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 01-MAY-2013, entry version 110.
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 (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted (Probable).
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 -!- DEVELOPMENTAL STAGE: First expressed at 13.5 dpc, in the meninges,
CC nasal mesenchyme, primordial cartilage and skeletal structures.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC -!- SIMILARITY: Contains 1 F5/8 type C domain.
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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 IPI; IPI00129310; -.
DR RefSeq; NP_062670.2; NM_019696.2.
DR UniGene; Mm.112701; -.
DR ProteinModelPortal; Q9Z100; -.
DR SMR; Q9Z100; 100-263, 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 CTD; 56265; -.
DR MGI; MGI:1934569; Cpxm1.
DR eggNOG; NOG322453; -.
DR GeneTree; ENSGT00680000099712; -.
DR HOGENOM; HOG000232185; -.
DR HOVERGEN; HBG003410; -.
DR InParanoid; A2BI86; -.
DR KO; K08638; -.
DR OMA; WAARELT; -.
DR OrthoDB; EOG4K9BBS; -.
DR NextBio; 312152; -.
DR ArrayExpress; Q9Z100; -.
DR Bgee; Q9Z100; -.
DR Genevestigator; Q9Z100; -.
DR GermOnline; ENSMUSG00000027408; Mus musculus.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0008237; F:metallopeptidase 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; 2.60.40.1120; -; 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; CarboxypepD_reg; 1.
DR SUPFAM; SSF49785; Gal_bind_like; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; FALSE_NEG.
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 Potential.
FT CHAIN 21 722 Probable carboxypeptidase X1.
FT /FTId=PRO_0000004408.
FT DOMAIN 103 263 F5/8 type C.
FT COMPBIAS 62 65 Poly-Lys.
FT COMPBIAS 358 362 Poly-Leu.
FT ACT_SITE 580 580 Nucleophile (By similarity).
FT METAL 349 349 Zinc (By similarity).
FT METAL 352 352 Zinc (By similarity).
FT METAL 487 487 Zinc (By similarity).
FT CARBOHYD 49 49 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 200 200 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 210 210 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 307 307 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 461 461 N-linked (GlcNAc...) (Potential).
FT DISULFID 105 263 By similarity.
FT CONFLICT 253 253 A -> V (in Ref. 1; AAD15985).
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
//
