LOCUS       NP_082202                420 aa            linear   ROD 05-JUN-2024
DEFINITION  carboxypeptidase A4 preproprotein [Mus musculus].
ACCESSION   NP_082202
VERSION     NP_082202.1
DBSOURCE    REFSEQ: accession NM_027926.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Gao,W., Guo,N., Zhao,S., Chen,Z., Zhang,W., Yan,F., Liao,H. and
            Chi,K.
  TITLE     Carboxypeptidase A4 promotes cardiomyocyte hypertrophy through
            activating PI3K-AKT-mTOR signaling
  JOURNAL   Biosci Rep 40 (5) (2020)
   PUBMED   32347291
  REMARK    GeneRIF: Carboxypeptidase A4 promotes cardiomyocyte hypertrophy
            through activating PI3K-AKT-mTOR signaling.
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Inagawa,M., Nakajima,K., Makino,T., Ogawa,S., Kojima,M., Ito,S.,
            Ikenishi,A., Hayashi,T., Schwartz,R.J., Nakamura,K., Obayashi,T.,
            Tachibana,M., Shinkai,Y., Maeda,K., Miyagawa-Tomita,S. and
            Takeuchi,T.
  TITLE     Histone H3 lysine 9 methyltransferases, G9a and GLP are essential
            for cardiac morphogenesis
  JOURNAL   Mech Dev 130 (11-12), 519-531 (2013)
   PUBMED   23892084
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Tanco,S., Zhang,X., Morano,C., Aviles,F.X., Lorenzo,J. and
            Fricker,L.D.
  TITLE     Characterization of the substrate specificity of human
            carboxypeptidase A4 and implications for a role in extracellular
            peptide processing
  JOURNAL   J Biol Chem 285 (24), 18385-18396 (2010)
   PUBMED   20385563
  REMARK    GeneRIF: CPA4 functions in neuropeptide processing and regulation
            in the extracellular environment
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Hald,J., Hjorth,J.P., German,M.S., Madsen,O.D., Serup,P. and
            Jensen,J.
  TITLE     Activated Notch1 prevents differentiation of pancreatic acinar
            cells and attenuate endocrine development
  JOURNAL   Dev Biol 260 (2), 426-437 (2003)
   PUBMED   12921743
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC155656.10, AK030705.1 and
            AK003823.1.
            
            Summary: This gene encodes a member of the carboxypeptidase A
            family of zinc metalloproteases that could be involved in the
            histone hyperacetylation pathway. The encoded preproprotein
            undergoes proteolytic processing that removes the N-terminal
            activation peptide to generate a functional enzyme. This gene is
            located in a cluster of carboxypeptidase genes on chromosome 6.
            [provided by RefSeq, Jul 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061206.1, AK030705.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849375,
                                           SAMN00849376 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 12.52 cM"
     Protein         1..420
                     /product="carboxypeptidase A4 preproprotein"
                     /EC_number="3.4.17.15"
                     /calculated_mol_wt=45617
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1740
     Region          27..101
                     /region_name="Propep_M14"
                     /note="Carboxypeptidase activation peptide; pfam02244"
                     /db_xref="CDD:460505"
     mat_peptide     114..420
                     /product="Carboxypeptidase A4. /id=PRO_0000004360"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P8K8.2)"
                     /calculated_mol_wt=34505
     Region          117..418
                     /region_name="M14_CPA"
                     /note="Peptidase M14 carboxypeptidase subfamily A/B-like;
                     Carboxypeptidase A subgroup; cd03870"
                     /db_xref="CDD:349442"
     Site            order(180,183,238,255..256,307,359,361,381)
                     /site_type="active"
                     /db_xref="CDD:349442"
     Site            order(182..183,238,274,307..309,350,355,357..360,381,390)
                     /site_type="active"
                     /note="inhibitor binding interface [active]"
                     /db_xref="CDD:349442"
     Site            259
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P8K8.2)"
     CDS             1..420
                     /gene="Cpa4"
                     /gene_synonym="1110019K20Rik"
                     /coded_by="NM_027926.3:26..1288"
                     /db_xref="CCDS:CCDS19975.1"
                     /db_xref="GeneID:71791"
                     /db_xref="MGI:MGI:1919041"
ORIGIN      
        1 mkwllffgal igagicgrdk ffgdqvfrin vrngdeirkl telvnsdhlk lsvwkspstf
       61 drpvdilvps vsllpvksfl ksqgldysvt iedlqalldn edeemqhneg iersgdfnyg
      121 ayhpleaiyh emdsiatdfp elvsrvkige tfekrpmyvl kfstgggkkr paiwlnagih
      181 arewisqata iwtarkivtd ykkdpaitsi lkkvdifllp vanpdgyvyt qsqnrlwrkt
      241 rsrnpgsrcv gadpnrnwna sfagegtsdn pcsevyhgsh pnsevevksv vdfiqkhgnf
      301 kcfidlhsys qllmypygyt vkkapdaeel ddvarnaaqa laslsgtkyr vgptcttvyp
      361 asgssvdway dngikyaftf elrdtgyygf llpasqiipt aeetwlglkt imehvrdhly
//
