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Q09M05 (CBPC4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosolic carboxypeptidase 4

EC=3.4.17.-
Alternative name(s):
ATP/GTP-binding protein-like 1
Gene names
Name:Agbl1
Synonyms:Ccp4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length972 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. Ref.2

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Interacts with MYLK. Ref.2

Subcellular location

Cytoplasmcytosol By similarity.

Tissue specificity

Expressed at low level. Expressed in eye, muscle, pituitary, testis and to a lower extent in brain. Ref.1 Ref.2

Sequence similarities

Belongs to the peptidase M14 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandMetal-binding
Zinc
   Molecular functionCarboxypeptidase
Hydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processC-terminal protein deglutamylation

Inferred from direct assay Ref.2. Source: UniProtKB

protein side chain deglutamylation

Inferred from direct assay Ref.2. Source: UniProtKB

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetallocarboxypeptidase activity

Inferred from direct assay Ref.2. Source: UniProtKB

tubulin binding

Inferred from direct assay Ref.2. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q09M05-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q09M05-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-206: Missing.
     850-857: FCDFHGHS → SHFLLFIL
     858-972: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q09M05-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-206: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q09M05-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAEQEGSGLQMLLHTLQNSSDKASTLSILQVLGDLLSVGTDRRIYYM
     952-972: VCEVYTARSLCSAADHKNRGK → GLQFGTGELE...GTGWRRRSVT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 972972Cytosolic carboxypeptidase 4
PRO_0000305000

Regions

Compositional bias256 – 28328Asp-rich

Sites

Active site8071Nucleophile By similarity
Metal binding7571Zinc Probable
Metal binding7601Zinc Probable
Metal binding8541Zinc By similarity

Natural variations

Alternative sequence1 – 206206Missing in isoform 2 and isoform 3.
VSP_028179
Alternative sequence11M → MAEQEGSGLQMLLHTLQNSS DKASTLSILQVLGDLLSVGT DRRIYYM in isoform 4.
VSP_040424
Alternative sequence850 – 8578FCDFHGHS → SHFLLFIL in isoform 2.
VSP_028180
Alternative sequence858 – 972115Missing in isoform 2.
VSP_028181
Alternative sequence952 – 97221VCEVY…KNRGK → GLQFGTGELEEMGAMYCLGL LILELKSVNCSHKLLARASS LLNADVLEHYLQRCSSSSSN SSNRTSEVDDEPYCMEEIDY SADSSSDAEQNFTELDRQIQ ECALNKDEEEEEKEEGTGWR RRSVT in isoform 4.
VSP_040425

Experimental info

Mutagenesis7571H → S: Abolishes deglutamylase activity; when associated with Q-760. Ref.2
Mutagenesis7601E → Q: Abolishes deglutamylase activity; when associated with S-757. Ref.2
Sequence conflict130 – 1334SKHL → KSNC in CAZ69802. Ref.2
Sequence conflict1971S → I in CAZ69802. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 35CA57FDEC4D12DB

FASTA972109,368
        10         20         30         40         50         60 
MISKGGSEAL LQTLVDTARS SSPDWDILLP LFRLLAKVGL RDKKFGQKAL ELEALDVTLI 

        70         80         90        100        110        120 
LARKNLSHSQ NLLHCLWVLR VFASSVTTGA MLGINGAMEL LFKVLSPYTR KHTRTIRAAT 

       130        140        150        160        170        180 
EVLAALLKSS KHLRRAVNRG YVNSLLRLHQ DWHSRDVTNT YVTIRHGLLL CLRHIVALRS 

       190        200        210        220        230        240 
GREAFLAAQG METLFSSAQT CLENKNMELV ISAVIQILRQ CYPASRLPLV TASSAYTFPA 

       250        260        270        280        290        300 
PGSTSSELPL NLTEEDFDDD GDEEMDKDSD VEAVKEDDDL ETDLSKLSSK PGLDLPEEEL 

       310        320        330        340        350        360 
AQYDAMCPEL SCSFEELEPK CGDDLNNKDT LHANHHHIPS VASLRQHCFN REHSSWRQER 

       370        380        390        400        410        420 
EDTVHSSILH MVKTGKSGVP SSSKQRSATN VNQSLQQNGL EIDSSGHDTS DIQAPLEQAA 

       430        440        450        460        470        480 
WDMEAISCPR ITASFPNSTK PEESIGAAEK LLHTHAKHIP FHDPHLYIAN AMRTRSAVGF 

       490        500        510        520        530        540 
KTMAFPDLWG HCPPPAAQPM LDRKLGVQRI KILEDIRRLL HPSDVINKVV FSLDEPRPLQ 

