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Protein

Carboxypeptidase D

Gene

Cpd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Releases C-terminal Arg and Lys from polypeptides.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi138 – 1381Zinc 1; catalyticBy similarity
Metal bindingi141 – 1411Zinc 1; catalyticBy similarity
Metal bindingi256 – 2561Zinc 1; catalyticBy similarity
Sitei349 – 3491Important for catalytic activityBy similarity
Metal bindingi563 – 5631Zinc 2; catalyticBy similarity
Metal bindingi566 – 5661Zinc 2; catalyticBy similarity
Metal bindingi670 – 6701Zinc 2; catalyticBy similarity
Active sitei761 – 7611Proton donor/acceptorBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.22. 3474.

Protein family/group databases

MEROPSiM14.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase D (EC:3.4.17.22)
Alternative name(s):
Metallocarboxypeptidase D
gp180
Gene namesi
Name:Cpd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:107265. Cpd.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini38 – 12961259ExtracellularSequence analysisAdd
BLAST
Transmembranei1297 – 131721HelicalSequence analysisAdd
BLAST
Topological domaini1318 – 137760CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3737Sequence analysisAdd
BLAST
Chaini38 – 13771340Carboxypeptidase DPRO_0000004402Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence analysis
Glycosylationi216 – 2161N-linked (GlcNAc...)Sequence analysis
Modified residuei264 – 2641PhosphotyrosineCombined sources
Modified residuei269 – 2691PhosphoserineCombined sources
Glycosylationi398 – 3981N-linked (GlcNAc...)1 Publication
Glycosylationi409 – 4091N-linked (GlcNAc...)1 Publication
Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence analysis
Glycosylationi521 – 5211N-linked (GlcNAc...)1 Publication
Glycosylationi625 – 6251N-linked (GlcNAc...)Sequence analysis
Glycosylationi810 – 8101N-linked (GlcNAc...)Sequence analysis
Glycosylationi854 – 8541N-linked (GlcNAc...)Sequence analysis
Glycosylationi866 – 8661N-linked (GlcNAc...)Sequence analysis
Glycosylationi878 – 8781N-linked (GlcNAc...)Sequence analysis
Glycosylationi952 – 9521N-linked (GlcNAc...)Sequence analysis
Glycosylationi975 – 9751N-linked (GlcNAc...)Sequence analysis
Glycosylationi1067 – 10671N-linked (GlcNAc...)Sequence analysis
Glycosylationi1139 – 11391N-linked (GlcNAc...)Sequence analysis
Lipidationi1314 – 13141S-palmitoyl cysteineBy similarity
Lipidationi1318 – 13181S-palmitoyl cysteineBy similarity
Lipidationi1320 – 13201S-palmitoyl cysteineBy similarity
Modified residuei1355 – 13551PhosphoserineCombined sources
Modified residuei1358 – 13581PhosphoserineCombined sources
Modified residuei1365 – 13651PhosphothreonineCombined sources
Modified residuei1367 – 13671PhosphothreonineCombined sources

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiO89001.
PaxDbiO89001.
PRIDEiO89001.

PTM databases

iPTMnetiO89001.
PhosphoSiteiO89001.
SwissPalmiO89001.

Expressioni

Gene expression databases

BgeeiO89001.
CleanExiMM_CPD.
GenevisibleiO89001. MM.

Interactioni

Protein-protein interaction databases

IntActiO89001. 3 interactions.
MINTiMINT-4996296.
STRINGi10090.ENSMUSP00000021201.

Structurei

3D structure databases

ProteinModelPortaliO89001.
SMRiO89001. Positions 52-872, 928-1263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 492455Carboxypeptidase-like 1Add
BLAST
Regioni493 – 896404Carboxypeptidase-like 2Add
BLAST
Regioni897 – 1296400Carboxypeptidase-like 3Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi161 – 1633Cell attachment siteSequence analysis

Domaini

There are 3 carboxypeptidase-like domains. Only the first two domains seem to have kept a catalytic activity.

