ID   ATG7_MOUSE              Reviewed;         698 AA.
AC   Q9D906; Q3TCD9; Q8K4Q5;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   14-DEC-2011, entry version 87.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7;
DE   AltName: Full=ATG12-activating enzyme E1 ATG7;
DE   AltName: Full=Autophagy-related protein 7;
DE            Short=APG7-like;
DE            Short=mAGP7;
DE   AltName: Full=Ubiquitin-activating enzyme E1-like protein;
GN   Name=Atg7; Synonyms=Apg7l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN GABARAPL1-ATG7 INTERMEDIATE
RP   CONJUGATE FORMATION, TISSUE SPECIFICITY, INTERACTION WITH ATG12, AND
RP   MUTAGENESIS OF CYS-567.
RC   TISSUE=Brain;
RX   MEDLINE=21888283; PubMed=11890701; DOI=10.1006/bbrc.2002.6645;
RA   Tanida I., Tanida-Miyake E., Nishitani T., Komatsu M., Yamazaki H.,
RA   Ueno T., Kominami E.;
RT   "Murine Apg12p has a substrate preference for murine Apg7p over three
RT   Apg8p homologs.";
RL   Biochem. Biophys. Res. Commun. 292:256-262(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Pancreas, Spleen, and Urinary bladder;
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   TISSUE=Eye;
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   INTERACTION WITH ATG10 AND ATG12.
RX   MEDLINE=22370793; PubMed=12482611; DOI=10.1016/S0014-5793(02)03739-0;
RA   Mizushima N., Yoshimori T., Ohsumi Y.;
RT   "Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the
RT   conjugation-mediated yeast two-hybrid method.";
RL   FEBS Lett. 532:450-454(2002).
RN   [5]
RP   FUNCTION.
RX   PubMed=20723759; DOI=10.1016/j.cell.2010.07.018;
RA   Radoshevich L., Murrow L., Chen N., Fernandez E., Roy S., Fung C.,
RA   Debnath J.;
RT   "ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and
RT   cell death.";
RL   Cell 142:590-600(2010).
CC   -!- FUNCTION: Functions as an E1 enzyme essential for multisubstrates
CC       such as ATG8-like proteins and ATG12. Forms intermediate
CC       conjugates with ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2
CC       or MAP1LC3A). PE-conjugation to ATG8-like proteins is essential
CC       for autophagy. Also acts as an E1 enzyme for ATG12 conjugation to
CC       ATG5 and ATG3.
CC   -!- SUBUNIT: Homodimer. Interacts with ATG3 and ATG12. The complex,
CC       composed of ATG3 and ATG7, plays a role in the conjugation of
CC       ATG12 to ATG5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Widely expressed, especially in kidney, liver,
CC       lymph nodes and bone marrow.
CC   -!- DOMAIN: The C-terminal part of the protein is essential for the
CC       dimerization and interaction with ATG3 and ATG12 (By similarity).
CC   -!- SIMILARITY: Belongs to the ATG7 family.
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DR   EMBL; AB079385; BAC10416.1; -; mRNA.
DR   EMBL; AK007484; BAB25060.1; -; mRNA.
DR   EMBL; AK035604; BAC29122.1; -; mRNA.
DR   EMBL; AK161133; BAE36208.1; -; mRNA.
DR   EMBL; AK170769; BAE42018.1; -; mRNA.
DR   EMBL; AK172272; BAE42917.1; -; mRNA.
DR   EMBL; BC058597; AAH58597.1; -; mRNA.
DR   IPI; IPI00463195; -.
DR   RefSeq; NP_083111.1; NM_028835.3.
DR   UniGene; Mm.275332; -.
DR   ProteinModelPortal; Q9D906; -.
DR   SMR; Q9D906; 347-502.
DR   STRING; Q9D906; -.
DR   PhosphoSite; Q9D906; -.
DR   PRIDE; Q9D906; -.
DR   Ensembl; ENSMUST00000032457; ENSMUSP00000032457; ENSMUSG00000030314.
DR   Ensembl; ENSMUST00000169310; ENSMUSP00000133215; ENSMUSG00000030314.
DR   GeneID; 74244; -.
DR   KEGG; mmu:74244; -.
DR   UCSC; uc009dhz.1; mouse.
DR   CTD; 10533; -.
