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P00794

- CHYM_BOVIN

UniProt

P00794 - CHYM_BOVIN

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Protein

Chymosin

Gene

CYM

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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.

Expressioni

Gene expression databases

ExpressionAtlasiP00794. baseline.

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.
GeneTreeiENSGT00760000118929.
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

        10         20         30         40         50
MRCLVVLLAV FALSQGAEIT RIPLYKGKSL RKALKEHGLL EDFLQKQQYG
60 70 80 90 100
ISSKYSGFGE VASVPLTNYL DSQYFGKIYL GTPPQEFTVL FDTGSSDFWV
110 120 130 140 150
PSIYCKSNAC KNHQRFDPRK SSTFQNLGKP LSIHYGTGSM QGILGYDTVT
160 170 180 190 200
VSNIVDIQQT VGLSTQEPGD VFTYAEFDGI LGMAYPSLAS EYSIPVFDNM
210 220 230 240 250
MNRHLVAQDL FSVYMDRNGQ ESMLTLGAID PSYYTGSLHW VPVTVQQYWQ
260 270 280 290 300
FTVDSVTISG VVVACEGGCQ AILDTGTSKL VGPSSDILNI QQAIGATQNQ
310 320 330 340 350
YGEFDIDCDN LSYMPTVVFE INGKMYPLTP SAYTSQDQGF CTSGFQSENH
360 370 380
SQKWILGDVF IREYYSVFDR ANNLVGLAKA I
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 ENSGT00760000118929.
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.

Gene expression databases

ExpressionAtlasi P00794. baseline.

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 29, 2014
This is version 133 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