Carboxypeptidase D precursor - Mus musculus (Mouse)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Carboxypeptidase D
EC=3.4.17.22

Alternative name(s):
Metallocarboxypeptidase D
gp180

Gene names

Name:

Cpd

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Releases C-terminal Arg and Lys from polypeptides.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein Potential.
Domain	There are 3 carboxypeptidase-like domains. Only the first two domains seem to have kept a catalytic activity.
Sequence similarities	Belongs to the peptidase M14 family.

Ontologies

Keywords
Cellular component	Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metallocarboxypeptidase activity Inferred from electronic annotation. Source: InterPro serine-type carboxypeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 37

37

Potential

Chain

38 – 1377

1340

Carboxypeptidase D

PRO_0000004402

Regions

Topological domain

38 – 1296

1259

Extracellular Potential

Transmembrane

1297 – 1317

21

Helical; Potential

Topological domain

1318 – 1377

60

Cytoplasmic Potential

Region

38 – 492

455

Carboxypeptidase-like 1

Region

493 – 896

404

Carboxypeptidase-like 2

Region

897 – 1296

400

Carboxypeptidase-like 3

Motif

161 – 163

3

Cell attachment site Potential

Sites

Active site

349

1

Nucleophile 1 By similarity

Active site

761

1

Nucleophile 2 By similarity

Metal binding

138

1

Zinc 1 By similarity

Metal binding

141

1

Zinc 1 By similarity

Metal binding

256

1

Zinc 1 By similarity

Metal binding

563

1

Zinc 2 By similarity

Metal binding

566

1

Zinc 2 By similarity

Metal binding

670

1

Zinc 2 By similarity

Amino acid modifications

Modified residue

1341

1

Phosphotyrosine By similarity

Modified residue

1355

1

Phosphoserine By similarity

Modified residue

1358

1

Phosphoserine By similarity

Modified residue

1365

1

Phosphothreonine Ref.4

Modified residue

1367

1

Phosphothreonine Ref.4

Modified residue

1373

1

Phosphotyrosine By similarity

Lipidation

1314

1

S-palmitoyl cysteine By similarity

Lipidation

1318

1

S-palmitoyl cysteine By similarity

Lipidation

1320

1

S-palmitoyl cysteine By similarity

Glycosylation

171

1

N-linked (GlcNAc...) Potential

Glycosylation

216

1

N-linked (GlcNAc...) Potential

Glycosylation

398

1

N-linked (GlcNAc...) Ref.5

Glycosylation

409

1

N-linked (GlcNAc...) Ref.5

Glycosylation

428

1

N-linked (GlcNAc...) Potential

Glycosylation

521

1

N-linked (GlcNAc...) Ref.5

Glycosylation

625

1

N-linked (GlcNAc...) Potential

Glycosylation

810

1

N-linked (GlcNAc...) Potential

Glycosylation

854

1

N-linked (GlcNAc...) Potential

Glycosylation

866

1

N-linked (GlcNAc...) Potential

Glycosylation

878

1

N-linked (GlcNAc...) Potential

Glycosylation

952

1

N-linked (GlcNAc...) Potential

Glycosylation

975

1

N-linked (GlcNAc...) Potential

Glycosylation

1067

1

N-linked (GlcNAc...) Potential

Glycosylation

1139

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

53

1

S → T in BAA33371. Ref.1

Sequence conflict

1039 – 1040

2

ER → DG in BAA33371. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O89001 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 73CC0861EE674053
Show »

FASTA

1,377

152,406

        10         20         30         40         50         60 
MASGRDERPP WRLGRLRLLP PPPLLLLLLL LRSSAQAAHI KKAEATTTTV GGSEAAEGQF 

        70         80         90        100        110        120 
DHYYHEAALG EALEAAAAAG PPGLARLFSI GSSVEGRPLW VLRLTAGLGP PPTAAAGLDA 

       130        140        150        160        170        180 
AGPLLPGRPQ VKLVGNMHGD ETVSRQVLVY LARELASGYR RGDPRLVRLL NTTDVYLLPS 

       190        200        210        220        230        240 
LNPDGFERAR EGDCGLGDSG PPGTSGRDNS RGRDLNRSFP DQFSTGEPPS LDEVPEVRAL 

       250        260        270        280        290        300 
IDWIRRNKFV LSGNLHGGSV VASYPFDDSP EHKTTGLYSK TSDDEVFRYL AKAYASNHPI 

       310        320        330        340        350        360 
MKTGEPHCPG DEDETFKDGI TNGAHWYDVE GGMQDYNYVW ANCFEITLEL SCCKYPPASQ 

       370        380        390        400        410        420 
LRQEWENNRE SLITLIEKVH IGIKGFVKDS VTGSGLENAT ISVAGINHNI TTGRFGDFHR 

       430        440        450        460        470        480 
LLVPGTYNLT ALSTGYMPLT INNIMVKEGP ATEMDFSLRP TVMSVMPGST EAVTTPGTVA 

       490        500        510        520        530        540 
VPNIPPGTPS SHQPIQPKDF HHHHFPDMEI FLRRFANEYP NITRLYSLGK SVESRELYVM 

       550        560        570        580        590        600 
EISDNPGVHE PGEPEFKYIG NMHGNEVVGR ELLLNLIEYL CKNFGTDPEV TDLVRSTRIH 

