ID   ATG7_HUMAN              Reviewed;         703 AA.
AC   O95352; Q7L8L0; Q9BWP2; Q9UFH4;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   09-FEB-2010, entry version 72.
DE   RecName: Full=Autophagy-related protein 7;
DE   AltName: Full=APG7-like;
DE            Short=hAGP7;
DE   AltName: Full=Ubiquitin-activating enzyme E1-like protein;
GN   Name=ATG7; Synonyms=APG7L;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=99250148; PubMed=10233149;
RA   Yuan W., Stromhaug P.E., Dunn W.A. Jr.;
RT   "Glucose-induced autophagy of peroxisomes in Pichia pastoris requires
RT   a unique E1-like protein.";
RL   Mol. Biol. Cell 10:1353-1366(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 179-703 (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   TISSUE SPECIFICITY.
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   [5]
RP   INTERACTION WITH ATG3 AND ATG12.
RC   TISSUE=Brain;
RX   MEDLINE=21950715; PubMed=11825910; DOI=10.1074/jbc.M200385200;
RA   Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
RT   "Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
RT   substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the
RT   conjugation of hApg12p to hApg5p.";
RL   J. Biol. Chem. 277:13739-13744(2002).
RN   [6]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-306, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
CC   -!- FUNCTION: Functions as an E1 enzyme essential for multisubstrates
CC       such as GABARAPL1 and ATG12. Forms intermediate conjugates with
CC       GABARAPL1 (GABARAPL2, GABARAP or MAP1ALC3). Formation of the final
CC       GABARAPL1-PE conjugate is essential for autophagy (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with ATG3 and ATG12.
CC       The complex, composed of ATG3 and ATG7, plays a role in the
CC       conjugation of ATG12 to ATG5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O95352-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O95352-2; Sequence=VSP_013205;
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; AF094516; AAC69630.1; -; mRNA.
DR   EMBL; BC000091; AAH00091.1; -; mRNA.
DR   EMBL; AL122075; CAB59250.1; -; mRNA.
DR   IPI; IPI00007404; -.
DR   IPI; IPI00479911; -.
DR   PIR; T34556; T34556.
DR   RefSeq; NP_001129503.2; -.
DR   RefSeq; NP_001138384.1; -.
DR   RefSeq; NP_006386.1; -.
DR   SMR; O95352; 15-68, 349-597.
DR   DIP; DIP-29759N; -.
DR   IntAct; O95352; 4.
DR   STRING; O95352; -.
DR   PRIDE; O95352; -.
DR   Ensembl; ENST00000354449; ENSP00000346437; ENSG00000197548; Homo sapiens.
DR   GeneID; 10533; -.
DR   KEGG; hsa:10533; -.
DR   UCSC; uc003bwc.1; human.
DR   UCSC; uc003bwd.1; human.
DR   CTD; 10533; -.
DR   GeneCards; GC03P011290; -.
DR   H-InvDB; HIX0003055; -.
DR   HGNC; HGNC:16935; ATG7.
DR   HPA; CAB018771; -.
DR   HPA; HPA007639; -.
DR   MIM; 608760; gene.
DR   PharmGKB; PA134983397; -.
DR   eggNOG; prNOG15924; -.
DR   HOGENOM; HBG619497; -.
DR   HOVERGEN; O95352; -.
DR   InParanoid; O95352; -.
DR   OMA; ANEIWES; -.
DR   OrthoDB; EOG9R7XXG; -.
DR   PhylomeDB; O95352; -.
DR   NextBio; 39961; -.
DR   ArrayExpress; O95352; -.
DR   Bgee; O95352; -.
DR   CleanEx; HS_ATG7; -.
DR   Genevestigator; O95352; -.
DR   GermOnline; ENSG00000197548; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; TAS:ProtInc.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0006944; P:membrane fusion; TAS:ProtInc.
DR   GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW.
DR   GO; GO:0031401; P:positive regulation of protein modification...; IDA:MGI.
DR   GO; GO:0006497; P:protein amino acid lipidation; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   TIGRFAMs; TIGR01381; E1_like_apg7; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Autophagy; Complete proteome;
KW   Cytoplasm; Polymorphism; Protein transport; Transport;
KW   Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    703       Autophagy-related protein 7.
FT                                /FTId=PRO_0000212806.
FT   ACT_SITE    572    572       Glycyl thioester intermediate
FT                                (Potential).
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES     306    306       N6-acetyllysine.
FT   VAR_SEQ     626    652       Missing (in isoform 2).
FT                                /FTId=VSP_013205.
FT   VARIANT     471    471       V -> A (in dbSNP:rs36117895).
FT                                /FTId=VAR_053014.
SQ   SEQUENCE   703 AA;  77960 MW;  ABBD1A29A6C58356 CRC64;
     MAAATGDPGL SKLQFAPFSS ALDVGFWHEL TQKKLNEYRL DEAPKDIKGY YYNGDSAGLP
     ARLTLEFSAF DMSAPTPARC CPAIGTLYNT NTLESFKTAD KKLLLEQAAN EIWESIKSGT
     ALENPVLLNK FLLLTFADLK KYHFYYWFCY PALCLPESLP LIQGPVGLDQ RFSLKQIEAL
     ECAYDNLCQT EGVTALPYFL IKYDENMVLV SLLKHYSDFF QGQRTKITIG VYDPCNLAQY
     PGWPLRNFLV LAAHRWSSSF QSVEVVCFRD RTMQGARDVA HSIIFEVKLP EMAFSPDCPK
     AVGWEKNQKG GMGPRMVNLS ECMDPKRLAE SSVDLNLKLM CWRLVPTLDL DKVVSVKCLL
     LGAGTLGCNV ARTLMGWGVR HITFVDNAKI SYSNPVRQPL YEFEDCLGGG KPKALAAADR
     LQKIFPGVNA RGFNMSIPMP GHPVNFSSVT LEQARRDVEQ LEQLIESHDV VFLLMDTRES
     RWLPAVIAAS KRKLVINAAL GFDTFVVMRH GLKKPKQQGA GDLCPNHPVA SADLLGSSLF
     ANIPGYKLGC YFCNDVVAPG DSTRDRTLDQ QCTVSRPGLA VIAGALAVEL MVSVLQHPEG
     GYAIASSSDD RMNEPPTSLG LVPHQIRGFL SRFDNVLPVS LAFDKCTACS SKVLDQYERE
     GFNFLAKVFN SSHSFLEDLT GLTLLHQETQ AAEIWDMSDD ETI
//