ID   ATG3_HUMAN              Reviewed;         314 AA.
AC   Q9NT62; Q6PKC5; Q9H6L9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-NOV-2009, entry version 62.
DE   RecName: Full=Autophagy-related protein 3;
DE   AltName: Full=APG3-like;
DE            Short=hApg3;
DE   AltName: Full=Protein PC3-96;
GN   Name=ATG3; Synonyms=APG3, APG3L;
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), TISSUE SPECIFICITY,
RP   MUTAGENESIS OF CYS-264, SUBCELLULAR LOCATION, CHARACTERIZATION, AND
RP   INTERACTION WITH ATG7 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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RA   Wu B.X., Li Y., Laser M., Crosson C.E., Hazard E.S. III, Ma J.X.;
RT   "Cloning and characterization of human PC3-96 gene.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Lung, and Lymph;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-314 (ISOFORM 2).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-18, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [7]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: GABARAPL1 (GABARAPL2 or GABARAP or MAP1LC3)-modifier
CC       protein conjugating enzyme involved in its E2-like covalent
CC       binding to PE. ATG7 (E1-like enzyme) facilitates this reaction by
CC       forming an E1-E2 complex with ATG3 (E2-like enzyme). Preferred
CC       substrate is MAP1LC3A. Formation of the GABARAPL1-PE conjugate is
CC       essential for autophagy.
CC   -!- SUBUNIT: Interacts with ATG7 and ATG12. The complex, composed of
CC       ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5.
CC   -!- INTERACTION:
CC       P60520:GABARAPL2; NbExp=1; IntAct=EBI-988094, EBI-720116;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NT62-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NT62-2; Sequence=VSP_013037;
CC         Note=No experimental confirmation available. Ref.4 (AAH02830)
CC         isoform 2 sequence differs from that shown due to a frameshift
CC         in position 311;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with a highest expression in
CC       heart, skeletal muscle, kidney, liver and placenta.
CC   -!- SIMILARITY: Belongs to the ATG3 family.
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DR   EMBL; AB079384; BAB90843.1; -; mRNA.
DR   EMBL; AF202092; AAG35611.1; -; mRNA.
DR   EMBL; AL137515; CAB70781.1; -; mRNA.
DR   EMBL; BC002830; AAH02830.1; ALT_FRAME; mRNA.
DR   EMBL; BC024221; AAH24221.1; -; mRNA.
DR   EMBL; AK025778; BAB15237.1; ALT_INIT; mRNA.
DR   IPI; IPI00022254; -.
DR   IPI; IPI00449201; -.
DR   PIR; T46276; T46276.
DR   RefSeq; NP_071933.2; -.
DR   UniGene; Hs.477126; -.
DR   IntAct; Q9NT62; 6.
DR   STRING; Q9NT62; -.
DR   PhosphoSite; Q9NT62; -.
DR   PRIDE; Q9NT62; -.
DR   Ensembl; ENST00000283290; ENSP00000283290; ENSG00000144848; Homo sapiens.
DR   Ensembl; ENST00000402314; ENSP00000385943; ENSG00000144848; Homo sapiens.
DR   GeneID; 64422; -.
DR   KEGG; hsa:64422; -.
DR   UCSC; uc003dzc.2; human.
DR   UCSC; uc003dzd.1; human.
DR   CTD; 64422; -.
DR   GeneCards; GC03M113735; -.
DR   H-InvDB; HIX0003548; -.
DR   HGNC; HGNC:20962; ATG3.
DR   MIM; 609606; gene.
DR   PharmGKB; PA134883444; -.
DR   HOGENOM; Q9NT62; -.
DR   HOVERGEN; Q9NT62; -.
DR   OMA; YHNTGIA; -.
DR   NextBio; 66413; -.
DR   ArrayExpress; Q9NT62; -.
DR   Bgee; Q9NT62; -.
DR   CleanEx; HS_ATG3; -.
DR   Genevestigator; Q9NT62; -.
DR   GermOnline; ENSG00000144848; Homo sapiens.
DR   GO; GO:0000153; C:cytoplasmic ubiquitin ligase complex; IPI:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0019787; F:small conjugating protein ligase activity; IDA:MGI.
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   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   InterPro; IPR007135; Autophagy-rel_prot_3.
DR   InterPro; IPR019461; Autophagy-rel_prot_3_C.
DR   InterPro; IPR007134; Autophagy-rel_prot_3_N.
DR   Pfam; PF03987; Autophagy_act_C; 1.
DR   Pfam; PF10381; Autophagy_Cterm; 1.
DR   Pfam; PF03986; Autophagy_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Autophagy; Complete proteome; Cytoplasm;
KW   Phosphoprotein; Protein transport; Transport; Ubl conjugation pathway.
FT   CHAIN         1    314       Autophagy-related protein 3.
FT                                /FTId=PRO_0000213569.
FT   ACT_SITE    264    264       Glycyl thioester intermediate
FT                                (Potential).
FT   MOD_RES      18     18       Phosphotyrosine.
FT   VAR_SEQ     290    314       LLIFLKFVQAVIPTIEYDYTRHFTM -> PSLYVRLVAKWL
FT                                LTIFFLRNLV (in isoform 2).
FT                                /FTId=VSP_013037.
FT   MUTAGEN     264    264       C->S: Instead of the formation of an
FT                                intermediate complex with a thiol ester
FT                                bond between ATG3 (E2-like enzyme) and
FT                                GABARAPL1/APG8L (substrate), a stable
FT                                complex with an O-ester bond is formed.
SQ   SEQUENCE   314 AA;  35864 MW;  40EFE88DB5FE3EAB CRC64;
     MQNVINTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFV AAGDHLVHHC PTWQWATGEE
     LKVKAYLPTG KQFLVTKNVP CYKRCKQMEY SDELEAIIEE DDGDGGWVDT YHNTGITGIT
     EAVKEITLEN KDNIRLQDCS ALCEEEEDED EGEAADMEEY EESGLLETDE ATLDTRKIVE
     ACKAKTDAGG EDAILQTRTY DLYITYDKYY QTPRLWLFGY DEQRQPLTVE HMYEDISQDH
     VKKTVTIENH PHLPPPPMCS VHPCRHAEVM KKIIETVAEG GGELGVHMYL LIFLKFVQAV
     IPTIEYDYTR HFTM
//