CPXM1_MOUSE
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 03-AUG-2022, entry version 160.
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. Moderatly
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; 2.
DR STRING; 10090.ENSMUSP00000028897; -.
DR MEROPS; M14.015; -.
DR GlyGen; Q9Z100; 5 sites.
DR iPTMnet; Q9Z100; -.
DR PhosphoSitePlus; Q9Z100; -.
DR MaxQB; Q9Z100; -.
DR PaxDb; Q9Z100; -.
DR PRIDE; Q9Z100; -.
DR ProteomicsDB; 283818; -.
DR Antibodypedia; 23301; 95 antibodies from 21 providers.
DR DNASU; 56264; -.
DR Ensembl; ENSMUST00000028897; ENSMUSP00000028897; ENSMUSG00000027408.
DR GeneID; 56264; -.
DR KEGG; mmu:56264; -.
DR UCSC; uc008mir.2; mouse.
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; 101221at2759; -.
DR PhylomeDB; Q9Z100; -.
DR TreeFam; TF315592; -.
DR BioGRID-ORCS; 56264; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q9Z100; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9Z100; protein.
DR Bgee; ENSMUSG00000027408; Expressed in vault of skull and 225 other tissues.
DR Genevisible; Q9Z100; MM.
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 InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000834; Peptidase_M14.
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; SSF49464; 1.
DR SUPFAM; SSF49785; SSF49785; 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.
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 REGION 30..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 580
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 487
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
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
