ID   ATG4B_MOUSE             Reviewed;         393 AA.
AC   Q8BGE6; Q6ZQ22; Q8R098;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   19-JAN-2010, entry version 55.
DE   RecName: Full=Cysteine protease ATG4B;
DE            EC=3.4.22.-;
DE   AltName: Full=Autophagy-related protein 4 homolog B;
DE   AltName: Full=Autophagin-1;
DE   AltName: Full=Autophagy-related cysteine endopeptidase 1;
DE   AltName: Full=AUT-like 1 cysteine endopeptidase;
GN   Name=Atg4b; Synonyms=Apg4b, Autl1, Kiaa0943;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   PubMed=12446702; DOI=10.1074/jbc.M208247200;
RA   Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J.,
RA   Lopez-Otin C.;
RT   "Human autophagins, a family of cysteine proteinases potentially
RT   implicated in cell degradation by autophagy.";
RL   J. Biol. Chem. 278:3671-3678(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas, Skin, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-393.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Cysteine protease required for autophagy, which cleaves
CC       the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP,
CC       allowing the liberation of form I. A subpopulation of form I is
CC       subsequently converted to a smaller form (form II). Form II, with
CC       a revealed C-terminal glycine, is considered to be the
CC       phosphatidylethanolamine (PE)-conjugated form, and has the
CC       capacity for the binding to autophagosomes.
CC   -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the peptidase C54 family.
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DR   EMBL; AJ504653; CAD43220.1; -; mRNA.
DR   EMBL; AK028712; BAC26079.1; -; mRNA.
DR   EMBL; AK031570; BAC27455.1; -; mRNA.
DR   EMBL; AK075796; BAC35965.1; -; mRNA.
DR   EMBL; AK088811; BAC40587.1; -; mRNA.
DR   EMBL; BC027184; AAH27184.1; -; mRNA.
DR   EMBL; AK129242; BAC98052.1; -; mRNA.
DR   IPI; IPI00387185; -.
DR   RefSeq; NP_777363.1; -.
DR   UniGene; Mm.29087; -.
DR   SMR; Q8BGE6; 10-373.
DR   STRING; Q8BGE6; -.
DR   MEROPS; C54.003; -.
DR   PhosphoSite; Q8BGE6; -.
DR   PRIDE; Q8BGE6; -.
DR   Ensembl; ENSMUST00000027502; ENSMUSP00000027502; ENSMUSG00000026280; Mus musculus.
DR   GeneID; 66615; -.
DR   KEGG; mmu:66615; -.
DR   UCSC; uc007cej.1; mouse.
DR   CTD; 66615; -.
DR   MGI; MGI:1913865; Atg4b.
DR   HOGENOM; HBG403051; -.
DR   HOVERGEN; Q8BGE6; -.
DR   InParanoid; Q8BGE6; -.
DR   OrthoDB; EOG90ZTHB; -.
DR   PhylomeDB; Q8BGE6; -.
DR   ArrayExpress; Q8BGE6; -.
DR   Bgee; Q8BGE6; -.
DR   CleanEx; MM_ATG4B; -.
DR   Genevestigator; Q8BGE6; -.
DR   GermOnline; ENSMUSG00000026280; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR   GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005078; Peptidase_C54.
DR   PANTHER; PTHR22624; Peptidase_C54; 1.
DR   Pfam; PF03416; Peptidase_C54; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Autophagy; Cytoplasm; Hydrolase; Phosphoprotein;
KW   Protease; Protein transport; Thiol protease; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN         1    393       Cysteine protease ATG4B.
FT                                /FTId=PRO_0000215845.
FT   ACT_SITE     74     74       Nucleophile (By similarity).
FT   ACT_SITE    278    278       Potential.
FT   ACT_SITE    280    280       By similarity.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      34     34       Phosphoserine.
FT   MOD_RES     316    316       Phosphoserine (By similarity).
FT   MOD_RES     383    383       Phosphoserine.
FT   MOD_RES     392    392       Phosphoserine (By similarity).
FT   CONFLICT    128    153       IAQMGVGEGKSIGQWYGPNTVAQVLK -> NCLNCHCCGVM
FT                                LMLYKAHGSVLAFCR (in Ref. 3).
FT   CONFLICT    190    190       A -> V (in Ref. 1; CAD43220 and 2;
FT                                BAC26079/BAC27455/BAC35965).
FT   CONFLICT    325    325       T -> K (in Ref. 2; BAC40587, 3 and 4).
SQ   SEQUENCE   393 AA;  44375 MW;  EB9BF54B06F79135 CRC64;
     MDAATLTYDT LRFAEFEDFP ETSEPVWILG RKYSIFTEKD EILSDVASRL WFTYRRNFPA
     IGGTGPTSDT GWGCMLRCGQ MIFAQALVCR HLGRDWRWTQ RKRQPDSYFN VLNAFLDRKD
     SYYSIHQIAQ MGVGEGKSIG QWYGPNTVAQ VLKKLAVFDT WSSLAVHIAM DNTVVMEEIR
     RLCRANLPCA GAAALPTDSE RHCNGFPAGA EVTNRPSAWR PLVLLIPLRL GLTDINEAYV
     ETLKHCFMMP QSLGVIGGKP NSAHYFIGYV GEELIYLDPH TTQPAVELTD SCFIPDESFH
     CQHPPSRMGI GELDPSIAVG FFCKTEEDFN DWCQQVKKLS QLGGALPMFE LVEQQPSHLA
     CQDVLNLSLD SSDVERLERF FDSEDEDFEI LSL
//