SORF1_CAEEL
ID SORF1_CAEEL Reviewed; 239 AA.
AC Q23533;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Suppressor of organelle fusion 1 {ECO:0000303|PubMed:26783301};
GN Name=sorf-1 {ECO:0000303|PubMed:26783301, ECO:0000312|WormBase:ZK563.5};
GN ORFNames=ZK563.5 {ECO:0000312|WormBase:ZK563.5};
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, INTERACTION WITH SORF-2 AND BEC-1, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=26783301; DOI=10.1083/jcb.201506081;
RA Liu K., Jian Y., Sun X., Yang C., Gao Z., Zhang Z., Liu X., Li Y., Xu J.,
RA Jing Y., Mitani S., He S., Yang C.;
RT "Negative regulation of phosphatidylinositol 3-phosphate levels in early-
RT to-late endosome conversion.";
RL J. Cell Biol. 212:181-198(2016).
RN [3]
RP ERRATUM OF PUBMED:26783301.
RX PubMed=26975852; DOI=10.1083/jcb.20150608103012016c;
RA Liu K., Jian Y., Sun X., Yang C., Gao Z., Zhang Z., Liu X., Li Y., Xu J.,
RA Jing Y., Mitani S., He S., Yang C.;
RT "Correction: Negative regulation of phosphatidylinositol 3-phosphate levels
RT in early-to-late endosome conversion.";
RL J. Cell Biol. 212:739-739(2016).
CC -!- FUNCTION: Together with sorf-2 negatively regulates the levels of
CC phosphatidylinositol 3-phosphate (PtdIns3P) to enable the conversion of
CC early endosomes to late endosomes. Binds to sorf-2 and the sorf-1-sorf-
CC 2 complex likely acts through bec-1, a non-catalytic subunit of
CC phosphatidylinositol 3-kinase (PI3K), to suppress PI3K activity,
CC thereby negatively regulating endosomal PtdIns3P levels.
CC {ECO:0000269|PubMed:26783301}.
CC -!- SUBUNIT: Interacts with sorf-2; the interaction is direct. Interacts
CC with bec-1. {ECO:0000269|PubMed:26783301}.
CC -!- INTERACTION:
CC Q23533; Q22592: bec-1; NbExp=3; IntAct=EBI-13941886, EBI-2413500;
CC Q23533; Q10122: sorf-2; NbExp=2; IntAct=EBI-13941886, EBI-13941960;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000305|PubMed:26783301}.
CC Late endosome {ECO:0000305|PubMed:26783301}. Cytoplasm
CC {ECO:0000269|PubMed:26783301}.
CC -!- DISRUPTION PHENOTYPE: Coelomocytes contain larger early and late
CC endosomes enriched with PtdIns3P. Delayed conversion of early endosomes
CC to late endosomes with early endosomes retaining PtdInsP3 for a longer
CC duration of time which may possibly be due to a delay in either the
CC turnover or transport of PtdIns3P out of the endosome. This leads to
CC continuous fusion of early endosomes which continues until rab-5 is
CC displaced and rab-7 is recruited. Double knockout with sorf-2 results
CC in a similar phenotype as the individual single sorf-1 knockout. Double
CC knockout with bec-1 results in smaller endosomes and an irregular
CC distribution pattern of PtdIns3P in the cytoplasm. Double knockout with
CC vps-11, vps-18 or vps-39, subunits of the CORVET/HOPS complex, results
CC in larger endosomes and larger lysosomes and thus suppresses the
CC endosome/lysosome fusion defects in coelomocytes of the individual vps-
CC 11, vps-18 and vps-39 single mutants. Likewise, RNAi-mediated knockdown
CC in a vps-41 mutant background (a subunit of the CORVET/HOPS complex)
CC also suppresses the endosome/lysosome fusion defects in the vps-41
CC single mutant. However, double knockout with the CORVET/HOPS complex
CC subunits vps-16 or vps-33.1, does not suppress the endosome/lysosome
CC fusion defects in coelomocytes of the individual vps-16 and vps-33.1
CC single mutants. Double knockout with proteins involved in rab-5 to rab-
CC 7 switching in early to late endosome conversion such as rab-7, sand-1
CC and tbc-2 results in enlarged vacuoles, delayed endosomal cargo
CC transport and persistent PtdIns3P in early endosomes in coelomocytes.
CC {ECO:0000269|PubMed:26783301}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR91 family. {ECO:0000305}.
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DR EMBL; BX284606; CCD63045.1; -; Genomic_DNA.
DR PIR; T27917; T27917.
DR RefSeq; NP_508584.3; NM_076183.6.
DR AlphaFoldDB; Q23533; -.
DR ComplexPortal; CPX-1059; Sorf-1-Sorf-2 complex.
DR IntAct; Q23533; 2.
DR STRING; 6239.ZK563.5; -.
DR EPD; Q23533; -.
DR PaxDb; Q23533; -.
DR EnsemblMetazoa; ZK563.5.1; ZK563.5.1; WBGene00022769.
DR EnsemblMetazoa; ZK563.5.2; ZK563.5.2; WBGene00022769.
DR GeneID; 180626; -.
DR KEGG; cel:CELE_ZK563.5; -.
DR UCSC; ZK563.5; c. elegans.
DR CTD; 180626; -.
DR WormBase; ZK563.5; CE35817; WBGene00022769; sorf-1.
DR eggNOG; KOG1333; Eukaryota.
DR GeneTree; ENSGT00390000001566; -.
DR HOGENOM; CLU_1002233_0_0_1; -.
DR InParanoid; Q23533; -.
DR OMA; TWIEIYY; -.
DR OrthoDB; 1118743at2759; -.
DR PhylomeDB; Q23533; -.
DR PRO; PR:Q23533; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00022769; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031905; C:early endosome lumen; IDA:ComplexPortal.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031906; C:late endosome lumen; IDA:ComplexPortal.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0035014; F:phosphatidylinositol 3-kinase regulator activity; ISS:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IDA:ComplexPortal.
DR GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; IDA:ComplexPortal.
DR GO; GO:0048284; P:organelle fusion; IGI:UniProtKB.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IMP:UniProtKB.
DR GO; GO:0051036; P:regulation of endosome size; IGI:UniProtKB.
DR GO; GO:0043551; P:regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR InterPro; IPR039724; WDR91.
DR PANTHER; PTHR13083; PTHR13083; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endosome; Reference proteome.
FT CHAIN 1..239
FT /note="Suppressor of organelle fusion 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000440674"
SQ SEQUENCE 239 AA; 27242 MW; 6B63890EF96DDCFC CRC64;
MSHVSNSTDE VVRNYLAAKS MVTSLKAFDQ ESSFAKEANY QVDRCIDEMT DAIDKHDVDT
LCAMWESWNA RVFHSLDTEG IKQAQCYEAS AYRLFLVRCV QKKNISKCNE FFRKMSSLTL
NNPQWADWFA FPYNHHAKDT EPFRKYFDKT WIEIYYVSLH NFLSTSLANV SPSVIGTIVE
GIARDPTGND HVDFDEDLID DFAVIAQCSA PVKRGHSKPS LRNLLKSLTS SKKPSPSTD
