ID   CPXM1_MOUSE             Reviewed;         722 AA.
AC   Q9Z100; A2BI86; Q99LA3;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=Probable carboxypeptidase X1;
DE            EC=3.4.17.-;
DE   AltName: Full=Metallocarboxypeptidase CPX-1;
DE   Flags: Precursor;
GN   Name=Cpxm1; Synonyms=Cpx1, Cpxm;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Heart;
RX   PubMed=10073577; DOI=10.1089/104454999315565;
RA   Lei Y., Xin X., Morgan D., Pintar J.E., Fricker L.D.;
RT   "Identification of mouse CPX-1, a novel member of the
RT   metallocarboxypeptidase gene family with highest similarity to CPX-2.";
RL   DNA Cell Biol. 18:175-185(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in cell-cell interactions. No
CC       carboxypeptidase activity was found yet.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in testis and spleen. Moderately
CC       expressed in salivary gland, brain, heart, lung, and kidney. Extremely
CC       low expression in liver and muscle. No expression in eye, adrenal, and
CC       white adipose tissues. {ECO:0000269|PubMed:10073577}.
CC   -!- DEVELOPMENTAL STAGE: First expressed at 13.5 dpc, in the meninges,
CC       nasal mesenchyme, primordial cartilage and skeletal structures.
CC       {ECO:0000269|PubMed:10073577}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; AF077738; AAD15985.1; -; mRNA.
DR   EMBL; BX890605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466519; EDL28262.1; -; Genomic_DNA.
DR   EMBL; BC003713; AAH03713.1; -; mRNA.
DR   CCDS; CCDS16740.1; -.
DR   RefSeq; NP_062670.2; NM_019696.2.
DR   AlphaFoldDB; Q9Z100; -.
DR   SMR; Q9Z100; -.
DR   BioGRID; 207866; 3.
DR   STRING; 10090.ENSMUSP00000028897; -.
DR   MEROPS; M14.015; -.
DR   GlyCosmos; Q9Z100; 5 sites, No reported glycans.
DR   GlyGen; Q9Z100; 5 sites.
DR   iPTMnet; Q9Z100; -.
DR   PhosphoSitePlus; Q9Z100; -.
DR   MaxQB; Q9Z100; -.
DR   PaxDb; 10090-ENSMUSP00000028897; -.
DR   ProteomicsDB; 283818; -.
DR   Antibodypedia; 23301; 101 antibodies from 21 providers.
DR   DNASU; 56264; -.
DR   Ensembl; ENSMUST00000028897.8; ENSMUSP00000028897.8; ENSMUSG00000027408.8.
DR   GeneID; 56264; -.
DR   KEGG; mmu:56264; -.
DR   UCSC; uc008mir.2; mouse.
DR   AGR; MGI:1934569; -.
DR   CTD; 56265; -.
DR   MGI; MGI:1934569; Cpxm1.
DR   VEuPathDB; HostDB:ENSMUSG00000027408; -.
DR   eggNOG; KOG2649; Eukaryota.
DR   GeneTree; ENSGT00940000156141; -.
DR   HOGENOM; CLU_006722_4_0_1; -.
DR   InParanoid; Q9Z100; -.
DR   OMA; TDRRPCH; -.
DR   OrthoDB; 5490979at2759; -.
DR   PhylomeDB; Q9Z100; -.
DR   TreeFam; TF315592; -.
DR   BioGRID-ORCS; 56264; 4 hits in 80 CRISPR screens.
DR   PRO; PR:Q9Z100; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9Z100; Protein.
DR   Bgee; ENSMUSG00000027408; Expressed in vault of skull and 227 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR   CDD; cd00057; FA58C; 1.
DR   CDD; cd03869; M14_CPX_like; 1.
DR   CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11532:SF43; CARBOXYPEPTIDASE X1-RELATED; 1.
DR   PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS52035; PEPTIDASE_M14; 1.
DR   Genevisible; Q9Z100; MM.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..722
FT                   /note="Probable carboxypeptidase X1"
FT                   /id="PRO_0000004408"
FT   DOMAIN          103..263
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DOMAIN          287..610
FT                   /note="Peptidase M14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   REGION          30..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        580
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   BINDING         352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   BINDING         487
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        105..263
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   CONFLICT        253
FT                   /note="A -> V (in Ref. 1; AAD15985)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   722 AA;  80907 MW;  CC365C119420A9D4 CRC64;
     MWGLLLAVTA FAPSVGLGLG APSASVPGLA PGSTLAPHSS VAQPSTKANE TSERHVRLRV
     IKKKKIVVKK RKKLRHPGPL GTARPVVPTH PAKTLTLPEK QEPGCPPLGL ESLRVSDSQL
     EASSSQSFGL GAHRGRLNIQ SGLEDGDLYD GAWCAEQQDT EPWLQVDAKN PVRFAGIVTQ
     GRNSVWRYDW VTSFKVQFSN DSQTWWKSRN STGMDIVFPA NSDAETPVLN LLPEPQVARF
     IRLLPQTWFQ GGAPCLRAEI LACPVSDPND LFPEAHTLGS SNSLDFRHHN YKAMRKLMKQ
     VNEQCPNITR IYSIGKSHQG LKLYVMEMSD HPGEHELGEP EVRYVAGMHG NEALGRELLL
     LLMQFLCHEF LRGDPRVTRL LTETRIHLLP SMNPDGYETA YHRGSELVGW AEGRWTHQGI
     DLNHNFADLN TQLWYAEDDG LVPDTVPNHH LPLPTYYTLP NATVAPETWA VIKWMKRIPF
     VLSANLHGGE LVVSYPFDMT RTPWAARELT PTPDDAVFRW LSTVYAGTNR AMQDTDRRPC
     HSQDFSLHGN VINGADWHTV PGSMNDFSYL HTNCFEVTVE LSCDKFPHEK ELPQEWENNK
     DALLTYLEQV RMGITGVVRD KDTELGIADA VIAVEGINHD VTTAWGGDYW RLLTPGDYVV
     TASAEGYHTV RQHCQVTFEE GPVPCNFLLT KTPKERLREL LATRGKLPPD LRRKLERLRG
     QK
//