位置:首页 > 蛋白库 > ATG3_SCHPO
ATG3_SCHPO
ID   ATG3_SCHPO              Reviewed;         275 AA.
AC   O43035;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Autophagy-related protein 3;
DE   AltName: Full=Autophagy-related E2-like conjugation enzyme atg3;
GN   Name=atg3; ORFNames=SPBC3B9.06c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   FUNCTION.
RX   PubMed=19778961; DOI=10.1099/mic.0.034389-0;
RA   Mukaiyama H., Kajiwara S., Hosomi A., Giga-Hama Y., Tanaka N., Nakamura T.,
RA   Takegawa K.;
RT   "Autophagy-deficient Schizosaccharomyces pombe mutants undergo partial
RT   sporulation during nitrogen starvation.";
RL   Microbiology 155:3816-3826(2009).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23950735; DOI=10.1371/journal.pgen.1003715;
RA   Sun L.L., Li M., Suo F., Liu X.M., Shen E.Z., Yang B., Dong M.Q., He W.Z.,
RA   Du L.L.;
RT   "Global analysis of fission yeast mating genes reveals new autophagy
RT   factors.";
RL   PLoS Genet. 9:E1003715-E1003715(2013).
CC   -!- FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole
CC       transport (Cvt) and autophagy. Required for selective autophagic
CC       degradation of the nucleus (nucleophagy) as well as for mitophagy which
CC       contributes to regulate mitochondrial quantity and quality by
CC       eliminating the mitochondria to a basal level to fulfill cellular
CC       energy requirements and preventing excess ROS production. Responsible
CC       for the E2-like covalent binding of phosphatidylethanolamine to the C-
CC       terminal Gly of atg8. The atg12-atg5 conjugate plays a role of an E3
CC       and promotes the transfer of atg8 from atg3 to phosphatidylethanolamine
CC       (PE). This step is required for the membrane association of atg8. The
CC       formation of the atg8-phosphatidylethanolamine conjugate is essential
CC       for autophagy and for the cytoplasm to vacuole transport (Cvt). The
CC       atg8-PE conjugate mediates tethering between adjacent membranes and
CC       stimulates membrane hemifusion, leading to expansion of the
CC       autophagosomal membrane during autophagy (By similarity). Plays a role
CC       in meiosis and sporulation. {ECO:0000250, ECO:0000269|PubMed:19778961}.
CC   -!- SUBUNIT: Monomer. Interacts with atg8 through an intermediate thioester
CC       bond through the C-terminal Gly of atg8. Also interacts with the 40
CC       amino acid C-terminal region of the E1-like atg7 enzyme. Interacts also
CC       with the atg12-atg5 conjugate. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- DOMAIN: The N-terminal region is involved in phosphatidylethanolamine-
CC       binding and is required for atg8-PE conjugation. {ECO:0000250}.
CC   -!- DOMAIN: The flexible region (FR) is required for atg7-binding.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The handle region (HR) contains the atg8 interaction motif
CC       (AIM) and mediates binding to atg8. It is crucial for the cytoplasm-to-
CC       vacuole targeting pathway (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC       {ECO:0000269|PubMed:23950735}.
CC   -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329671; CAA17786.1; -; Genomic_DNA.
DR   PIR; T40345; T40345.
DR   RefSeq; NP_596664.1; NM_001022586.2.
DR   AlphaFoldDB; O43035; -.
DR   SMR; O43035; -.
DR   BioGRID; 277540; 4.
DR   STRING; 4896.SPBC3B9.06c.1; -.
DR   iPTMnet; O43035; -.
DR   MaxQB; O43035; -.
DR   PaxDb; O43035; -.
DR   PRIDE; O43035; -.
DR   EnsemblFungi; SPBC3B9.06c.1; SPBC3B9.06c.1:pep; SPBC3B9.06c.
DR   GeneID; 2541025; -.
DR   KEGG; spo:SPBC3B9.06c; -.
DR   PomBase; SPBC3B9.06c; atg3.
DR   VEuPathDB; FungiDB:SPBC3B9.06c; -.
DR   eggNOG; KOG2981; Eukaryota.
DR   HOGENOM; CLU_027518_2_0_1; -.
DR   InParanoid; O43035; -.
DR   OMA; IKEIYIH; -.
DR   PhylomeDB; O43035; -.
DR   Reactome; R-SPO-1632852; Macroautophagy.
DR   PRO; PR:O43035; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000153; C:cytoplasmic ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0019776; F:Atg8 ligase activity; ISO:PomBase.
DR   GO; GO:0000045; P:autophagosome assembly; ISO:PomBase.
DR   GO; GO:0006914; P:autophagy; IMP:PomBase.
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; ISO:PomBase.
DR   GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007135; Atg3/Atg10.
DR   PANTHER; PTHR12866; PTHR12866; 1.
DR   Pfam; PF03987; Autophagy_act_C; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Nucleus; Protein transport; Reference proteome;
KW   Transport; Ubl conjugation pathway.
FT   CHAIN           1..275
FT                   /note="Autophagy-related protein 3"
FT                   /id="PRO_0000213584"
FT   REGION          83..156
FT                   /note="Flexible region"
FT                   /evidence="ECO:0000250"
FT   REGION          123..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..251
FT                   /note="Handle region"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        124..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        227
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1..10
FT                   /ligand="1,2-diacylglycero-3-phosphoethanolamine"
FT                   /ligand_id="ChEBI:CHEBI:57613"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   275 AA;  31886 MW;  8877B33079B592F7 CRC64;
     MAQRLTSAFL NWREHITPAS KTSDFENTGM ISPEEFVLAG DYLVSKFPTW SWECGDRIRG
     FLPKDKQYLV TRHVFCVQRN INIGVNEEWV DIETDDTRNK DDDQDDDAIS SIHSDTSDIA
     SAERLKGQSK ELSDSGPLPL KDEEDDDQMV SPVIKEDEGR YYDLYIVYDK YYRTPRLFLR
     GWNAGGQLLT MKDIYEDVSG EHAGKTVTME PFPHYHSHNT MASVHPCKHA SVLLKLIKQH
     RERNDPIRVD QYMVLFLKFV STMLPYFEID YTIQA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024