ID   ATG12_NEUCR             Reviewed;         157 AA.
AC   Q7S083;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Ubiquitin-like protein atg12;
DE   AltName: Full=Autophagy-related protein 12;
GN   Name=atg12; ORFNames=NCU10049;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Ubiquitin-like protein involved in cytoplasm to vacuole
CC       transport (Cvt), autophagy vesicles formation, mitophagy, and
CC       nucleophagy. Conjugation with apg-4/atg5 through a ubiquitin-like
CC       conjugating system involving also apg-5/atg7 as an E1-like activating
CC       enzyme and atg10 as an E2-like conjugating enzyme, is essential for its
CC       function. The atg12-apg-4/atg5 conjugate functions as an E3-like enzyme
CC       which is required for lipidation of apg-6/atg8 and apg-6/atg8
CC       association to the vesicle membranes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a conjugate with apg-4/atg5. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG12 family. {ECO:0000305}.
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DR   EMBL; CM002241; EAA28720.3; -; Genomic_DNA.
DR   RefSeq; XP_957956.3; XM_952863.3.
DR   AlphaFoldDB; Q7S083; -.
DR   SMR; Q7S083; -.
DR   STRING; 367110.Q7S083; -.
DR   EnsemblFungi; EAA28720; EAA28720; NCU10049.
DR   GeneID; 3874103; -.
DR   KEGG; ncr:NCU10049; -.
DR   VEuPathDB; FungiDB:NCU10049; -.
DR   HOGENOM; CLU_106795_1_1_1; -.
DR   InParanoid; Q7S083; -.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR   GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007242; Atg12.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR13385; PTHR13385; 1.
DR   Pfam; PF04110; APG12; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   3: Inferred from homology;
KW   Autophagy; Isopeptide bond; Membrane; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation pathway.
FT   CHAIN           1..157
FT                   /note="Ubiquitin-like protein atg12"
FT                   /id="PRO_0000212482"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        157
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-263 in ATG5)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   157 AA;  17001 MW;  B887E991D4C44008 CRC64;
     MASSQPLHGT ASPSLVHDDN NPNSSTASPV LEGRDSPNLP LTMTASTVLM TLPRDATAAL
     AEAGTFDQEK VVIRFKPVGS APALRREQVK VLSTHSFETV VAYLRKTLKV QETDSVFLYV
     NSVFAPALDE VVGNLWRCFK DSTNQLNVSY SMTPSFG