CBPD_MOUSE
ID CBPD_MOUSE Reviewed; 1377 AA.
AC O89001; Q5SVH8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Carboxypeptidase D;
DE EC=3.4.17.22;
DE AltName: Full=Metallocarboxypeptidase D;
DE AltName: Full=gp180;
DE Flags: Precursor;
GN Name=Cpd;
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].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=9714835; DOI=10.1016/s0378-1119(98)00270-4;
RA Ishikawa T., Murakami K., Kido Y., Ohnishi S., Yazaki Y., Harada F.,
RA Kuroki K.;
RT "Cloning, functional expression, and chromosomal localization of the human
RT and mouse gp180-carboxypeptidase D-like enzyme.";
RL Gene 215:361-370(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Vagina;
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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1365 AND THR-1367, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-398; ASN-409 AND ASN-521.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-264; SER-269; SER-1355;
RP SER-1358; THR-1365 AND THR-1367, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Releases C-terminal Arg and Lys from polypeptides.;
CC EC=3.4.17.22;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q90240};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q90240};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q90240};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- DOMAIN: There are 3 carboxypeptidase-like domains. Only the first two
CC domains seem to have kept a catalytic activity.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; D85391; BAA33371.1; -; mRNA.
DR EMBL; AK137737; BAE23483.1; -; mRNA.
DR EMBL; AL645479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25071.1; -.
DR RefSeq; NP_031780.2; NM_007754.2.
DR AlphaFoldDB; O89001; -.
DR SMR; O89001; -.
DR BioGRID; 198853; 5.
DR IntAct; O89001; 2.
DR MINT; O89001; -.
DR STRING; 10090.ENSMUSP00000021201; -.
DR MEROPS; M14.011; -.
DR MEROPS; M14.016; -.
DR GlyConnect; 2184; 7 N-Linked glycans (7 sites).
DR GlyGen; O89001; 15 sites, 7 N-linked glycans (7 sites).
DR iPTMnet; O89001; -.
DR PhosphoSitePlus; O89001; -.
DR SwissPalm; O89001; -.
DR EPD; O89001; -.
DR jPOST; O89001; -.
DR MaxQB; O89001; -.
DR PaxDb; O89001; -.
DR PeptideAtlas; O89001; -.
DR PRIDE; O89001; -.
DR ProteomicsDB; 265566; -.
DR Antibodypedia; 26863; 106 antibodies from 26 providers.
DR DNASU; 12874; -.
DR Ensembl; ENSMUST00000021201; ENSMUSP00000021201; ENSMUSG00000020841.
DR GeneID; 12874; -.
DR KEGG; mmu:12874; -.
DR UCSC; uc007kga.1; mouse.
DR CTD; 1362; -.
DR MGI; MGI:107265; Cpd.
DR VEuPathDB; HostDB:ENSMUSG00000020841; -.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000156919; -.
DR HOGENOM; CLU_002495_1_0_1; -.
DR InParanoid; O89001; -.
DR OMA; DLWVMEI; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; O89001; -.
DR TreeFam; TF315592; -.
DR BRENDA; 3.4.17.22; 3474.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 12874; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cpd; mouse.
DR PRO; PR:O89001; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O89001; protein.
DR Bgee; ENSMUSG00000020841; Expressed in submandibular gland and 276 other tissues.
DR Genevisible; O89001; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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; cd03863; M14_CPD_II; 1.
DR CDD; cd06245; M14_CPD_III; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR034224; M14_CPD_II.
DR InterPro; IPR033848; M14_CPD_III.
DR InterPro; IPR015567; Pept_M14B_carboxypept_D2.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF73; PTHR11532:SF73; 3.
DR Pfam; PF00246; Peptidase_M14; 3.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 3.