       550        560        570        580        590        600 
GSISNCLMFH SKFESGNLRK AIQVREFEYD LLVNADVNSS QHQQWFYFKV SGMRAAVPYH 

       610        620        630        640        650        660 
FNIINCEKPN SQFNYGMQPT LYSVKEALLG RPAWIRTGSD ICYYKNHYRQ NAATMDGALG 

       670        680        690        700        710        720 
KRYYTLTFAV TFPHNEDACY LAYHYPYTYS TLMTHLEILE RSIDHREIYF RHDVLCQTLG 

       730        740        750        760        770        780 
GNPCPLVTIT AFPESNSTEH LEQFRCRPYQ VITARVHPGE SNASWVMKGT LEFLVSSDPV 

       790        800        810        820        830        840 
AKLLRENFVF KIIPMLNPDG VINGNHRCSL RGEDLNRQWL SPQAHLQPTI YHAKGLLHYL 

       850        860        870        880        890        900 
SSTGRGPVVF CDFHGHSQKK NVFLYGCSMK ETLWQAGCTV GESALLEDVS YRTLPKILDK 

       910        920        930        940        950        960 
LAPAFTMNSC SFLVEKSRAS TARVVVWREM GVSRSYTMES SYCGCNQGPY QVCEVYTARS 

       970 
LCSAADHKNR GK 

« Hide

Isoform 2 [UniParc].

Checksum: DC8FA5375A1C1E3E
Show »

FASTA65173,608
Isoform 3 [UniParc].

Checksum: E8656F1875720724
Show »

FASTA76686,375
Isoform 4 [UniParc].

Checksum: F9B818FB39F03B37
Show »

FASTA1,122126,149

References

« Hide 'large scale' references
[1]"A novel subfamily of mouse cytosolic carboxypeptidases."
Kalinina E., Biswas R., Berezniuk I., Hermoso A., Aviles F.X., Fricker L.D.
FASEB J. 21:836-850(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
Strain: C57BL/KsJ.
[2]"A family of protein-deglutamylating enzymes associated with neurodegeneration."
Rogowski K., van Dijk J., Magiera M.M., Bosc C., Deloulme J.C., Bosson A., Peris L., Gold N.D., Lacroix B., Grau M.B., Bec N., Larroque C., Desagher S., Holzer M., Andrieux A., Moutin M.J., Janke C.
Cell 143:564-578(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH MYLK, MUTAGENESIS OF HIS-757 AND GLU-760.
[3]"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. expand/collapse author list , 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] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Lung.
[4]"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. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/KsJ.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ867033 mRNA. Translation: ABI51952.1.
FN429927 mRNA. Translation: CAZ69802.1.
AK052433 mRNA. Translation: BAC34986.1.
AC115830 Genomic DNA. No translation available.
AC165265 Genomic DNA. No translation available.
AC121812 Genomic DNA. No translation available.
AC123792 Genomic DNA. No translation available.
AC121971 Genomic DNA. No translation available.
IPIIPI00226518.
IPI00856787.
IPI00857194.
IPI00973603.
RefSeqNP_001186153.1. NM_001199224.1.
UniGeneMm.322829.

3D structure databases

ProteinModelPortalQ09M05.
SMRQ09M05. Positions 97-199, 547-869.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000103066.

Protein family/group databases

MEROPSM14.030.

PTM databases

PhosphoSiteQ09M05.

Proteomic databases

PaxDbQ09M05.
PRIDEQ09M05.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026854; ENSMUSP00000026854; ENSMUSG00000025754.
ENSMUST00000107442; ENSMUSP00000103066; ENSMUSG00000025754.
GeneID244071.
KEGGmmu:244071.
UCSCuc009hxb.1. mouse.
uc009hxc.1. mouse.
uc012fnc.1. mouse.

Organism-specific databases

CTD123624.
MGIMGI:3646469. Agbl1.

Phylogenomic databases

eggNOGCOG2866.
GeneTreeENSGT00550000074405.
HOGENOMHOG000293310.
HOVERGENHBG107587.
InParanoidQ09M05.
OrthoDBEOG4JDH61.

Gene expression databases

ArrayExpressQ09M05.
BgeeQ09M05.
CleanExMM_AGBL1.
GenevestigatorQ09M05.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000834. Peptidase_M14.
[Graphical view]
PfamPF00246. Peptidase_M14. 1 hit.
[Graphical view]
SUPFAMSSF48371. ARM-type_fold. 1 hit.
PROSITEPS00132. CARBOXYPEPT_ZN_1. False negative.
PS00133. CARBOXYPEPT_ZN_2. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio386109.
SOURCESearch...

Entry information

Entry nameCBPC4_MOUSE
AccessionPrimary (citable) accession number: Q09M05
Secondary accession number(s): Q8C768
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: May 1, 2013
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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