CBPA5_MOUSE
ID CBPA5_MOUSE Reviewed; 436 AA.
AC Q8R4H4;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Carboxypeptidase A5;
DE EC=3.4.17.-;
DE Flags: Precursor;
GN Name=Cpa5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=11836249; DOI=10.1074/jbc.m112254200;
RA Wei S., Segura S., Vendrell J., Aviles F.X., Lanoue E., Day R., Feng Y.,
RA Fricker L.D.;
RT "Identification and characterization of three members of the human
RT metallocarboxypeptidase gene family.";
RL J. Biol. Chem. 277:14954-14964(2002).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in testis germ cells.
CC {ECO:0000269|PubMed:11836249}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF466283; AAM19306.1; -; mRNA.
DR CCDS; CCDS19976.1; -.
DR RefSeq; NP_653120.1; NM_144537.4.
DR RefSeq; XP_006505251.1; XM_006505188.1.
DR RefSeq; XP_006505253.1; XM_006505190.3.
DR RefSeq; XP_017177284.1; XM_017321795.1.
DR AlphaFoldDB; Q8R4H4; -.
DR SMR; Q8R4H4; -.
DR STRING; 10090.ENSMUSP00000057722; -.
DR MEROPS; M14.020; -.
DR PhosphoSitePlus; Q8R4H4; -.
DR PaxDb; Q8R4H4; -.
DR PRIDE; Q8R4H4; -.
DR ProteomicsDB; 265346; -.
DR Antibodypedia; 32057; 97 antibodies from 24 providers.
DR DNASU; 74649; -.
DR Ensembl; ENSMUST00000062758; ENSMUSP00000057722; ENSMUSG00000029788.
DR Ensembl; ENSMUST00000115139; ENSMUSP00000110792; ENSMUSG00000029788.
DR GeneID; 74649; -.
DR KEGG; mmu:74649; -.
DR UCSC; uc009bfp.1; mouse.
DR CTD; 93979; -.
DR MGI; MGI:1921899; Cpa5.
DR VEuPathDB; HostDB:ENSMUSG00000029788; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000161666; -.
DR HOGENOM; CLU_019326_0_0_1; -.
DR InParanoid; Q8R4H4; -.
DR OMA; AAWGQMN; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; Q8R4H4; -.
DR TreeFam; TF317197; -.
DR BioGRID-ORCS; 74649; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8R4H4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8R4H4; protein.
DR Bgee; ENSMUSG00000029788; Expressed in spermatid and 10 other tissues.
DR ExpressionAtlas; Q8R4H4; baseline and differential.
DR Genevisible; Q8R4H4; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd03870; M14_CPA; 1.
DR Gene3D; 3.30.70.340; -; 1.
DR InterPro; IPR034248; CPA_M14_CPD.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Cleavage on pair of basic residues; Disulfide bond;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..126
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004363"
FT CHAIN 127..436
FT /note="Carboxypeptidase A5"
FT /id="PRO_0000004364"
FT ACT_SITE 397
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 196..199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 271..272
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 324..325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT DISULFID 265..288
FT /evidence="ECO:0000250|UniProtKB:Q96IY4"
SQ SEQUENCE 436 AA; 49151 MW; 798EE817B7EC21F4 CRC64;
MQGTQRGGLV PGLSPLDRRT LLFCNFILAV AWGQVNFTGD QVLRVLAKNE KQLSLLRDLE
TQKPQKVDFW RGPARPSLPV DMRVPFSELP SVKAYLKSHG LAYSIMIKDI QVLLDEERDA
MAKSRRLERS TNSFSYSSYH TLDEIYSWID NFVAEHSNLV SKIHIGKSFE NRSILVLKFS
TGGPNRPAIW IDTGIHSREW ITHATGIWIS QKIVNAYGKD HVLKRILNTM DIFIEIVTNP
DGFAFTHSMN RLWRKNKSSQ PGIFCIGVDL NRNWKAGFGG NGSNKNPCSE TYRGPAPESE
PEVAAIVDFI TGHGNFKAMI SIHSYSQMVM YPYGHSLEPV PNHEELFNLA KDAVKALNKV
HGIQYIFGSI STTLYSASGI SVDWAYDSGI KYAFSFELRD TGQYGFLLPA SQIVPTAEET
WMALQTIMKH TLNHPY
