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Protein

Mast cell carboxypeptidase A

Gene

Cpa3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi171 – 1711Zinc; catalyticBy similarity
Metal bindingi174 – 1741Zinc; catalyticBy similarity
Metal bindingi299 – 2991Zinc; catalyticBy similarity
Active sitei373 – 3731Proton donor/acceptorBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Mast cell carboxypeptidase A (EC:3.4.17.1)
Alternative name(s):
Carboxypeptidase A3
R-CPA
RMC-CP
Gene namesi
Name:Cpa3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2390. Cpa3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 10›10By similarity
Propeptidei11 – 10494Activation peptidePRO_0000004399Add
BLAST
Chaini105 – 412308Mast cell carboxypeptidase APRO_0000004400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi168 ↔ 181By similarity
Disulfide bondi240 ↔ 263By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP21961.
PRIDEiP21961.

PTM databases

PhosphoSiteiP21961.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014970.

Structurei

3D structure databases

ProteinModelPortaliP21961.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2650. Eukaryota.
COG2866. LUCA.
HOGENOMiHOG000252968.
HOVERGENiHBG050815.
InParanoidiP21961.
KOiK08780.
PhylomeDBiP21961.

Family and domain databases

Gene3Di3.30.70.340. 1 hit.
InterProiIPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[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: Fragment.

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

P21961-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LMGVIYSTLA IAPVQFDREK VFRVKLQDEK QASILKNLTQ TIELDFWYPD
60 70 80 90 100
AIHDIAVNMT VDFRVTEKES QTIQSTLEQH KMDYEILIND LQEEIDKQFD
110 120 130 140 150
VKEEIAGRHS YAKYNDWNKI VSWTEKMVEK HPEMVSRIKI GSTVEDNPLY
160 170 180 190 200
VLKIGRKDGE RKAIFMDCGI HAREWVSPAF CQWFVYQAAK SYGKNKIMTK
210 220 230 240 250
LLDRMNFYVL PVFNVDGYIW SWTKDRMWRK NRSKNPNSTC IGTDLNRNFD
260 270 280 290 300
VSWDSSPNTD NPCLSVYRGP APESEKETKA VTNFIRSHLN SIKAYITFHS
310 320 330 340 350
YSQMLLFPYG YTIKLPPNHQ DLLKVARIAT DVLSSRYETR YIYGPIASTI
360 370 380 390 400
YKTSGSSLDW AYDLGIKHTF AFELRDKGKS GFLLPESRIK PTCKETMLSV
410
KFIAKYILKH TS
Length:412
Mass (Da):47,944
Last modified:April 13, 2004 - v2
Checksum:iDAB59555FC49137D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Sequence conflicti196 – 1961K → N AA sequence (PubMed:1988052).Curated
Sequence conflicti237 – 2371N → S AA sequence (PubMed:1988052).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67914 mRNA. Translation: AAB48267.1.
PIRiA38395.
RefSeqiNP_062173.1. NM_019300.1.
UniGeneiRn.10700.

Genome annotation databases

GeneIDi54242.
KEGGirno:54242.
UCSCiRGD:2390. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67914 mRNA. Translation: AAB48267.1.
PIRiA38395.
RefSeqiNP_062173.1. NM_019300.1.
UniGeneiRn.10700.

3D structure databases

ProteinModelPortaliP21961.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014970.

PTM databases

PhosphoSiteiP21961.

Proteomic databases

PaxDbiP21961.
PRIDEiP21961.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi54242.
KEGGirno:54242.
UCSCiRGD:2390. rat.

Organism-specific databases

CTDi1359.
RGDi2390. Cpa3.

Phylogenomic databases

eggNOGiKOG2650. Eukaryota.
COG2866. LUCA.
HOGENOMiHOG000252968.
HOVERGENiHBG050815.
InParanoidiP21961.
KOiK08780.
PhylomeDBiP21961.

Miscellaneous databases

NextBioi610704.

Family and domain databases

Gene3Di3.30.70.340. 1 hit.
InterProiIPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[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...

Publicationsi

  1. "Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations."
    Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.
    J. Exp. Med. 185:13-29(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "Rat mast cell carboxypeptidase: amino acid sequence and evidence of enzyme activity within mast cell granules."
    Cole K.R., Kumar S., le Trong H., Woodbury R.G., Walsh K.A., Neurath H.
    Biochemistry 30:648-655(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 104-412.

Entry informationi

Entry nameiCBPA3_RAT
AccessioniPrimary (citable) accession number: P21961
Secondary accession number(s): P97597
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: April 13, 2004
Last modified: May 11, 2016
This is version 127 of the entry and version 2 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

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.