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Protein

Carboxypeptidase A1

Gene

CPA1

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

Functioni

Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.By similarity

Catalytic activityi

Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi179Zinc; catalyticCombined sources1 Publication1
Metal bindingi182Zinc; catalyticCombined sources1 Publication1
Binding sitei237SubstrateCombined sources1 Publication1
Metal bindingi306Zinc; catalyticCombined sources1 Publication1
Binding sitei358SubstrateCombined sources1 Publication1
Active sitei380Proton donor/acceptorBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.1. 908.
SABIO-RKP00730.

Protein family/group databases

MEROPSiM14.001.

Chemistry databases

SwissLipidsiSLP:000001634.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase A1 (EC:3.4.17.1)
Gene namesi
Name:CPA1
Synonyms:CPA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3481.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 161 PublicationAdd BLAST16
PropeptideiPRO_000000434317 – 110Activation peptide1 PublicationAdd BLAST94
ChainiPRO_0000004344111 – 419Carboxypeptidase A1Add BLAST309

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi248 ↔ 271By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP00730.
PRIDEiP00730.

Expressioni

Tissue specificityi

Pancreas.1 Publication

Interactioni

Subunit structurei

Monomer. The zymogen is secreted as a ternary complex composed of procarboxypeptidase A, chymotrypsinogen C and proproteinase E.6 Publications

Protein-protein interaction databases

DIPiDIP-44716N.
MINTiMINT-1505101.
STRINGi9913.ENSBTAP00000009745.

Chemistry databases

BindingDBiP00730.

Structurei

Secondary structure

1419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 29Combined sources6
Helixi33 – 40Combined sources8
Turni41 – 43Combined sources3
Helixi46 – 48Combined sources3
Beta strandi51 – 54Combined sources4
Beta strandi63 – 67Combined sources5
Helixi69 – 81Combined sources13
Beta strandi85 – 91Combined sources7
Helixi93 – 106Combined sources14
Turni114 – 116Combined sources3
Beta strandi119 – 121Combined sources3
Helixi125 – 138Combined sources14
Turni140 – 142Combined sources3
Beta strandi143 – 150Combined sources8
Beta strandi156 – 162Combined sources7
Beta strandi164 – 168Combined sources5
Beta strandi171 – 176Combined sources6
Helixi183 – 199Combined sources17
Turni200 – 202Combined sources3
Helixi204 – 212Combined sources9
Beta strandi214 – 219Combined sources6
Helixi223 – 231Combined sources9
Beta strandi244 – 247Combined sources4
Helixi253 – 255Combined sources3
Beta strandi257 – 260Combined sources4
Beta strandi263 – 267Combined sources5
Beta strandi273 – 275Combined sources3
Helixi284 – 296Combined sources13
Beta strandi299 – 306Combined sources8
Beta strandi311 – 315Combined sources5
Helixi326 – 341Combined sources16
Turni342 – 344Combined sources3
Beta strandi349 – 352Combined sources4
Helixi353 – 356Combined sources4
Helixi364 – 370Combined sources7
Beta strandi375 – 380Combined sources6
Beta strandi384 – 387Combined sources4
Helixi388 – 390Combined sources3
Helixi393 – 395Combined sources3
Helixi396 – 416Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ARLX-ray1.88A111-417[»]
1ARMX-ray1.76A111-419[»]
1BAVX-ray1.60A/B/C/D111-419[»]
1CBXX-ray2.00A111-417[»]
1CPSX-ray2.25A111-417[»]
1CPXX-ray2.00A111-417[»]
1EE3X-ray1.70P111-419[»]
1ELLX-ray1.76P111-419[»]
1ELMX-ray2.00P111-419[»]
1F57X-ray1.75A111-417[»]
1HDQX-ray2.30A111-417[»]
1HDUX-ray1.75A/B/D/E111-414[»]
1HEEX-ray1.75A/B/D/E111-414[»]
1IY7X-ray2.00A111-417[»]
1M4LX-ray1.25A111-417[»]
1PYTX-ray2.35A17-110[»]
B111-419[»]
1YMEX-ray1.53A111-419[»]
1ZLHX-ray1.70A111-419[»]
2ABZX-ray2.16A/B111-419[»]
2CTBX-ray1.50A111-417[»]
2CTCX-ray1.40A111-417[»]
2RFHX-ray1.70A111-417[»]
3CPAX-ray2.00A111-417[»]
3FVLX-ray1.85A/C/E111-417[»]
3FX6X-ray1.85A/C/E111-417[»]
3I1UX-ray1.39A111-419[»]
3KGQX-ray1.70A111-419[»]
4CPAX-ray2.50A/B111-417[»]
5CPAX-ray1.54A111-417[»]
6CPAX-ray2.00A111-417[»]
7CPAX-ray2.00A111-417[»]
8CPAX-ray2.00A111-417[»]
ProteinModelPortaliP00730.
SMRiP00730.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00730.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni179 – 182Substrate bindingCombined sources1 Publication4
Regioni254 – 255Substrate bindingCombined sources1 Publication2
Regioni307 – 308Substrate bindingCombined sources1 Publication2

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2650. Eukaryota.
COG2866. LUCA.
HOGENOMiHOG000252967.
HOVERGENiHBG050815.
InParanoidiP00730.
KOiK08779.

