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Protein sepa-1 (Suppressor of ectopic P granules in autophagy)

 SEPA1_CAEEL             Reviewed;         702 AA.
G5EC37;
07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
31-JAN-2018, entry version 46.
RecName: Full=Protein sepa-1 {ECO:0000305};
AltName: Full=Suppressor of ectopic P granules in autophagy {ECO:0000312|WormBase:M01E5.6};
Name=sepa-1 {ECO:0000303|PubMed:19167332,
ECO:0000312|WormBase:M01E5.6};
ORFNames=M01E5.6 {ECO:0000312|WormBase:M01E5.6};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000305}
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=19377305; DOI=10.4161/auto.5.5.8624;
Tian E., Wang F., Han J., Zhang H.;
"epg-1 functions in autophagy-regulated processes and may encode a
highly divergent Atg13 homolog in C. elegans.";
Autophagy 5:608-615(2009).
[3] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19372764;
Zhao Y., Tian E., Zhang H.;
"Selective autophagic degradation of maternally-loaded germline P
granule components in somatic cells during C. elegans embryogenesis.";
Autophagy 5:717-719(2009).
[4] {ECO:0000305}
FUNCTION, SUBUNIT, INTERACTION WITH LGG-1 AND PGL-3, SUBCELLULAR
LOCATION, DEVELOPMENTAL STAGE, PROTEOLYTIC DEGRADATION, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF CYS-255 AND GLU-275.
PubMed=19167332; DOI=10.1016/j.cell.2008.12.022;
Zhang Y., Yan L., Zhou Z., Yang P., Tian E., Zhang K., Zhao Y., Li Z.,
Song B., Han J., Miao L., Zhang H.;
"SEPA-1 mediates the specific recognition and degradation of P granule
components by autophagy in C. elegans.";
Cell 136:308-321(2009).
[5] {ECO:0000305}
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=21802374; DOI=10.1016/j.devcel.2011.06.024;
Lu Q., Yang P., Huang X., Hu W., Guo B., Wu F., Lin L., Kovacs A.L.,
Yu L., Zhang H.;
"The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates
progression of omegasomes to autophagosomes.";
Dev. Cell 21:343-357(2011).
[6] {ECO:0000305}
FUNCTION, INTERACTION WITH EPG-2 AND PGL-3, SUBCELLULAR LOCATION,
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=24140420; DOI=10.1016/j.molcel.2013.09.014;
Li S., Yang P., Tian E., Zhang H.;
"Arginine methylation modulates autophagic degradation of PGL granules
in C. elegans.";
Mol. Cell 52:421-433(2013).
[7]
FUNCTION, AND INTERACTION WITH EPG-2.
PubMed=28806108; DOI=10.1080/15548627.2017.1339843;
Zhang G., Lin L., Qi D., Zhang H.;
"The composition of a protein aggregate modulates the specificity and
efficiency of its autophagic degradation.";
Autophagy 13:1487-1495(2017).
-!- FUNCTION: Adapter protein that connects P-granules in somatic
cells with the autophagic machinery (PubMed:19377305,
PubMed:19372764, PubMed:19167332, PubMed:24140420). Association
with other adapters such as epg-2 and P-granule components such as
pgl-3 is required for the accumulation and degradation of P-
granules by autophagy in somatic cells (PubMed:19372764,
PubMed:19167332, PubMed:24140420, PubMed:28806108). This ensures
exclusive localization of the P-granules in germ cells
(PubMed:19372764, PubMed:19167332, PubMed:24140420,
PubMed:28806108). {ECO:0000269|PubMed:19167332,
ECO:0000269|PubMed:19372764, ECO:0000269|PubMed:19377305,
ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:28806108}.
-!- SUBUNIT: Self-associates (PubMed:19167332). Interacts with lgg-1
(PubMed:19167332). Interacts with pgl-3; interaction is enhanced
in the presence of RNA (PubMed:19167332, PubMed:24140420).
Interacts with epg-2; may be modulated by prmt-1 (PubMed:24140420,
PubMed:28806108). {ECO:0000269|PubMed:19167332,
ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:28806108}.
-!- INTERACTION:
Q09490:lgg-1; NbExp=3; IntAct=EBI-2256317, EBI-325374;
G5EBV6:pgl-3; NbExp=5; IntAct=EBI-2256317, EBI-328338;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00311}. Cytoplasm {ECO:0000269|PubMed:19167332,
ECO:0000269|PubMed:19372764, ECO:0000269|PubMed:21802374,
ECO:0000269|PubMed:24140420}. Cytoplasmic granule
{ECO:0000305|PubMed:19167332}. Note=Diffuse cytoplasmic
localization, but also localized to cytoplasmic aggregates
throughout development (PubMed:19167332, PubMed:21802374). Co-
localizes with epg-2 and lgg-1 in cytoplasmic aggregates
(PubMed:19167332, PubMed:24140420). {ECO:0000269|PubMed:19167332,
ECO:0000269|PubMed:21802374, ECO:0000269|PubMed:24140420}.
