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Protein

Cytosolic carboxypeptidase 4

Gene

Agbl1

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

Functioni

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/CCP5.2 Publications

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi757 – 7571ZincCurated
Metal bindingi760 – 7601ZincCurated
Active sitei807 – 8071NucleophileBy similarity
Metal bindingi854 – 8541ZincBy similarity

GO - Molecular functioni

  • metallocarboxypeptidase activity Source: UniProtKB
  • tubulin binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • C-terminal protein deglutamylation Source: UniProtKB
  • protein side chain deglutamylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM14.030.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic carboxypeptidase 4 (EC:3.4.17.-)
Alternative name(s):
ATP/GTP-binding protein-like 1
Gene namesi
Name:Agbl1
Synonyms:Ccp4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:3646469. Agbl1.

Subcellular locationi

  • Cytoplasmcytosol By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi757 – 7571H → S: Abolishes deglutamylase activity; when associated with Q-760. 1 Publication
Mutagenesisi760 – 7601E → Q: Abolishes deglutamylase activity; when associated with S-757. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 972972Cytosolic carboxypeptidase 4PRO_0000305000Add
BLAST

Proteomic databases

PaxDbiQ09M05.
PRIDEiQ09M05.

PTM databases

iPTMnetiQ09M05.
PhosphoSiteiQ09M05.

Expressioni

Tissue specificityi

Widely expressed at low level. Expressed in eye, muscle, pituitary, testis and to a lower extent in brain.3 Publications

Gene expression databases

BgeeiQ09M05.
CleanExiMM_AGBL1.
ExpressionAtlasiQ09M05. baseline.

Interactioni

Subunit structurei

Interacts with TCF4 (By similarity). Interacts with MYLK.By similarity1 Publication

GO - Molecular functioni

  • tubulin binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000128342.

Structurei

3D structure databases

ProteinModelPortaliQ09M05.
SMRiQ09M05. Positions 547-869.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi256 – 28328Asp-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Phylogenomic databases

eggNOGiKOG3641. Eukaryota.
COG2866. LUCA.
GeneTreeiENSGT00550000074405.
HOGENOMiHOG000293310.
HOVERGENiHBG107587.
InParanoidiQ09M05.
OMAiFKVMAFP.
OrthoDBiEOG712TVD.
TreeFamiTF333192.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000834. Peptidase_M14.
[Graphical view]
PfamiPF00246. Peptidase_M14. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q09M05-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MISKGGSEAL LQTLVDTARS SSPDWDILLP LFRLLAKVGL RDKKFGQKAL
60 70 80 90 100
ELEALDVTLI LARKNLSHSQ NLLHCLWVLR VFASSVTTGA MLGINGAMEL
110 120 130 140 150
LFKVLSPYTR KHTRTIRAAT EVLAALLKSS KHLRRAVNRG YVNSLLRLHQ
160 170 180 190 200
DWHSRDVTNT YVTIRHGLLL CLRHIVALRS GREAFLAAQG METLFSSAQT
210 220 230 240 250
CLENKNMELV ISAVIQILRQ CYPASRLPLV TASSAYTFPA PGSTSSELPL
260 270 280 290 300
NLTEEDFDDD GDEEMDKDSD VEAVKEDDDL ETDLSKLSSK PGLDLPEEEL
310 320 330 340 350
AQYDAMCPEL SCSFEELEPK CGDDLNNKDT LHANHHHIPS VASLRQHCFN
360 370 380 390 400
REHSSWRQER EDTVHSSILH MVKTGKSGVP SSSKQRSATN VNQSLQQNGL
410 420 430 440 450
EIDSSGHDTS DIQAPLEQAA WDMEAISCPR ITASFPNSTK PEESIGAAEK
460 470 480 490 500
LLHTHAKHIP FHDPHLYIAN AMRTRSAVGF KTMAFPDLWG HCPPPAAQPM
510 520 530 540 550
LDRKLGVQRI KILEDIRRLL HPSDVINKVV FSLDEPRPLQ GSISNCLMFH
560 570 580 590 600
SKFESGNLRK AIQVREFEYD LLVNADVNSS QHQQWFYFKV SGMRAAVPYH
610 620 630 640 650
FNIINCEKPN SQFNYGMQPT LYSVKEALLG RPAWIRTGSD ICYYKNHYRQ
660 670 680 690 700
NAATMDGALG KRYYTLTFAV TFPHNEDACY LAYHYPYTYS TLMTHLEILE
710 720 730 740 750
RSIDHREIYF RHDVLCQTLG GNPCPLVTIT AFPESNSTEH LEQFRCRPYQ
760 770 780 790 800
VITARVHPGE SNASWVMKGT LEFLVSSDPV AKLLRENFVF KIIPMLNPDG
810 820 830 840 850
VINGNHRCSL RGEDLNRQWL SPQAHLQPTI YHAKGLLHYL SSTGRGPVVF
860 870 880 890 900
CDFHGHSQKK NVFLYGCSMK ETLWQAGCTV GESALLEDVS YRTLPKILDK
910 920 930 940 950
LAPAFTMNSC SFLVEKSRAS TARVVVWREM GVSRSYTMES SYCGCNQGPY
960 970
QVCEVYTARS LCSAADHKNR GK
Note: No experimental confirmation available.
Length:972
Mass (Da):109,368
Last modified:October 2, 2007 - v2
Checksum:i35CA57FDEC4D12DB
GO
Isoform 2 (identifier: Q09M05-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:651
Mass (Da):73,608
Checksum:iDC8FA5375A1C1E3E
GO
Isoform 3 (identifier: Q09M05-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-206: Missing.

