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P00794

- CHYM_BOVIN

UniProt

P00794 - CHYM_BOVIN

Protein

Chymosin

Gene

CYM

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (01 Feb 2005)
      Previous versions | rss
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    Functioni

    Chymosin is synthesized in the mucosa of the abomasum (fourth stomach) of young (unweaned) ruminants. The enzyme hydrolyzes casein to paracasein.

    Catalytic activityi

    Broad specificity similar to that of pepsin A. Clots milk by cleavage of a single 104-Ser-Phe-|-Met-Ala-107 bond in kappa-chain of casein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei92 – 9212 PublicationsPROSITE-ProRule annotation
    Active sitei274 – 27412 PublicationsPROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. digestion Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Keywords - Biological processi

    Digestion

    Enzyme and pathway databases

    SABIO-RKP00794.

    Protein family/group databases

    MEROPSiA01.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chymosin (EC:3.4.23.4)
    Alternative name(s):
    Preprorennin
    Gene namesi
    Name:CYM
    Synonyms:CPC
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 3

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi308 – 3081C → D: Propeptide is not cleaved. 1 Publication
    Mutagenesisi341 – 3411C → S: Propeptide is not cleaved. 1 Publication

    Protein family/group databases

    Allergomei3882. Bos d Chymosin.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 16163 PublicationsAdd
    BLAST
    Propeptidei17 – 5842Activation peptide1 PublicationPRO_0000025988Add
    BLAST
    Chaini59 – 381323ChymosinPRO_0000025989Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi105 ↔ 1101 Publication
    Disulfide bondi265 ↔ 2691 Publication
    Disulfide bondi308 ↔ 3411 Publication

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    PRIDEiP00794.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    381
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi62 – 654
    Beta strandi67 – 693
    Turni70 – 723
    Beta strandi73 – 808
    Turni81 – 844
    Beta strandi85 – 928
    Beta strandi98 – 1003
    Helixi108 – 1114
    Helixi118 – 1203
    Beta strandi125 – 13410
    Beta strandi139 – 15113
    Beta strandi154 – 16613
    Turni171 – 1733
    Beta strandi176 – 1827
    Helixi186 – 1883
    Helixi196 – 2027
    Beta strandi206 – 2149
    Beta strandi217 – 2204
    Beta strandi223 – 2275
    Helixi231 – 2333
    Beta strandi234 – 2429
    Turni246 – 2494
    Beta strandi250 – 2534
    Beta strandi255 – 2584
    Beta strandi261 – 2644
    Beta strandi269 – 2735
    Beta strandi279 – 2835
    Helixi284 – 29411
    Beta strandi297 – 2993
    Turni300 – 3023
    Beta strandi304 – 3063
    Helixi308 – 3136
    Beta strandi317 – 3215
    Beta strandi324 – 3285
    Helixi330 – 3334
    Beta strandi334 – 3374
    Beta strandi340 – 35011
    Beta strandi354 – 3563
    Helixi358 – 3614
    Beta strandi364 – 3696
    Turni370 – 3734
    Beta strandi374 – 3807

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CMSX-ray2.30A59-381[»]
    1CZIX-ray2.30E59-381[»]
    3CMSX-ray2.00A59-381[»]
    4AA8X-ray1.80A59-381[»]
    4AUCX-ray1.60A59-381[»]
    4CMSX-ray2.20A59-381[»]
    ProteinModelPortaliP00794.
    SMRiP00794. Positions 59-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00794.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG248684.
    GeneTreeiENSGT00670000097830.
    HOGENOMiHOG000197681.
    HOVERGENiHBG000482.
    InParanoidiP00794.
    KOiK01378.
    OMAiQYFGKIY.
    OrthoDBiEOG7HQN88.
    TreeFamiTF314990.