       610        620        630        640        650        660 
LMPSMNPDGY EKSQEGDSIS VVGRNNSNNF DLNRNFPDQF VPITEPTQPE TIAVMSWVKA 

       670        680        690        700        710        720 
YPFVLSANLH GGSLVVNYPY DDNEQGVATY SKSPDDAVFQ QIALSYSKEN SQMFQGRPCK 

       730        740        750        760        770        780 
DMYLNEYFPH GITNGASWYN VPGGMQDWNY LQTNCFEVTI ELGCVKYPFE NELPKYWEQN 

       790        800        810        820        830        840 
RRSLIQFMKQ VHQGVKGFVL DATDGRGILN ATLSVAEINH PVTTYKAGDY WRLLVPGTYK 

       850        860        870        880        890        900 
ITASARGYNP VTKNVTVRSE GAVQVNFTLV RSSADANNES KKGRGHSTST DDTSDPTSKE 

       910        920        930        940        950        960 
FEALIKHLSA ENGLEGFMLS SSSDLALYRY HSYKDLSEFL RGLVMNYPHI TNLTTLGQSV 

       970        980        990       1000       1010       1020 
EYRHIWSLEI SNKPNISEPE EPKIRFVAGI HGNAPVGTEL LLALAEFLCL NYKRNPVVTQ 

      1030       1040       1050       1060       1070       1080 
LVDRTRIVIV PSLNPDGRER AQEKDCTSKT GHTNAHGKDL DTDFTSNASQ PETKAIIENL 

      1090       1100       1110       1120       1130       1140 
IQKQDFSLSI ALDGGSVLVT YPYDKPVQTV ENKETLKHLA SLYANNHPSM HMGQPSCPNN 

      1150       1160       1170       1180       1190       1200 
SDENIPGGVM RGAEWHSHLG SMKDYSVTYG HCPEITVYTS CCYFPSAAQL PALWAENKKS 

      1210       1220       1230       1240       1250       1260 
LLSMLVEVHK GVHGLVKDKA GKPISKAVIV LNEGIKVYTK EGGYFHVLLA PGVHNINAIA 

      1270       1280       1290       1300       1310       1320 
DGYQQQHTQV FVHHDAASSV VIVFDTDNRI FGLPRELVVT VSGATMSALI LTACIIWCIC 

      1330       1340       1350       1360       1370 
SIKSNRHKDG FHRLRQHHDE YEDEIRMMST GSKKSLLSHE FQDETDTEEE TLYSSKH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, functional expression, and chromosomal localization of the human and mouse gp180-carboxypeptidase D-like enzyme." Ishikawa T., Murakami K., Kido Y., Ohnishi S., Yazaki Y., Harada F., Kuroki K. Gene 215:361-370(1998) [PubMed: 9714835] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Vagina.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1365 AND THR-1367, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-398; ASN-409 AND ASN-521, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D85391 mRNA. Translation: BAA33371.1. AK137737 mRNA. Translation: BAE23483.1. AL645479 Genomic DNA. Translation: CAI25538.1.
IPI	IPI00130573.
RefSeq	NP_031780.2. NM_007754.2.
UniGene	Mm.276736.
3D structure databases
ProteinModelPortal	O89001.
SMR	O89001. Positions 56-461, 493-872, 923-1286.
ModBase	Search...
Protein-protein interaction databases
IntAct	O89001. 1 interaction.
STRING	O89001.
Protein family/group databases
MEROPS	M14.011.
PTM databases
PhosphoSite	O89001.
Proteomic databases
PRIDE	O89001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000021201; ENSMUSP00000021201; ENSMUSG00000020841.
GeneID	12874.
KEGG	mmu:12874.
Organism-specific databases
CTD	1362.
MGI	MGI:107265. Cpd.
Phylogenomic databases
eggNOG	roNOG06219.
HOGENOM	HBG444298.
HOVERGEN	HBG006932.
InParanoid	O89001.
OrthoDB	EOG44J2H6.
Gene expression databases
ArrayExpress	O89001.
Bgee	O89001.
CleanEx	MM_CPD.
Genevestigator	O89001.
GermOnline	ENSMUSG00000020841. Mus musculus.
Family and domain databases
InterPro	IPR008969. CarboxyPept-like_regulatory. IPR014766. CarboxyPept_regulatory_dom. IPR015567. Pept_M14B_carboxypept_D2. IPR000834. Peptidase_M14. [Graphical view]
Gene3D	G3DSA:2.60.40.1120. CarboxyPept_regulatory. 3 hits.
KO	K07752.
PANTHER	PTHR11532:SF8. C_peptidase_D. 1 hit.
Pfam	PF00246. Peptidase_M14. 3 hits. [Graphical view]
PRINTS	PR00765. CRBOXYPTASEA.
SMART	SM00631. Zn_pept. 3 hits. [Graphical view]
SUPFAM	SSF49464. CarboxypepD_reg. 3 hits.
PROSITE	PS00132. CARBOXYPEPT_ZN_1. 2 hits. PS00133. CARBOXYPEPT_ZN_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

CBPD_MOUSE

Accession

Primary (citable) accession number: O89001
Secondary accession number(s): Q5SVH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	July 27, 2011
Last modified:	December 14, 2011
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents