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P98074

- ENTK_PIG

UniProt

P98074 - ENTK_PIG

Protein

Enteropeptidase

Gene

TMPRSS15

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    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

    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

    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.
    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.
    InterProiIPR008985. 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]
    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

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    MGSKRIIPSR HRSLSTYEVM FTALFAILMV LCAGLIAVSW LTIKGSEKDA     50
    ALGKSHEARG TMKITSGVTY NPNLQDKLSV DFKVLAFDIQ QMIGEIFQSS 100
    NLKNEYKNSR VLQFENGSVI VIFDLLFAQW VSDENIKEEL IQGIEANKSS 150
    QLVAFHIDVN SIDITESLEN YSTTSPSTTS DKLTTSSPPA TPGNVSIECL 200
    PGSRPCADAL KCIAVDLFCD GELNCPDGSD EDSKICATAC DGKFLLTESS 250
    GSFDAAQYPK LSEASVVCQW IIRVNQGLSI ELNFSYFNTY SMDVLNIYEG 300
    VGSSKILRAS LWLMNPGTIR IFSNQVTVTF LIESDENDYI GFNATYTAFN 350
    STELNNDEKI NCNFEDGFCF WIQDLNDDNE WERIQGTTFP PFTGPNFDHT 400
    FGNASGFYIS TPTGPGGRQE RVGLLSLPLE PTLEPVCLSF WYYMYGENVY 450
    KLSINISNDQ NIEKIIFQKE GNYGENWNYG QVTLNETVEF KVAFNAFKNQ 500
    FLSDIALDDI SLTYGICNVS LYPEPTLVPT SPPELPTDCG GPFELWEPNT 550
    TFTSMNFPNN YPNQAFCVWN LNAQKGKNIQ LHFEEFDLEN IADVVEIRDG 600
    EEDDSLLLAV YTGPGPVEDV FSTTNRMTVL FITNDALTKG GFKANFTTGY 650
    HLGIPEPCKE DNFQCENGEC VLLVNLCDGF SHCKDGSDEA HCVRFLNGTA 700
    NNSGLVQFRI QSIWHTACAE NWTTQTSDDV CQLLGLGTGN SSMPFFSSGG 750
    GPFVKLNTAP NGSLILTASE QCFEDSLILL QCNHKSCGKK QVAQEVSPKI 800
    VGGNDSREGA WPWVVALYYN GQLLCGASLV SRDWLVSAAH CVYGRNLEPS 850
    KWKAILGLHM TSNLTSPQIV TRLIDEIVIN PHYNRRRKDS DIAMMHLEFK 900
    VNYTDYIQPI CLPEENQVFP PGRICSIAGW GKVIYQGSPA DILQEADVPL 950
    LSNEKCQQQM PEYNITENMM CAGYEEGGID SCQGDSGGPL MCLENNRWLL 1000
    AGVTSFGYQC ALPNRPGVYA RVPKFTEWIQ SFLH 1034
    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.
    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 IPR008985. 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 ]
    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 1, 2014
    This is version 115 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