DR   MGI; MGI:1921494; Atg7.
DR   GeneTree; ENSGT00390000017509; -.
DR   HOGENOM; HBG619497; -.
DR   HOVERGEN; HBG080877; -.
DR   InParanoid; Q9D906; -.
DR   OMA; ANEIWES; -.
DR   OrthoDB; EOG43N7C8; -.
DR   PhylomeDB; Q9D906; -.
DR   NextBio; 340222; -.
DR   ArrayExpress; Q9D906; -.
DR   Bgee; Q9D906; -.
DR   CleanEx; MM_ATG7; -.
DR   Genevestigator; Q9D906; -.
DR   GermOnline; ENSMUSG00000030314; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019778; F:APG12 activating enzyme activity; IMP:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; IDA:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0006914; P:autophagy; IMP:MGI.
DR   GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IMP:MGI.
DR   GO; GO:0016044; P:cellular membrane organization; IMP:MGI.
DR   GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI.
DR   GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR   GO; GO:0050877; P:neurological system process; IMP:MGI.
DR   GO; GO:0006996; P:organelle organization; IMP:MGI.
DR   GO; GO:0031401; P:positive regulation of protein modification process; IDA:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0021860; P:pyramidal neuron development; IMP:MGI.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; IMP:MGI.
DR   GO; GO:0042594; P:response to starvation; IMP:MGI.
DR   InterPro; IPR006285; E1-like_Apg7.
DR   InterPro; IPR009036; Molybdenum_cofac_synth_MoeB.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2.
DR   KO; K08337; -.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; MoeB; 1.
DR   TIGRFAMs; TIGR01381; E1_like_apg7; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Autophagy; Complete proteome; Cytoplasm;
KW   Protein transport; Reference proteome; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN         1    698       Ubiquitin-like modifier-activating enzyme
FT                                ATG7.
FT                                /FTId=PRO_0000212807.
FT   ACT_SITE    567    567       Glycyl thioester intermediate (Probable).
FT   MOD_RES     302    302       N6-acetyllysine (By similarity).
FT   MUTAGEN     567    567       C->S: Instead of the formation of an
FT                                intermediate complex with a thiol ester
FT                                bond between ATG7 (E1-like enzyme) and
FT                                GABARAPL1 (MAP1LC3, GABARAP or GABARAPL;
FT                                substrates), a stable complex with an O-
FT                                ester bond is formed.
FT   CONFLICT     22     22       F -> L (in Ref. 1; BAC10416).
SQ   SEQUENCE   698 AA;  77520 MW;  79D94EA7464C6ADB CRC64;
     MGDPGLAKLQ FAPFNSALDV GFWHELTQKK LNEYRLDEAP KDIKGYYYNG DSAGLPTRLT
     LEFSAFDMSA STPAHCCPAM GTLHNTNTLE AFKTADKKLL LEQSANEIWE AIKSGAALEN
     PMLLNKFLLL TFADLKKYHF YYWFCCPALC LPESIPLIRG PVSLDQRLSP KQIQALEHAY
     DDLCRAEGVT ALPYFLFKYD DDTVLVSLLK HYSDFFQGQR TKITVGVYDP CNLAQYPGWP
     LRNFLVLAAH RWSGSFQSVE VLCFRDRTMQ GARDVTHSII FEVKLPEMAF SPDCPKAVGW
     EKNQKGGMGP RMVNLSGCMD PKRLAESSVD LNLKLMCWRL VPTLDLDKVV SVKCLLLGAG
     TLGCNVARTL MGWGVRHVTF VDNAKISYSN PVRQPLYEFE DCLGGGKPKA LAAAERLQKI
     FPGVNARGFN MSIPMPGHPV NFSDVTMEQA RRDVEQLEQL IDNHDVIFLL MDTRESRWLP
     TVIAASKRKL VINAALGFDT FVVMRHGLKK PKQQGAGDLC PSHLVAPADL GSSLFANIPG
     YKLGCYFCND VVAPGDSTRD RTLDQQCTVS RPGLAVIAGA LAVELMVSVL QHPEGGYAIA
     SSSDDRMNEP PTSLGLVPHQ IRGFLSRFDN VLPVSLAFDK CTACSPKVLD QYEREGFTFL
     AKVFNSSHSF LEDLTGLTLL HQETQAAEIW DMSDEETV
//