DR SUPFAM; SSF49464; SSF49464; 3.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 2.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 2.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cell membrane; Glycoprotein; Hydrolase; Lipoprotein;
KW Membrane; Metal-binding; Metalloprotease; Palmitate; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..1377
FT /note="Carboxypeptidase D"
FT /id="PRO_0000004402"
FT TOPO_DOM 38..1296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1297..1317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1318..1377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 38..492
FT /note="Carboxypeptidase-like 1"
FT REGION 188..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..896
FT /note="Carboxypeptidase-like 2"
FT REGION 874..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..1296
FT /note="Carboxypeptidase-like 3"
FT REGION 1038..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 161..163
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 877..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 761
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P19222"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P19222"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P19222"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 670
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT SITE 349
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q90240"
FT MOD_RES 264
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1365
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1367
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT LIPID 1314
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 1318
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 1320
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 854
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 952
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 975
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1067
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 53
FT /note="S -> T (in Ref. 1; BAA33371)"
FT /evidence="ECO:0000305"
FT CONFLICT 1039..1040
FT /note="ER -> DG (in Ref. 1; BAA33371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1377 AA; 152406 MW; 73CC0861EE674053 CRC64;
MASGRDERPP WRLGRLRLLP PPPLLLLLLL LRSSAQAAHI KKAEATTTTV GGSEAAEGQF
DHYYHEAALG EALEAAAAAG PPGLARLFSI GSSVEGRPLW VLRLTAGLGP PPTAAAGLDA
AGPLLPGRPQ VKLVGNMHGD ETVSRQVLVY LARELASGYR RGDPRLVRLL NTTDVYLLPS
LNPDGFERAR EGDCGLGDSG PPGTSGRDNS RGRDLNRSFP DQFSTGEPPS LDEVPEVRAL
IDWIRRNKFV LSGNLHGGSV VASYPFDDSP EHKTTGLYSK TSDDEVFRYL AKAYASNHPI
MKTGEPHCPG DEDETFKDGI TNGAHWYDVE GGMQDYNYVW ANCFEITLEL SCCKYPPASQ
LRQEWENNRE SLITLIEKVH IGIKGFVKDS VTGSGLENAT ISVAGINHNI TTGRFGDFHR
LLVPGTYNLT ALSTGYMPLT INNIMVKEGP ATEMDFSLRP TVMSVMPGST EAVTTPGTVA
VPNIPPGTPS SHQPIQPKDF HHHHFPDMEI FLRRFANEYP NITRLYSLGK SVESRELYVM
EISDNPGVHE PGEPEFKYIG NMHGNEVVGR ELLLNLIEYL CKNFGTDPEV TDLVRSTRIH
LMPSMNPDGY EKSQEGDSIS VVGRNNSNNF DLNRNFPDQF VPITEPTQPE TIAVMSWVKA
YPFVLSANLH GGSLVVNYPY DDNEQGVATY SKSPDDAVFQ QIALSYSKEN SQMFQGRPCK
DMYLNEYFPH GITNGASWYN VPGGMQDWNY LQTNCFEVTI ELGCVKYPFE NELPKYWEQN
RRSLIQFMKQ VHQGVKGFVL DATDGRGILN ATLSVAEINH PVTTYKAGDY WRLLVPGTYK
ITASARGYNP VTKNVTVRSE GAVQVNFTLV RSSADANNES KKGRGHSTST DDTSDPTSKE
FEALIKHLSA ENGLEGFMLS SSSDLALYRY HSYKDLSEFL RGLVMNYPHI TNLTTLGQSV
EYRHIWSLEI SNKPNISEPE EPKIRFVAGI HGNAPVGTEL LLALAEFLCL NYKRNPVVTQ
LVDRTRIVIV PSLNPDGRER AQEKDCTSKT GHTNAHGKDL DTDFTSNASQ PETKAIIENL
IQKQDFSLSI ALDGGSVLVT YPYDKPVQTV ENKETLKHLA SLYANNHPSM HMGQPSCPNN
SDENIPGGVM RGAEWHSHLG SMKDYSVTYG HCPEITVYTS CCYFPSAAQL PALWAENKKS
LLSMLVEVHK GVHGLVKDKA GKPISKAVIV LNEGIKVYTK EGGYFHVLLA PGVHNINAIA
DGYQQQHTQV FVHHDAASSV VIVFDTDNRI FGLPRELVVT VSGATMSALI LTACIIWCIC
SIKSNRHKDG FHRLRQHHDE YEDEIRMMST GSKKSLLSHE FQDETDTEEE TLYSSKH