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
GeneTreeiENSGT00760000119124.
HOGENOMiHOG000046445.
HOVERGENiHBG006932.
InParanoidiO89001.
KOiK07752.
OMAiDWIRRNK.
OrthoDBiEOG7B8S32.
TreeFamiTF315592.

Family and domain databases

Gene3Di2.60.40.1120. 3 hits.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR015567. Pept_M14B_carboxypept_D2.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF50. PTHR11532:SF50. 3 hits.
PfamiPF00246. Peptidase_M14. 3 hits.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 3 hits.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 3 hits.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 2 hits.
PS00133. CARBOXYPEPT_ZN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O89001-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGRDERPP WRLGRLRLLP PPPLLLLLLL LRSSAQAAHI KKAEATTTTV
60 70 80 90 100
GGSEAAEGQF DHYYHEAALG EALEAAAAAG PPGLARLFSI GSSVEGRPLW
110 120 130 140 150
VLRLTAGLGP PPTAAAGLDA AGPLLPGRPQ VKLVGNMHGD ETVSRQVLVY
160 170 180 190 200
LARELASGYR RGDPRLVRLL NTTDVYLLPS LNPDGFERAR EGDCGLGDSG
210 220 230 240 250
PPGTSGRDNS RGRDLNRSFP DQFSTGEPPS LDEVPEVRAL IDWIRRNKFV
260 270 280 290 300
LSGNLHGGSV VASYPFDDSP EHKTTGLYSK TSDDEVFRYL AKAYASNHPI
310 320 330 340 350
MKTGEPHCPG DEDETFKDGI TNGAHWYDVE GGMQDYNYVW ANCFEITLEL
360 370 380 390 400
SCCKYPPASQ LRQEWENNRE SLITLIEKVH IGIKGFVKDS VTGSGLENAT
410 420 430 440 450
ISVAGINHNI TTGRFGDFHR LLVPGTYNLT ALSTGYMPLT INNIMVKEGP
460 470 480 490 500
ATEMDFSLRP TVMSVMPGST EAVTTPGTVA VPNIPPGTPS SHQPIQPKDF
510 520 530 540 550
HHHHFPDMEI FLRRFANEYP NITRLYSLGK SVESRELYVM EISDNPGVHE
560 570 580 590 600
PGEPEFKYIG NMHGNEVVGR ELLLNLIEYL CKNFGTDPEV TDLVRSTRIH
610 620 630 640 650
LMPSMNPDGY EKSQEGDSIS VVGRNNSNNF DLNRNFPDQF VPITEPTQPE
660 670 680 690 700
TIAVMSWVKA YPFVLSANLH GGSLVVNYPY DDNEQGVATY SKSPDDAVFQ
710 720 730 740 750
QIALSYSKEN SQMFQGRPCK DMYLNEYFPH GITNGASWYN VPGGMQDWNY
760 770 780 790 800
LQTNCFEVTI ELGCVKYPFE NELPKYWEQN RRSLIQFMKQ VHQGVKGFVL
810 820 830 840 850
DATDGRGILN ATLSVAEINH PVTTYKAGDY WRLLVPGTYK ITASARGYNP
860 870 880 890 900
VTKNVTVRSE GAVQVNFTLV RSSADANNES KKGRGHSTST DDTSDPTSKE
910 920 930 940 950
FEALIKHLSA ENGLEGFMLS SSSDLALYRY HSYKDLSEFL RGLVMNYPHI
960 970 980 990 1000
TNLTTLGQSV EYRHIWSLEI SNKPNISEPE EPKIRFVAGI HGNAPVGTEL
1010 1020 1030 1040 1050
LLALAEFLCL NYKRNPVVTQ LVDRTRIVIV PSLNPDGRER AQEKDCTSKT
1060 1070 1080 1090 1100
GHTNAHGKDL DTDFTSNASQ PETKAIIENL IQKQDFSLSI ALDGGSVLVT
1110 1120 1130 1140 1150
YPYDKPVQTV ENKETLKHLA SLYANNHPSM HMGQPSCPNN SDENIPGGVM
1160 1170 1180 1190 1200
RGAEWHSHLG SMKDYSVTYG HCPEITVYTS CCYFPSAAQL PALWAENKKS
1210 1220 1230 1240 1250
LLSMLVEVHK GVHGLVKDKA GKPISKAVIV LNEGIKVYTK EGGYFHVLLA
1260 1270 1280 1290 1300
PGVHNINAIA DGYQQQHTQV FVHHDAASSV VIVFDTDNRI FGLPRELVVT
1310 1320 1330 1340 1350
VSGATMSALI LTACIIWCIC SIKSNRHKDG FHRLRQHHDE YEDEIRMMST
1360 1370
GSKKSLLSHE FQDETDTEEE TLYSSKH
Length:1,377
Mass (Da):152,406
Last modified:July 27, 2011 - v2
Checksum:i73CC0861EE674053
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531S → T in BAA33371 (PubMed:9714835).Curated
Sequence conflicti1039 – 10402ER → DG in BAA33371 (PubMed:9714835).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85391 mRNA. Translation: BAA33371.1.
AK137737 mRNA. Translation: BAE23483.1.
AL645479 Genomic DNA. Translation: CAI25538.1.
CCDSiCCDS25071.1.
RefSeqiNP_031780.2. NM_007754.2.
UniGeneiMm.276736.