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PANTHERiPTHR13683. PTHR13683. 1 hit.
    PfamiPF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00794-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRCLVVLLAV FALSQGAEIT RIPLYKGKSL RKALKEHGLL EDFLQKQQYG    50
    ISSKYSGFGE VASVPLTNYL DSQYFGKIYL GTPPQEFTVL FDTGSSDFWV 100
    PSIYCKSNAC KNHQRFDPRK SSTFQNLGKP LSIHYGTGSM QGILGYDTVT 150
    VSNIVDIQQT VGLSTQEPGD VFTYAEFDGI LGMAYPSLAS EYSIPVFDNM 200
    MNRHLVAQDL FSVYMDRNGQ ESMLTLGAID PSYYTGSLHW VPVTVQQYWQ 250
    FTVDSVTISG VVVACEGGCQ AILDTGTSKL VGPSSDILNI QQAIGATQNQ 300
    YGEFDIDCDN LSYMPTVVFE INGKMYPLTP SAYTSQDQGF CTSGFQSENH 350
    SQKWILGDVF IREYYSVFDR ANNLVGLAKA I 381
    Length:381
    Mass (Da):42,180
    Last modified:February 1, 2005 - v3
    Checksum:iA4425013B4E2E56A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171A → T in AAA30446. (PubMed:3091454)Curated
    Sequence conflicti109 – 1091A → G in AAA30446. (PubMed:3091454)Curated
    Sequence conflicti155 – 1551V → L in AAA30447. (PubMed:6183168)Curated
    Sequence conflicti174 – 1741Y → T AA sequence (PubMed:329280)Curated
    Sequence conflicti218 – 2181N → D AA sequence (PubMed:329280)Curated
    Sequence conflicti218 – 2181N → D AA sequence (PubMed:381305)Curated
    Sequence conflicti230 – 2301D → N in AAA30448. (PubMed:6283469)Curated
    Sequence conflicti232 – 2321S → C in AAA30447. (PubMed:6183168)Curated
    Sequence conflicti252 – 2521T → Y AA sequence (PubMed:381305)Curated
    Sequence conflicti325 – 3251M → I(PubMed:6804449)Curated
    Sequence conflicti335 – 3351S → G(PubMed:6804449)Curated
    Sequence conflicti343 – 3431S → T(PubMed:6804449)Curated
    Sequence conflicti380 – 3801A → T(PubMed:6804449)Curated

    Polymorphismi

    Forms A and B are probably allelic variants. Form B is the predominant form and differs only in one position.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti302 – 3021G → D in chymosin A. 2 Publications

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00002 mRNA. Translation: AAA30447.1.
    J00003 mRNA. Translation: AAA30448.1.
    M14077
    , M14069, M14070, M14071, M14072, M14073, M14074, M14075 Genomic DNA. Translation: AAA30446.1.
    EF541122 mRNA. Translation: ABU41411.1.
    PIRiA25631. CMBO.
    RefSeqiNP_851337.1. NM_180994.2.
    UniGeneiBt.394.

    Genome annotation databases

    EnsembliENSBTAT00000013970; ENSBTAP00000013970; ENSBTAG00000010565.
    GeneIDi529879.
    KEGGibta:529879.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00002 mRNA. Translation: AAA30447.1 .
    J00003 mRNA. Translation: AAA30448.1 .
    M14077
    , M14069 , M14070 , M14071 , M14072 , M14073 , M14074 , M14075 Genomic DNA. Translation: AAA30446.1 .
    EF541122 mRNA. Translation: ABU41411.1 .
    PIRi A25631. CMBO.
    RefSeqi NP_851337.1. NM_180994.2.
    UniGenei Bt.394.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CMS X-ray 2.30 A 59-381 [» ]
    1CZI X-ray 2.30 E 59-381 [» ]
    3CMS X-ray 2.00 A 59-381 [» ]
    4AA8 X-ray 1.80 A 59-381 [» ]
    4AUC X-ray 1.60 A 59-381 [» ]
    4CMS X-ray 2.20 A 59-381 [» ]
    ProteinModelPortali P00794.
    SMRi P00794. Positions 59-381.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 3882. Bos d Chymosin.
    MEROPSi A01.006.

    Proteomic databases

    PRIDEi P00794.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000013970 ; ENSBTAP00000013970 ; ENSBTAG00000010565 .
    GeneIDi 529879.
    KEGGi bta:529879.

