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P00764

- TRYP_SQUAC

UniProt

P00764 - TRYP_SQUAC

Protein

Trypsin

Gene
N/A
Organism
Squalus acanthias (Spiny dogfish)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    • Comment

    Functioni

    Catalytic activityi

    Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei47 – 471Charge relay systemBy similarity
    Metal bindingi59 – 591CalciumBy similarity
    Metal bindingi69 – 691CalciumBy similarity
    Active sitei91 – 911Charge relay systemBy similarity
    Sitei177 – 1771Required for specificityBy similarity
    Active sitei183 – 1831Charge relay systemBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. digestion Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Digestion

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trypsin (EC:3.4.21.4)
    OrganismiSqualus acanthias (Spiny dogfish)
    Taxonomic identifieri7797 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiSqualimorphiiSqualiformesSqualidaeSqualus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 77Activation peptide1 PublicationPRO_0000028231
    Chaini8 – 229222TrypsinPRO_0000028232Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi14 ↔ 143PROSITE-ProRule annotation
    Disulfide bondi32 ↔ 48PROSITE-ProRule annotation
    Disulfide bondi116 ↔ 216PROSITE-ProRule annotation
    Disulfide bondi123 ↔ 189PROSITE-ProRule annotation
    Disulfide bondi154 ↔ 168PROSITE-ProRule annotation
    Disulfide bondi179 ↔ 203PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliP00764.
    SMRiP00764. Positions 8-227.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 227220Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOVERGENiHBG013304.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. 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.

    P00764-1 [UniParc]FASTAAdd to Basket

    « Hide

    APDDDDKIVG GYECPKHAAP WTVSLNVGYH FCGGSLIAPG WVVSAAHCYQ    50
    RRIQVRLGEH DISANEGDET YIDSSMVIRH PNYSGYDLDN DIMLIKLSKP 100
    AALNRNVDLI SLPTGCAYAG EMCLISGWGN TMDGAVSGDQ LQCLDAPVLS 150
    DAECKGAYPG MITNNMMCVG YMEGGKDSCQ GDSGGPVVCN GMLQGIVSWG 200
    YGCAERDHPG VYTRVCHYVS WIHETIASV 229
    Length:229
    Mass (Da):24,591
    Last modified:July 21, 1986 - v1
    Checksum:iE83B83C5AD72FCE4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti109 – 1091L → P.

    Sequence databases

    PIRiA00950. TRDFS.

    Cross-referencesi

    Sequence databases

    PIRi A00950. TRDFS.

    3D structure databases

    ProteinModelPortali P00764.
    SMRi P00764. Positions 8-227.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG013304.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: PROTEIN SEQUENCE OF 8-229.
    2. "Comparison of the amino terminal sequences of bovine, dogfish, and lungfish trypsinogens."
      Hermodson M.A., Tye R.W., Reeck G.R., Neurath H., Walsh K.A.
      FEBS Lett. 14:222-224(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-21.

    Entry informationi

    Entry nameiTRYP_SQUAC
    AccessioniPrimary (citable) accession number: P00764
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 83 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

    Direct protein sequencing

    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