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P98074

- ENTK_PIG

UniProt

P98074 - ENTK_PIG

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Protein

Enteropeptidase

Gene

TMPRSS15

Organism
Sus scrofa (Pig)
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 sitei840 – 8401Charge relay systemBy similarity
Active sitei891 – 8911Charge relay systemBy similarity
Active sitei986 – 9861Charge relay systemBy similarity

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 3 chains:
Gene namesi
Name:TMPRSS15
Synonyms:ENTK, PRSS7
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 5151PRO_0000027723Add
BLAST
Chaini52 – 11766Enteropeptidase non-catalytic mini chainPRO_0000027724Add
BLAST
Chaini118 – 799682Enteropeptidase non-catalytic heavy chainPRO_0000027725Add
BLAST
Chaini800 – 1034235Enteropeptidase catalytic light chainPRO_0000027726Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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
Disulfide bondi240 ↔ 268By similarity
Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi455 – 4551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi485 – 4851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi518 – 5181N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi539 ↔ 567By similarity
Glycosylationi549 – 5491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi645 – 6451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi658 ↔ 670By similarity
Disulfide bondi665 ↔ 683By similarity
Disulfide bondi677 ↔ 692By similarity
Glycosylationi697 – 6971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi701 – 7011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi740 – 7401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi761 – 7611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi772 ↔ 782By similarity
Disulfide bondi787 ↔ 911Interchain (between heavy and light chains)PROSITE-ProRule annotation
Glycosylationi804 – 8041N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi825 ↔ 841By similarity
Glycosylationi863 – 8631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi902 – 9021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi925 ↔ 992By similarity
Disulfide bondi956 ↔ 971By similarity
Glycosylationi964 – 9641N-linked (GlcNAc...)Sequence Analysis
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

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.
SMRiP98074. Positions 800-1034.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1817CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini48 – 1034987ExtracellularSequence 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 – 349110CUB 1PROSITE-ProRule annotationAdd
BLAST
Domaini357 – 519163MAMPROSITE-ProRule annotationAdd
BLAST
Domaini539 – 649111CUB 2PROSITE-ProRule annotationAdd
BLAST
Domaini656 – 69439LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini693 – 78694SRCRPROSITE-ProRule annotationAdd
BLAST
Domaini800 – 1034235Peptidase 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.
HOGENOMiHOG000112380.
HOVERGENiHBG005588.
InParanoidiP98074.
KOiK01316.

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]

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D30799 mRNA. Translation: BAA06459.1 .
PIRi A53663.
RefSeqi NP_001001259.1. NM_001001259.1.
UniGenei Ssc.298.

3D structure databases

ProteinModelPortali P98074.
SMRi P98074. Positions 800-1034.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000012801.

Protein family/group databases

MEROPSi S01.156.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397152.
KEGGi ssc:397152.

Organism-specific databases

CTDi 5651.

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000112380.
HOVERGENi HBG005588.
InParanoidi P98074.
KOi K01316.

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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Duodenal mucosa.

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: October 29, 2014
This is version 116 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

External Data

Dasty 3