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Database: UniProt
Entry: Q9Z100
LinkDB: Q9Z100
Original site: Q9Z100 
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   29-OCT-2014, entry version 124.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   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-
RT   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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: Binds 1 zinc ion per subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in testis and spleen.
CC       Moderatly expressed in salivary gland, brain, heart, lung, and
CC       kidney. Extremely low expression in liver and muscle. No
CC       expression in eye, adrenal, and white adipose tissues.
CC       {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}.
CC   -!- SIMILARITY: Contains 1 F5/8 type C domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00081}.
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DR   EMBL; AF077738; AAD15985.1; -; mRNA.
DR   EMBL; BX890605; CAM20117.1; -; 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   UniGene; Mm.112701; -.
DR   ProteinModelPortal; Q9Z100; -.
DR   SMR; Q9Z100; 107-263, 284-667.
DR   STRING; 10090.ENSMUSP00000028897; -.
DR   MEROPS; M14.952; -.
DR   PhosphoSite; Q9Z100; -.
DR   PRIDE; Q9Z100; -.
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   eggNOG; NOG322453; -.
DR   GeneTree; ENSGT00760000119124; -.
DR   HOGENOM; HOG000232185; -.
DR   HOVERGEN; HBG003410; -.
DR   InParanoid; Q9Z100; -.
DR   KO; K08638; -.
DR   OMA; RYDWVTS; -.
DR   OrthoDB; EOG7B8S32; -.
DR   TreeFam; TF315592; -.
DR   NextBio; 312152; -.
DR   PRO; PR:Q9Z100; -.
DR   Bgee; Q9Z100; -.
DR   ExpressionAtlas; Q9Z100; baseline and differential.
DR   Genevestigator; Q9Z100; -.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.1120; -; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR014766; CarboxyPept_regulatory_dom.
DR   InterPro; IPR000421; Coagulation_fac_5/8-C_type_dom.
DR   InterPro; IPR008979; Galactose-bd-like.
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; Complete proteome; Disulfide bond; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    722       Probable carboxypeptidase X1.
FT                                /FTId=PRO_0000004408.
FT   DOMAIN      103    263       F5/8 type C. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   COMPBIAS     62     65       Poly-Lys.
FT   COMPBIAS    358    362       Poly-Leu.
FT   ACT_SITE    580    580       Nucleophile. {ECO:0000250}.
FT   METAL       349    349       Zinc. {ECO:0000250}.
FT   METAL       352    352       Zinc. {ECO:0000250}.
FT   METAL       487    487       Zinc. {ECO:0000250}.
FT   CARBOHYD     49     49       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    200    200       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    210    210       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    307    307       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    461    461       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    105    263       {ECO:0000255|PROSITE-ProRule:PRU00081}.
FT   CONFLICT    253    253       A -> V (in Ref. 1; AAD15985).
FT                                {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
//
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