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BECN1_SCHPO
ID   BECN1_SCHPO             Reviewed;         464 AA.
AC   P87117; P87116;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 4.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Vacuolar protein sorting-associated protein atg6;
DE   AltName: Full=Autophagy-related protein 6;
GN   Name=atg6; ORFNames=SPAC20G8.10c, SPAC3A12.01c;
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, AND SUBCELLULAR LOCATION.
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: Required for cytoplasm to vacuole transport (Cvt), autophagy,
CC       nucleophagy, and mitophagy, as a part of the autophagy-specific vps34
CC       PI3-kinase complex I. This complex is essential to recruit the atg8-
CC       phosphatidylinositol conjugate and the atg12-atg5 conjugate to the
CC       preautophagosomal structure. Also involved in endosome-to-Golgi
CC       retrograde transport as part of the vps34 PI3-kinase complex II (By
CC       similarity). Plays a role in meiosis and sporulation. {ECO:0000250,
CC       ECO:0000269|PubMed:19778961}.
CC   -!- SUBUNIT: Component of the autophagy-specific vps34 PI3-kinase complex I
CC       and of the vps34 PI3-kinase complex II. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein.
CC       Vacuole membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Preautophagosomal structure membrane; Peripheral
CC       membrane protein. Cytoplasm.
CC   -!- DOMAIN: The C-terminal domain called the BARA domain is dispensable for
CC       the construction of both vps34 PI3-kinase complexes, but is
CC       specifically required for autophagy through the targeting of complex I
CC       to the preautophagosomal structure. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC       {ECO:0000269|PubMed:23950735}.
CC   -!- SIMILARITY: Belongs to the beclin family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB08604.2; -; Genomic_DNA.
DR   PIR; T38669; T38669.
DR   RefSeq; XP_001713051.1; XM_001712999.2.
DR   AlphaFoldDB; P87117; -.
DR   SMR; P87117; -.
DR   BioGRID; 280624; 210.
DR   STRING; 4896.SPAC20G8.10c.1; -.
DR   iPTMnet; P87117; -.
DR   MaxQB; P87117; -.
DR   PaxDb; P87117; -.
DR   PRIDE; P87117; -.
DR   EnsemblFungi; SPAC20G8.10c.1; SPAC20G8.10c.1:pep; SPAC20G8.10c.
DR   PomBase; SPAC20G8.10c; atg6.
DR   VEuPathDB; FungiDB:SPAC20G8.10c; -.
DR   eggNOG; KOG2751; Eukaryota.
DR   HOGENOM; CLU_024219_3_1_1; -.
DR   InParanoid; P87117; -.
DR   OMA; DTFCIGH; -.
DR   Reactome; R-SPO-1632852; Macroautophagy.
DR   Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR   PRO; PR:P87117; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005768; C:endosome; IDA:PomBase.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000407; C:phagophore assembly site; IDA:PomBase.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IDA:PomBase.
DR   GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IDA:PomBase.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR   GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISO:PomBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.418.40; -; 1.
DR   InterPro; IPR007243; Atg6/Beclin.
DR   InterPro; IPR038274; Atg6/Beclin_C_sf.
DR   InterPro; IPR041691; Atg6/beclin_CC.
DR   InterPro; IPR040455; Atg6_BARA.
DR   PANTHER; PTHR12768; PTHR12768; 1.
DR   Pfam; PF04111; APG6; 1.
DR   Pfam; PF17675; APG6_N; 1.
PE   3: Inferred from homology;
KW   Autophagy; Coiled coil; Cytoplasm; Endosome; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport; Vacuole.
FT   CHAIN           1..464
FT                   /note="Vacuolar protein sorting-associated protein atg6"
FT                   /id="PRO_0000218560"
FT   REGION          38..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..461
FT                   /note="BARA"
FT                   /evidence="ECO:0000250"
FT   COILED          144..274
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   464 AA;  53960 MW;  F7897A1B6C45BB17 CRC64;
     MQYLCQRCHS LINFKDVYDD DLLKLKNLPK SRFVQASSLT EMNESGESDD QMNSSSEDYP
     AQRLQLYKKT ISEGDYNFDN VPPPELRTPT LDSFVVLPAA KDGYEEEKNS PEEVNDLFSW
     KIEIYNRIFD LLSSKTKVDH PLCVECAELL TEEMSKTLRA LKEEKKMYFN YDNFLSSQTV
     HEENTAALDS EIDELMKQIN EKEEKIEEIS DETDKLQKLL RELDEEKEKV YAEEQEFYNN
     LNQFQIKKLS LERQYDCANL EFEHNSRKLE KLQKMNVFSD IFYISHYSEP NGEGSIATIN
     GLRLGRLPSQ KVNWAEINAA WGMTVLLLDV LTEKLDFHSS SYQLKPFGSQ SFIIRFDRDP
     NGNQVKPTKL DLFSSGELKI FMNRRFDQGM VAFLDYLHQF GDFCAAKTPS AVLPYAIEND
     RIGGKCIRLA FNQDENWTRA LKFVLTDIKF LEAYVSSQDK QSNF
 
 
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