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ATG13_CAEEL
ID   ATG13_CAEEL             Reviewed;         443 AA.
AC   P34379;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Autophagy-related protein 13 homolog;
GN   Name=atg-13 {ECO:0000303|PubMed:19377305, ECO:0000312|WormBase:D2007.5};
GN   Synonyms=epg-1 {ECO:0000303|PubMed:19377305, ECO:0000312|WormBase:D2007.5};
GN   ORFNames=D2007.5 {ECO:0000312|WormBase:D2007.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH UNC-51, SUBCELLULAR
RP   LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=19377305; DOI=10.4161/auto.5.5.8624;
RA   Tian E., Wang F., Han J., Zhang H.;
RT   "epg-1 functions in autophagy-regulated processes and may encode a highly
RT   divergent Atg13 homolog in C. elegans.";
RL   Autophagy 5:608-615(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LGG-1.
RX   PubMed=26687600; DOI=10.1016/j.molcel.2015.11.019;
RA   Wu F., Watanabe Y., Guo X.Y., Qi X., Wang P., Zhao H.Y., Wang Z.,
RA   Fujioka Y., Zhang H., Ren J.Q., Fang T.C., Shen Y.X., Feng W., Hu J.J.,
RA   Noda N.N., Zhang H.;
RT   "Structural Basis of the Differential Function of the Two C. elegans Atg8
RT   Homologs, LGG-1 and LGG-2, in Autophagy.";
RL   Mol. Cell 60:914-929(2015).
CC   -!- FUNCTION: Component of the unc-51/atg-13 complex required for
CC       autophagosome formation (PubMed:19377305, PubMed:26687600). Required
CC       for the degradation of germ cell specific P-granule components such as
CC       sepa-1 by autophagy in somatic cells (PubMed:19377305). This ensures
CC       exclusive localization of the P-granules in germ cells
CC       (PubMed:19377305). May function downstream of the let-363 (Tor)
CC       signaling pathway to mediate sepa-1 degradation (PubMed:19377305).
CC       Plays a role in survival during limited food availability
CC       (PubMed:19377305). {ECO:0000269|PubMed:19377305,
CC       ECO:0000269|PubMed:26687600}.
CC   -!- SUBUNIT: Interacts with unc-51 (via C-terminus) (PubMed:19377305).
CC       Interacts with lgg-1; the interaction is direct (PubMed:26687600).
CC       {ECO:0000269|PubMed:19377305, ECO:0000269|PubMed:26687600}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:O75143}. Cytoplasm
CC       {ECO:0000269|PubMed:19377305}. Preautophagosomal structure
CC       {ECO:0000269|PubMed:26687600}. Perikaryon
CC       {ECO:0000269|PubMed:19377305}. Cell projection, axon
CC       {ECO:0000269|PubMed:19377305}. Note=Under starvation conditions, is
CC       localized to punctate structures primarily representing the isolation
CC       membrane that sequesters a portion of the cytoplasm resulting in the
CC       formation of an autophagosome. Recruited to preautophagosomes by lgg-1
CC       (PubMed:26687600). {ECO:0000250|UniProtKB:O75143,
CC       ECO:0000269|PubMed:26687600}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from the 8-cell stage and subsequently
CC       throughout embryogenesis. After hatching, highly expressed in neurons
CC       including nerve ring cells, neurons in the tail and DD/VD motor neurons
CC       in the ventral nerve cord. Also expressed in body wall muscle and
CC       pharyngeal muscle. {ECO:0000269|PubMed:19377305}.
CC   -!- SIMILARITY: Belongs to the ATG13 family. Metazoan subfamily.
CC       {ECO:0000305}.
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DR   EMBL; FO080532; CCD64450.1; -; Genomic_DNA.
DR   PIR; S44786; S44786.
DR   RefSeq; NP_498782.1; NM_066381.4.
DR   AlphaFoldDB; P34379; -.
DR   SMR; P34379; -.
DR   BioGRID; 41356; 5.
DR   ComplexPortal; CPX-4821; unc-51-atg-13 complex.
DR   STRING; 6239.D2007.5.1; -.
DR   EPD; P34379; -.
DR   PaxDb; P34379; -.
DR   PeptideAtlas; P34379; -.
DR   EnsemblMetazoa; D2007.5.1; D2007.5.1; WBGene00017045.
DR   GeneID; 176150; -.
DR   KEGG; cel:CELE_D2007.5; -.
DR   CTD; 176150; -.
DR   WormBase; D2007.5; CE00130; WBGene00017045; atg-13.
DR   eggNOG; KOG3874; Eukaryota.
DR   GeneTree; ENSGT00390000007055; -.
DR   HOGENOM; CLU_050282_0_0_1; -.
DR   InParanoid; P34379; -.
DR   OMA; MHFEEPE; -.
DR   OrthoDB; 935872at2759; -.
DR   Reactome; R-CEL-1632852; Macroautophagy.
DR   PRO; PR:P34379; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00017045; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR   GO; GO:0005776; C:autophagosome; IC:ComplexPortal.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:1902554; C:serine/threonine protein kinase complex; IC:ComplexPortal.
DR   GO; GO:0000045; P:autophagosome assembly; IC:ComplexPortal.
DR   GO; GO:0006914; P:autophagy; IC:ComplexPortal.
DR   GO; GO:0016236; P:macroautophagy; IC:ComplexPortal.
DR   GO; GO:0000423; P:mitophagy; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR   Gene3D; 3.30.900.10; -; 1.
DR   InterPro; IPR040182; ATG13.
DR   InterPro; IPR036570; HORMA_dom_sf.
DR   PANTHER; PTHR13430; PTHR13430; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Cell projection; Cytoplasm; Reference proteome.
FT   CHAIN           1..443
FT                   /note="Autophagy-related protein 13 homolog"
FT                   /id="PRO_0000065267"
FT   REGION          232..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   443 AA;  49800 MW;  15B085155B8B485B CRC64;
     MVNEYDTYNK WLKFFSVRMV QSIIQSRLGD EIESKCVPYS ENAVDWFNMR IDELGEISAY
     LKSNIKSYPP VGTLTLEFLL YTPSGQLLPL EAWILSSSEG TDDCSRNELY HDMSTLLRSA
     IVSARMTPMH RLYVKKQHLE TFVIMYRVFE NDISSDMGKG KKTRKIGELV SKFGNISLDL
     HYRTSMHFEE PEIAPVTPVE DVEEEIDDGE KTVVDENIQT RTVSECVPIA DAKKRKASGS
     VESATSAGSS TSREAAPRFI LGQSTSSEDS RHSDVQNSYE EDHKPSLADL RNHSFPFVNL
     LQSAYNPANG TKKNSSSTCL NSPKSTPEDK EPTIEKVAES FRAAKIDEVV FEEDEDEELP
     LDSMELSEDS FVHFNQLSDF GGAPSLGNEL GDYLKQLKTA PDMTESGDID ICNMDLKTEL
     EKISSQTANF NNFLKHVNSF SDE
 
 
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