Note: No experimental confirmation available.
Show »
Length:766
Mass (Da):86,375
Checksum:iE8656F1875720724
GO
Isoform 4 (identifier: Q09M05-4) [UniParc]FASTAAdd to basket

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

Show »
Length:1,122
Mass (Da):126,149
Checksum:iF9B818FB39F03B37
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1334SKHL → KSNC in CAZ69802 (PubMed:21074048).Curated
Sequence conflicti197 – 1971S → I in CAZ69802 (PubMed:21074048).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 206206Missing in isoform 2 and isoform 3. 2 PublicationsVSP_028179Add
BLAST
Alternative sequencei1 – 11M → MAEQEGSGLQMLLHTLQNSS DKASTLSILQVLGDLLSVGT DRRIYYM in isoform 4. 1 PublicationVSP_040424
Alternative sequencei850 – 8578FCDFHGHS → SHFLLFIL in isoform 2. 1 PublicationVSP_028180
Alternative sequencei858 – 972115Missing in isoform 2. 1 PublicationVSP_028181Add
BLAST
Alternative sequencei952 – 97221VCEVY…KNRGK → GLQFGTGELEEMGAMYCLGL LILELKSVNCSHKLLARASS LLNADVLEHYLQRCSSSSSN SSNRTSEVDDEPYCMEEIDY SADSSSDAEQNFTELDRQIQ ECALNKDEEEEEKEEGTGWR RRSVT in isoform 4. 1 PublicationVSP_040425Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001186153.1. NM_001199224.1.
UniGeneiMm.322829.

Genome annotation databases

EnsembliENSMUST00000026854; ENSMUSP00000026854; ENSMUSG00000025754. [Q09M05-2]
ENSMUST00000107442; ENSMUSP00000103066; ENSMUSG00000025754. [Q09M05-3]
GeneIDi244071.
KEGGimmu:244071.
UCSCiuc009hxb.1. mouse. [Q09M05-2]
uc009hxc.1. mouse. [Q09M05-1]
uc012fnc.1. mouse. [Q09M05-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001186153.1. NM_001199224.1.
UniGeneiMm.322829.

3D structure databases

ProteinModelPortaliQ09M05.
SMRiQ09M05. Positions 547-869.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000128342.

Protein family/group databases

MEROPSiM14.030.

PTM databases

iPTMnetiQ09M05.
PhosphoSiteiQ09M05.

Proteomic databases

PaxDbiQ09M05.
PRIDEiQ09M05.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026854; ENSMUSP00000026854; ENSMUSG00000025754. [Q09M05-2]
ENSMUST00000107442; ENSMUSP00000103066; ENSMUSG00000025754. [Q09M05-3]
GeneIDi244071.
KEGGimmu:244071.
UCSCiuc009hxb.1. mouse. [Q09M05-2]
uc009hxc.1. mouse. [Q09M05-1]
uc012fnc.1. mouse. [Q09M05-4]

Organism-specific databases

CTDi123624.
MGIiMGI:3646469. Agbl1.

Phylogenomic databases

eggNOGiKOG3641. Eukaryota.
COG2866. LUCA.
GeneTreeiENSGT00550000074405.
HOGENOMiHOG000293310.
HOVERGENiHBG107587.
InParanoidiQ09M05.
OMAiFKVMAFP.
OrthoDBiEOG712TVD.
TreeFamiTF333192.

Miscellaneous databases

ChiTaRSiAgbl1. mouse.
PROiQ09M05.
SOURCEiSearch...

Gene expression databases

BgeeiQ09M05.
CleanExiMM_AGBL1.
ExpressionAtlasiQ09M05. baseline.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000834. Peptidase_M14.
[Graphical view]
PfamiPF00246. Peptidase_M14. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: C57BLKS/J.
  2. 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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BLKS/J.
  5. "The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids."
    Tort O., Tanco S., Rocha C., Bieche I., Seixas C., Bosc C., Andrieux A., Moutin M.J., Aviles F.X., Lorenzo J., Janke C.
    Mol. Biol. Cell 25:3017-3027(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCBPC4_MOUSE
AccessioniPrimary (citable) accession number: Q09M05
Secondary accession number(s): Q8C768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: June 8, 2016
This is version 75 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.