Family and domain databases

Gene3Di3.30.70.340. 1 hit.
InterProiIPR003146. M14A_act_pep.
IPR000834. Peptidase_M14.
IPR009020. Propept_inh.
[Graphical view]
PfamiPF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF54897. SSF54897. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00730-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQGLLILSVL LGAALGKEDF VGHQVLRITA ADEAEVQTVK ELEDLEHLQL
60 70 80 90 100
DFWRGPGQPG SPIDVRVPFP SLQAVKVFLE AHGIRYRIMI EDVQSLLDEE
110 120 130 140 150
QEQMFASQSR ARSTNTFNYA TYHTLDEIYD FMDLLVAEHP QLVSKLQIGR
160 170 180 190 200
SYEGRPIYVL KFSTGGSNRP AIWIDLGIHS REWITQATGV WFAKKFTEDY
210 220 230 240 250
GQDPSFTAIL DSMDIFLEIV TNPDGFAFTH SQNRLWRKTR SVTSSSLCVG
260 270 280 290 300
VDANRNWDAG FGKAGASSSP CSETYHGKYA NSEVEVKSIV DFVKDHGNFK
310 320 330 340 350
AFLSIHSYSQ LLLYPYGYTT QSIPDKTELN QVAKSAVEAL KSLYGTSYKY
360 370 380 390 400
GSIITTIYQA SGGSIDWSYN QGIKYSFTFE LRDTGRYGFL LPASQIIPTA
410
QETWLGVLTI MEHTLNNLY
Length:419
Mass (Da):47,082
Last modified:November 1, 1991 - v3
Checksum:i21B86407B3BFC452
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti95S → L AA sequence (PubMed:3147705).Curated1
Sequence conflicti199D → N AA sequence (PubMed:5102489).Curated1
Sequence conflicti203D → N AA sequence (PubMed:5102489).Curated1
Sequence conflicti224D → N AA sequence (PubMed:5102489).Curated1
Sequence conflicti232Q → E AA sequence (PubMed:5102489).Curated1
Sequence conflicti295D → N AA sequence (PubMed:5102489).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti289I → V in allelic variant. 1 Publication1
Natural varianti338E → A in allelic variant. 1 Publication1
Natural varianti415L → V in allelic variant. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61851 mRNA. Translation: AAA30426.1.
Z33906 mRNA. Translation: CAA83955.1.
PIRiJN0126. CPBOA.
RefSeqiNP_777175.1. NM_174750.2.
UniGeneiBt.4052.

Genome annotation databases

GeneIDi286762.
KEGGibta:286762.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61851 mRNA. Translation: AAA30426.1.
Z33906 mRNA. Translation: CAA83955.1.
PIRiJN0126. CPBOA.
RefSeqiNP_777175.1. NM_174750.2.
UniGeneiBt.4052.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ARLX-ray1.88A111-417[»]
1ARMX-ray1.76A111-419[»]
1BAVX-ray1.60A/B/C/D111-419[»]
1CBXX-ray2.00A111-417[»]
1CPSX-ray2.25A111-417[»]
1CPXX-ray2.00A111-417[»]
1EE3X-ray1.70P111-419[»]
1ELLX-ray1.76P111-419[»]
1ELMX-ray2.00P111-419[»]
1F57X-ray1.75A111-417[»]
1HDQX-ray2.30A111-417[»]
1HDUX-ray1.75A/B/D/E111-414[»]
1HEEX-ray1.75A/B/D/E111-414[»]
1IY7X-ray2.00A111-417[»]
1M4LX-ray1.25A111-417[»]
1PYTX-ray2.35A17-110[»]
B111-419[»]
1YMEX-ray1.53A111-419[»]
1ZLHX-ray1.70A111-419[»]
2ABZX-ray2.16A/B111-419[»]
2CTBX-ray1.50A111-417[»]
2CTCX-ray1.40A111-417[»]
2RFHX-ray1.70A111-417[»]
3CPAX-ray2.00A111-417[»]
3FVLX-ray1.85A/C/E111-417[»]
3FX6X-ray1.85A/C/E111-417[»]
3I1UX-ray1.39A111-419[»]
3KGQX-ray1.70A111-419[»]
4CPAX-ray2.50A/B111-417[»]
5CPAX-ray1.54A111-417[»]
6CPAX-ray2.00A111-417[»]
7CPAX-ray2.00A111-417[»]
8CPAX-ray2.00A111-417[»]
ProteinModelPortaliP00730.
SMRiP00730.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-44716N.
MINTiMINT-1505101.
STRINGi9913.ENSBTAP00000009745.

Chemistry databases

BindingDBiP00730.
ChEMBLiCHEMBL3481.
SwissLipidsiSLP:000001634.

Protein family/group databases

MEROPSiM14.001.

Proteomic databases

PaxDbiP00730.
PRIDEiP00730.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi286762.
KEGGibta:286762.

Organism-specific databases

CTDi1357.

Phylogenomic databases

eggNOGiKOG2650. Eukaryota.
COG2866. LUCA.
HOGENOMiHOG000252967.
HOVERGENiHBG050815.
InParanoidiP00730.
KOiK08779.

Enzyme and pathway databases

BRENDAi3.4.17.1. 908.
SABIO-RKP00730.

Miscellaneous databases

EvolutionaryTraceiP00730.
PROiP00730.

Family and domain databases

Gene3Di3.30.70.340. 1 hit.
InterProiIPR003146. M14A_act_pep.
IPR000834. Peptidase_M14.
IPR009020. Propept_inh.
[Graphical view]
PfamiPF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF54897. SSF54897. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBPA1_BOVIN
AccessioniPrimary (citable) accession number: P00730
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1991
Last modified: November 30, 2016
This is version 161 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.