Genome annotation databases

EnsembliENSMUST00000021201; ENSMUSP00000021201; ENSMUSG00000020841.
GeneIDi12874.
KEGGimmu:12874.
UCSCiuc007kga.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85391 mRNA. Translation: BAA33371.1.
AK137737 mRNA. Translation: BAE23483.1.
AL645479 Genomic DNA. Translation: CAI25538.1.
CCDSiCCDS25071.1.
RefSeqiNP_031780.2. NM_007754.2.
UniGeneiMm.276736.

3D structure databases

ProteinModelPortaliO89001.
SMRiO89001. Positions 52-872, 928-1263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO89001. 3 interactions.
MINTiMINT-4996296.
STRINGi10090.ENSMUSP00000021201.

Protein family/group databases

MEROPSiM14.011.

PTM databases

iPTMnetiO89001.
PhosphoSiteiO89001.
SwissPalmiO89001.

Proteomic databases

MaxQBiO89001.
PaxDbiO89001.
PRIDEiO89001.

Protocols and materials databases

DNASUi12874.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021201; ENSMUSP00000021201; ENSMUSG00000020841.
GeneIDi12874.
KEGGimmu:12874.
UCSCiuc007kga.1. mouse.

Organism-specific databases

CTDi1362.
MGIiMGI:107265. Cpd.

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
GeneTreeiENSGT00760000119124.
HOGENOMiHOG000046445.
HOVERGENiHBG006932.
InParanoidiO89001.
KOiK07752.
OMAiDWIRRNK.
OrthoDBiEOG7B8S32.
TreeFamiTF315592.

Enzyme and pathway databases

BRENDAi3.4.17.22. 3474.

Miscellaneous databases

ChiTaRSiCpd. mouse.
NextBioi282466.
PROiO89001.
SOURCEiSearch...

Gene expression databases

BgeeiO89001.
CleanExiMM_CPD.
GenevisibleiO89001. MM.

Family and domain databases

Gene3Di2.60.40.1120. 3 hits.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR015567. Pept_M14B_carboxypept_D2.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF50. PTHR11532:SF50. 3 hits.
PfamiPF00246. Peptidase_M14. 3 hits.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 3 hits.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 3 hits.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 2 hits.
PS00133. CARBOXYPEPT_ZN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    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.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Vagina.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1365 AND THR-1367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-398; ASN-409 AND ASN-521.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-264; SER-269; SER-1355; SER-1358; THR-1365 AND THR-1367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCBPD_MOUSE
AccessioniPrimary (citable) accession number: O89001
Secondary accession number(s): Q5SVH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.