    Organism-specific databases

    CTDi 229697.

    Phylogenomic databases

    eggNOGi NOG248684.
    GeneTreei ENSGT00670000097830.
    HOGENOMi HOG000197681.
    HOVERGENi HBG000482.
    InParanoidi P00794.
    KOi K01378.
    OMAi QYFGKIY.
    OrthoDBi EOG7HQN88.
    TreeFami TF314990.

    Enzyme and pathway databases

    SABIO-RK P00794.

    Miscellaneous databases

    EvolutionaryTracei P00794.
    NextBioi 20875125.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of double-stranded cDNA coding for bovine chymosin."
      Moir D., Mao J., Schumm J.W., Vovis G.F., Alford B.L., Taunton-Rigby A.
      Gene 19:127-138(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-302.
    2. "Molecular cloning and nucleotide sequence of cDNA coding for calf preprochymosin."
      Harris T.J.R., Lowe P.A., Lyons A., Thomas P.G., Eaton M.A.W., Millican T.A., Patel T.P., Bose C.C., Carey N.H., Doel M.T.
      Nucleic Acids Res. 10:2177-2187(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning and structural analysis of the calf prochymosin gene."
      Hidaka M., Sasaki K., Uozumi T., Beppu T.
      Gene 43:197-203(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "cDNA encoding bovine calf preprochymosin."
      Sun D., Jiang Y.
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Nucleotide sequence of calf prorennin cDNA cloned in Escherichia coli."
      Nishimori K., Kawaguchi Y., Hidaka M., Uozumi T., Beppu T.
      J. Biochem. 91:1085-1088(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 140-381, VARIANT ASP-302.
    6. "Isolation of human, swine, and rat prepepsinogens and calf preprochymosin, and determination of the primary structures of their NH2-terminal signal sequences."
      Ichihara Y., Sogawa K., Takahashi K.
      J. Biochem. 98:483-492(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-30.
    7. Cited for: PROTEIN SEQUENCE OF 17-381.
    8. "Amino-acid sequence of the peptide segment liberated during activation of prochymosin (prorennin)."
      Pedersen V.B., Foltmann B.
      Eur. J. Biochem. 55:95-103(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-77.
    9. "The primary structure of calf chymosin."
      Foltmann B., Pedersen V.B., Kauffman D., Wybrandt G.
      J. Biol. Chem. 254:8447-8456(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 59-381, DISULFIDE BONDS.
    10. "The structure and function of acid proteases. III. Isolation and characterization of the active-site peptides from bovine rennin."
      Chang W.-J., Takahashi K.
      J. Biochem. 76:467-474(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE PEPTIDES.
    11. "X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2-A resolution of bovine chymosin."
      Newman M., Safro M., Frazao C., Kahn G., Zdanov A., Tickle I.J., Blundell T.L., Andreeva N.
      J. Mol. Biol. 221:1295-1309(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    12. "Engineering enzyme subsite specificity: preparation, kinetic characterization, and X-ray analysis at 2.0-A resolution of Val111Phe site-mutated calf chymosin."
      Strop P., Sedlacek J., Stys J., Kaderabkova Z., Blaha I., Pavlickova L., Pohl J., Fabry M., Kostka V., Newman M., Frazao C., Shearer A., Tickle I.J., Blundell T.L.
      Biochemistry 29:9863-9871(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT.
    13. "The three-dimensional structure of recombinant bovine chymosin at 2.3-A resolution."
      Gilliland G.L., Winborne E.L., Nachman J., Wlodawer A.
      Proteins 8:82-101(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    14. "Functional implication of disulfide bond, Cys250 -Cys283, in bovine chymosin."
      Huang K., Zhang Z., Liu N., Zhang Y., Zhang G., Yang K.
      Biochem. Biophys. Res. Commun. 187:692-696(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-308 AND CYS-341.

    Entry informationi

    Entry nameiCHYM_BOVIN
    AccessioniPrimary (citable) accession number: P00794
    Secondary accession number(s): A8RRP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 132 of the entry and version 3 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