CBPM_MOUSE
ID CBPM_MOUSE Reviewed; 443 AA.
AC Q80V42; Q497S5; Q9CYH8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Carboxypeptidase M;
DE Short=CPM;
DE EC=3.4.17.12;
DE Flags: Precursor;
GN Name=Cpm;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=129, and C57BL/6J; TISSUE=Kidney, and 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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Specifically removes C-terminal basic residues (Arg or Lys)
CC from peptides and proteins. It is believed to play important roles in
CC the control of peptide hormone and growth factor activity at the cell
CC surface, and in the membrane-localized degradation of extracellular
CC proteins (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of C-terminal arginine or lysine residues from
CC polypeptides.; EC=3.4.17.12;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80V42-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80V42-2; Sequence=VSP_014606, VSP_014607;
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47389.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK017670; BAB30865.1; -; mRNA.
DR EMBL; BC047389; AAH47389.1; ALT_INIT; mRNA.
DR EMBL; BC100404; AAI00405.1; -; mRNA.
DR CCDS; CCDS48696.1; -. [Q80V42-1]
DR RefSeq; NP_081744.1; NM_027468.1. [Q80V42-1]
DR AlphaFoldDB; Q80V42; -.
DR SMR; Q80V42; -.
DR BioGRID; 214144; 1.
DR STRING; 10090.ENSMUSP00000020399; -.
DR MEROPS; M14.006; -.
DR GlyConnect; 2186; 10 N-Linked glycans (3 sites).
DR GlyGen; Q80V42; 4 sites, 10 N-linked glycans (3 sites).
DR PhosphoSitePlus; Q80V42; -.
DR SwissPalm; Q80V42; -.
DR EPD; Q80V42; -.
DR jPOST; Q80V42; -.
DR MaxQB; Q80V42; -.
DR PaxDb; Q80V42; -.
DR PeptideAtlas; Q80V42; -.
DR PRIDE; Q80V42; -.
DR ProteomicsDB; 265681; -. [Q80V42-1]
DR ProteomicsDB; 265682; -. [Q80V42-2]
DR Antibodypedia; 975; 358 antibodies from 35 providers.
DR DNASU; 70574; -.
DR Ensembl; ENSMUST00000020399; ENSMUSP00000020399; ENSMUSG00000020183. [Q80V42-1]
DR GeneID; 70574; -.
DR KEGG; mmu:70574; -.
DR UCSC; uc007hdi.2; mouse. [Q80V42-1]
DR UCSC; uc007hdk.2; mouse. [Q80V42-2]
DR CTD; 1368; -.
DR MGI; MGI:1917824; Cpm.
DR VEuPathDB; HostDB:ENSMUSG00000020183; -.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000158580; -.
DR HOGENOM; CLU_006722_1_0_1; -.
DR InParanoid; Q80V42; -.
DR OMA; IWAQCLE; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; Q80V42; -.
DR TreeFam; TF315592; -.
DR BRENDA; 3.4.17.12; 3474.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 70574; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cpm; mouse.
DR PRO; PR:Q80V42; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q80V42; protein.
DR Bgee; ENSMUSG00000020183; Expressed in left lung lobe and 232 other tissues.
DR Genevisible; Q80V42; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd03866; M14_CPM; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR033842; CPM_N.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; SSF49464; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carboxypeptidase; Cell membrane; Disulfide bond;
KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..423
FT /note="Carboxypeptidase M"
FT /id="PRO_0000004392"
FT PROPEP 424..443
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000251911"
FT ACT_SITE 281
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT LIPID 423
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 138..285
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT DISULFID 242..284
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT DISULFID 341..410
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT VAR_SEQ 1..255
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014606"
FT VAR_SEQ 256..262
FT /note="YSWYPLQ -> MRCACFA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014607"
SQ SEQUENCE 443 AA; 50556 MW; AC7F6F9E35FA3271 CRC64;
MDRARLWLGL LLPVVAALDF RYHHQEGMEA FLKSVAQNYS SITHLHSIGK SVRGRNLWVL
VVGQTPKEHR VGIPEFKYVA NMHGDETVGR ELLLHLIDYL VSSYRKDPEI THLIDSTRIH
IMPSMNPDGF EAVQKPDCYY SNGRENYNNY DLNRNFPDAF ENNNVTKQPE TLAIMEWLKT
ETFVLSANLH GGALVASYPF DNGVQATGTL LSRSLTPDDD VFQHLAYTYA SRNPNMTKGD
QCKNKRNFPN GIINGYSWYP LQGGMQDYNY IWAQCFEITL ELSCCKYPRE EKLPLFWNDN
KASLIEYIKQ VHLGVKGQVF DQSGAPLPNV IVEVQDRKHI CPFRTNKLGE YYLLLLPGSY
VINVTVPGHD SYLTKLTIPG KSQPFSALKK DFHLPLRWQP DSISVSNPSC PMIPLYKFMP
SHSAATKPSL GVFFMTLLYV FFK
