ALLO1_CAEEL
ID ALLO1_CAEEL Reviewed; 402 AA.
AC Q9U389; Q21891;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Allophagy receptor allo-1 {ECO:0000305};
GN Name=allo-1 {ECO:0000303|PubMed:29255173, ECO:0000312|WormBase:R102.5b};
GN ORFNames=R102.5 {ECO:0000312|WormBase:R102.5b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH IKKE-1;
RP LGG-1 AND UBIQUITINATED PROTEINS, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DOMAIN, PROTEOLYTIC DEGRADATION, PHOSPHORYLATION AT THR-74,
RP AND MUTAGENESIS OF 13-PHE--ILE-16 AND THR-74.
RX PubMed=29255173; DOI=10.1038/s41556-017-0008-9;
RA Sato M., Sato K., Tomura K., Kosako H., Sato K.;
RT "The autophagy receptor ALLO-1 and the IKKE-1 kinase control clearance of
RT paternal mitochondria in Caenorhabditis elegans.";
RL Nat. Cell Biol. 20:81-91(2018).
CC -!- FUNCTION: Autophagy receptor, which is required for allophagy, an
CC autophagic process in which paternal organelles, including mitochondria
CC and membranous organelles, are degraded in early embryos. After
CC fertilization, recruited to ubiquitin-modified paternal organelles and
CC is required for the formation of autophagosomes around the paternal
CC organelles. Also plays a role in the regulation of autophagy in germ
CC cells. {ECO:0000269|PubMed:29255173}.
CC -!- SUBUNIT: Self-associates. Interacts (via N-terminus) with ikke-1; the
CC interaction is direct. Interacts (via the LIR motif) with lgg-1.
CC Interacts (via C-terminus) with ubiquitinated proteins.
CC {ECO:0000269|PubMed:29255173}.
CC -!- INTERACTION:
CC Q9U389; P34605: trpp-3; NbExp=2; IntAct=EBI-312154, EBI-312149;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29255173}.
CC Note=Localizes to cytoplasmic puncta in oocytes and to paternal
CC organelles in 1-stage embryos. After fertilization, localizes around
CC paternal mitochondria and ubiquitinated membranous organelles at
CC metaphase phase of meiosis I, before lgg-1 is recruited. Also,
CC localizes to paternal organelles during meiosis II. Co-localizes with
CC ikke-1 in embryos and oocytes. {ECO:0000269|PubMed:29255173}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:R102.5b};
CC IsoId=Q9U389-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:R102.5a};
CC IsoId=Q9U389-2; Sequence=VSP_059584, VSP_059585;
CC -!- TISSUE SPECIFICITY: Expressed in oocytes, but not in spermatozoa.
CC {ECO:0000269|PubMed:29255173}.
CC -!- DOMAIN: The C-terminal region is required for localization to paternal
CC organelles. {ECO:0000269|PubMed:29255173}.
CC -!- PTM: Phosphorylation on Thr-74 by ikke-1 is required for allophagic
CC function. {ECO:0000269|PubMed:29255173}.
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DR EMBL; BX284604; CAA94359.2; -; Genomic_DNA.
DR EMBL; BX284604; CAB54290.2; -; Genomic_DNA.
DR PIR; T24101; T24101.
DR PIR; T24105; T24105.
DR RefSeq; NP_501980.2; NM_069579.4. [Q9U389-1]
DR RefSeq; NP_501981.2; NM_069580.4. [Q9U389-2]
DR AlphaFoldDB; Q9U389; -.
DR SMR; Q9U389; -.
DR DIP; DIP-26223N; -.
DR IntAct; Q9U389; 7.
DR STRING; 6239.R102.5b; -.
DR iPTMnet; Q9U389; -.
DR EPD; Q9U389; -.
DR PaxDb; Q9U389; -.
DR PeptideAtlas; Q9U389; -.
DR EnsemblMetazoa; R102.5a.1; R102.5a.1; WBGene00011292. [Q9U389-2]
DR EnsemblMetazoa; R102.5b.1; R102.5b.1; WBGene00011292. [Q9U389-1]
DR GeneID; 177962; -.
DR KEGG; cel:CELE_R102.5; -.
DR UCSC; R102.5a.1; c. elegans.
DR CTD; 177962; -.
DR WormBase; R102.5a; CE35601; WBGene00011292; allo-1. [Q9U389-2]
DR WormBase; R102.5b; CE35602; WBGene00011292; allo-1. [Q9U389-1]
DR eggNOG; ENOG502TG4U; Eukaryota.
DR HOGENOM; CLU_061875_0_0_1; -.
DR InParanoid; Q9U389; -.
DR OMA; WSIQQSI; -.
DR OrthoDB; 1233069at2759; -.
DR PhylomeDB; Q9U389; -.
DR PRO; PR:Q9U389; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00011292; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:WormBase.
DR GO; GO:0030017; C:sarcomere; HDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..402
FT /note="Allophagy receptor allo-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000444320"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..347
FT /evidence="ECO:0000255"
FT MOTIF 13..16
FT /note="LIR"
FT /evidence="ECO:0000305"
FT COMPBIAS 33..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphothreonine; by IKKE"
FT /evidence="ECO:0000269|PubMed:29255173"
FT VAR_SEQ 355..388
FT /note="LAGPTGEHPHARFERAGDQQSEAEMSSTWSAGRL -> DQQESTRMLASNEQ
FT VINSLKQKCRQLGVLEDFSS (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_059584"
FT VAR_SEQ 389..402
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_059585"
FT MUTAGEN 13..16
FT /note="FEII->AEIA: Impairs binding to lgg-1. Does not
FT affect accumulation on paternal organelles in embryos, but
FT lgg-1 is not recruited and paternal mitochondria are
FT retained and are not cleared."
FT /evidence="ECO:0000269|PubMed:29255173"
FT MUTAGEN 74
FT /note="T->A: Reduces phosphorylation. Localizes to paternal
FT organelles in 1-cell stage embryos, but does not completely
FT rescue the defects and clearance of paternal organelles in
FT the allo-1 tm4756 mutant."
FT /evidence="ECO:0000269|PubMed:29255173"
FT MUTAGEN 74
FT /note="T->D: Does not rescue the defects in paternal
FT mitochondrial clearance in the ikke-1 gk1264 mutant."
FT /evidence="ECO:0000269|PubMed:29255173"
SQ SEQUENCE 402 AA; 45158 MW; 67EFDB3EDA940ABB CRC64;
MNDPLDSLSN DEFEIIETFD PETEDREDQW SIQQSIRIEP ISIQMPNTLQ SQRAPSPVGS
KAPESLKDED PDRTPEASIV ETPLLTETLK EDRTPMSTPL ASLVNSSQSP EFTLQNMSIV
SESECSNNSS LVNVADVEST EIALRTSLLL VSELKSQLQA AKMSESTLLK SNSNHEIEEN
KKLSEKMEVM KNEFELKMQE SAASVEKVIQ EKDSAIEQLK VQLAQSQQVA ELWKQGAEKN
SNAQYSDSKT TIDRLLEENS KLRNLVDEEV ARRLEESERR KLAEDQLKHA RGGSVFDPPA
SFVASQLAER TTYSLNLEHE LITLRKELEE TKEALKKSVE ESSNKDEIVS ALHELAGPTG
EHPHARFERA GDQQSEAEMS STWSAGRLLE LSRQIVHFIS HQ
