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Reviewed, UniProtKB/Swiss-Prot Q8BGE6 (ATG4B_MOUSE)

Last modified November 25, 2008. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cysteine protease ATG4B
    EC=3.4.22.-
Alternative name(s):
    Autophagy-related protein 4 homolog B
    Autophagin-1
    Autophagy-related cysteine endopeptidase 1
    AUT-like 1 cysteine endopeptidase
Gene names
Name: Atg4b
Synonyms: Apg4b, Autl1, Kiaa0943
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.

Enzyme regulation

Inhibited by N-ethylmaleimide By similarity.

Subcellular location

CytoplasmProbable.

Sequence similarities

Belongs to the peptidase C54 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Cysteine protease ATG4B
PRO_0000215845

Sites

Active site741Nucleophile By similarity
Active site2781 Potential
Active site2801 By similarity

Amino acid modifications

Modified residue341Phosphoserine
Modified residue3161Phosphoserine By similarity
Modified residue3831Phosphoserine
Modified residue3921Phosphoserine By similarity

Experimental info

Sequence conflict128 – 15326IAQMG…AQVLK → NCLNCHCCGVMLMLYKAHGS VLAFCR Ref.3
Sequence conflict1901A → V in CAD43220. Ref.1
Sequence conflict1901A → V in BAC26079, BAC27455 and BAC35965. Ref.2
Sequence conflict3251T → K in BAC40587. Ref.2
Sequence conflict3251T → K Ref.3 Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8BGE6-1 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: EB9BF54B06F79135

FASTA39344,375
        10         20         30         40         50         60 
MDAATLTYDT LRFAEFEDFP ETSEPVWILG RKYSIFTEKD EILSDVASRL WFTYRRNFPA 

        70         80         90        100        110        120 
IGGTGPTSDT GWGCMLRCGQ MIFAQALVCR HLGRDWRWTQ RKRQPDSYFN VLNAFLDRKD 

       130        140        150        160        170        180 
SYYSIHQIAQ MGVGEGKSIG QWYGPNTVAQ VLKKLAVFDT WSSLAVHIAM DNTVVMEEIR 

       190        200        210        220        230        240 
RLCRANLPCA GAAALPTDSE RHCNGFPAGA EVTNRPSAWR PLVLLIPLRL GLTDINEAYV 

       250        260        270        280        290        300 
ETLKHCFMMP QSLGVIGGKP NSAHYFIGYV GEELIYLDPH TTQPAVELTD SCFIPDESFH 

       310        320        330        340        350        360 
CQHPPSRMGI GELDPSIAVG FFCKTEEDFN DWCQQVKKLS QLGGALPMFE LVEQQPSHLA 

       370        380        390 
CQDVLNLSLD SSDVERLERF FDSEDEDFEI LSL 

« Hide

References

« Hide 'large scale' references
[1]"Human autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy."
Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J., Lopez-Otin C.
J. Biol. Chem. 278:3671-3678(2003) [PubMed: 12446702] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[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. 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Pancreas, Skin and Testis.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed: 14621295] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-393.
Tissue: Brain.
[5]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, MASS SPECTROMETRY.
Tissue: Liver.
[6]"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 SER-34, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ504653 mRNA. Translation: CAD43220.1.
AK028712 mRNA. Translation: BAC26079.1.
AK031570 mRNA. Translation: BAC27455.1.
AK075796 mRNA. Translation: BAC35965.1.
AK088811 mRNA. Translation: BAC40587.1.
BC027184 mRNA. Translation: AAH27184.1.
AK129242 mRNA. Translation: BAC98052.1.
UniGeneMm.29087

3D structure databases

SMRQ8BGE6. Positions 10-373.
ModBaseSearch...

Protein family/group databases

MEROPSC54.003.

PTM databases

PhosphoSiteQ8BGE6.

Genome annotation databases

EnsemblENSMUSG00000026280. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:1913865. Atg4b.
RougeSearch...

Phylogenomic databases

HOGENOMQ8BGE6.
HOVERGENQ8BGE6.

Gene expression databases

ArrayExpressQ8BGE6.
CleanExMM_ATG4B.
GermOnlineENSMUSG00000026280. Mus musculus.

Family and domain databases

InterProIPR005078. Peptidase_C54.
[Graphical view]
PANTHERPTHR22624. Peptidase_C54. 1 hit.
PfamPF03416. Peptidase_C54. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameATG4B_MOUSE
AccessionPrimary (citable) accession number: Q8BGE6
Secondary accession number(s): Q6ZQ22, Q8R098
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: November 25, 2008
This is version 45 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

Peptidase families

Classification of peptidase families and list of entries

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents