YSTTSPSTTS DKLTTSSPPA TPGNVSIECL
210 220 230 240 250
PGSRPCADAL KCIAVDLFCD GELNCPDGSD EDSKICATAC DGKFLLTESS
260 270 280 290 300
GSFDAAQYPK LSEASVVCQW IIRVNQGLSI ELNFSYFNTY SMDVLNIYEG
310 320 330 340 350
VGSSKILRAS LWLMNPGTIR IFSNQVTVTF LIESDENDYI GFNATYTAFN
360 370 380 390 400
STELNNDEKI NCNFEDGFCF WIQDLNDDNE WERIQGTTFP PFTGPNFDHT
410 420 430 440 450
FGNASGFYIS TPTGPGGRQE RVGLLSLPLE PTLEPVCLSF WYYMYGENVY
460 470 480 490 500
KLSINISNDQ NIEKIIFQKE GNYGENWNYG QVTLNETVEF KVAFNAFKNQ
510 520 530 540 550
FLSDIALDDI SLTYGICNVS LYPEPTLVPT SPPELPTDCG GPFELWEPNT
560 570 580 590 600
TFTSMNFPNN YPNQAFCVWN LNAQKGKNIQ LHFEEFDLEN IADVVEIRDG
610 620 630 640 650
EEDDSLLLAV YTGPGPVEDV FSTTNRMTVL FITNDALTKG GFKANFTTGY
660 670 680 690 700
HLGIPEPCKE DNFQCENGEC VLLVNLCDGF SHCKDGSDEA HCVRFLNGTA
710 720 730 740 750
NNSGLVQFRI QSIWHTACAE NWTTQTSDDV CQLLGLGTGN SSMPFFSSGG
760 770 780 790 800
GPFVKLNTAP NGSLILTASE QCFEDSLILL QCNHKSCGKK QVAQEVSPKI
810 820 830 840 850
VGGNDSREGA WPWVVALYYN GQLLCGASLV SRDWLVSAAH CVYGRNLEPS
860 870 880 890 900
KWKAILGLHM TSNLTSPQIV TRLIDEIVIN PHYNRRRKDS DIAMMHLEFK
910 920 930 940 950
VNYTDYIQPI CLPEENQVFP PGRICSIAGW GKVIYQGSPA DILQEADVPL
960 970 980 990 1000
LSNEKCQQQM PEYNITENMM CAGYEEGGID SCQGDSGGPL MCLENNRWLL
1010 1020 1030
AGVTSFGYQC ALPNRPGVYA RVPKFTEWIQ SFLH
Length:1,034
Mass (Da):114,776
Last modified:February 1, 1996 - v1
Checksum:i0388C64CF64CC368
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30799 mRNA. Translation: BAA06459.1.
PIRiA53663.
RefSeqiNP_001001259.1. NM_001001259.1.
UniGeneiSsc.298.

Genome annotation databases

GeneIDi397152.
KEGGissc:397152.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30799 mRNA. Translation: BAA06459.1.
PIRiA53663.
RefSeqiNP_001001259.1. NM_001001259.1.
UniGeneiSsc.298.

3D structure databases

ProteinModelPortaliP98074.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000012801.

Protein family/group databases

MEROPSiS01.156.

Proteomic databases

PaxDbiP98074.
PRIDEiP98074.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397152.
KEGGissc:397152.

Organism-specific databases

CTDi5651.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000112380.
HOVERGENiHBG005588.
InParanoidiP98074.
KOiK01316.

Enzyme and pathway databases

BRENDAi3.4.21.9. 6170.

Family and domain databases

CDDicd00041. CUB. 2 hits.
cd06263. MAM. 1 hit.
cd00190. Tryp_SPc. 1 hit.
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.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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]
ProtoNetiSearch...

Entry informationi

Entry nameiENTK_PIG
AccessioniPrimary (citable) accession number: P98074
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 129 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.