-!- DEVELOPMENTAL STAGE: First expressed in 16-cell stage embryos
(PubMed:19167332). Temporal expression during embryogenesis with
high expression as embryos develop into 100-stage embryos, but
with low expression in most cells at the comma stage and almost
diminished expression at the 2-fold stage of embryogenesis
(PubMed:19377305, PubMed:19167332, PubMed:21802374,
PubMed:24140420). Expressed in the head, tail and intestine,
especially in the anterior and posterior intestinal cells, of
larvae (PubMed:19167332). {ECO:0000269|PubMed:19167332,
ECO:0000269|PubMed:19377305, ECO:0000269|PubMed:21802374,
ECO:0000269|PubMed:24140420}.
-!- PTM: Degraded by autophagy. {ECO:0000269|PubMed:19167332}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in the
accumulation of cytoplasmic aggregates containing the P-granule
component pgl-3 (PubMed:24140420). RNAi-mediated knockdown results
in the disrupted formation of P-granules in an atg-18 autophagy
mutant background (PubMed:19167332). {ECO:0000269|PubMed:19167332,
ECO:0000269|PubMed:24140420}.
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EMBL; BX284601; CAB07643.1; -; Genomic_DNA.
PIR; T23651; T23651.
RefSeq; NP_493339.1; NM_060938.3.
UniGene; Cel.18438; -.
ProteinModelPortal; G5EC37; -.
SMR; G5EC37; -.
ELM; G5EC37; -.
IntAct; G5EC37; 2.
STRING; 6239.M01E5.6; -.
EPD; G5EC37; -.
PaxDb; G5EC37; -.
PeptideAtlas; G5EC37; -.
EnsemblMetazoa; M01E5.6; M01E5.6; WBGene00010808.
GeneID; 173196; -.
KEGG; cel:CELE_M01E5.6; -.
CTD; 173196; -.
WormBase; M01E5.6; CE12286; WBGene00010808; sepa-1.
eggNOG; KOG1778; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00390000017901; -.
InParanoid; G5EC37; -.
KO; K22261; -.
OMA; NTSKEWI; -.
OrthoDB; EOG091G13OH; -.
PhylomeDB; G5EC37; -.
PRO; PR:G5EC37; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00010808; -.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0030674; F:protein binding, bridging; IDA:WormBase.
GO; GO:0043621; F:protein self-association; IPI:WormBase.
GO; GO:0003712; F:transcription cofactor activity; IEA:InterPro.
GO; GO:0006914; P:autophagy; IMP:WormBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
InterPro; IPR003101; KIX_dom.
InterPro; IPR036529; KIX_dom_sf.
Pfam; PF02172; KIX; 1.
SUPFAM; SSF47040; SSF47040; 1.
PROSITE; PS50952; KIX; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Cytoplasm; Nucleus;
Reference proteome.
CHAIN 1 702 Protein sepa-1. {ECO:0000305}.
/FTId=PRO_0000440173.
DOMAIN 597 674 KIX. {ECO:0000255|PROSITE-
ProRule:PRU00311}.
REGION 39 160 Required for self-association and
interaction with pgl-3.
{ECO:0000269|PubMed:19167332}.
REGION 289 575 Required for interaction with lgg-1.
{ECO:0000269|PubMed:19167332}.
COILED 508 543 {ECO:0000255}.
MUTAGEN 255 255 C->Y: In bp400; mutant protein does not
form aggregates, but cytoplasmic
localization is diffuse throughout
embryogenesis.
{ECO:0000269|PubMed:19167332}.
MUTAGEN 275 275 E->K: In bp401; temperature sensitive
with the mutant protein forming
"speckles" at 15 degrees Celsius and
diffusely localized at 25 degrees
Celsius. {ECO:0000269|PubMed:19167332}.
SEQUENCE 702 AA; 80262 MW; 209253AF6164BB88 CRC64;
MTPLSALTSN PAPSPPPKFA LGKCPATAIH VVSVLRPNRQ RFCYEKTDAG DLIPHKCLIC
QPILTEKHIS PYYAVYSDLL EDFVLFGYNT MTGKMEQFIY AFKTDCFVEV NRPEIKYNPA
FLVKGNVVVA LNGPEGELVV IERDCRGLLS KESTSYGQFR TLPTAALRTL TLQDLERDRW
DRAANSDEVK ISSGNESFDR LYAEYQKNLP RFQVRQCLHL NKEFLCVYSK TSGDYTRLEY
IDETGDFQKI SCTLCTCEVT ESNLIPLYVE RNASELVIHV HNTENNQIEQ YIYDVRTFGF
VQVKRNLVYD PKKITSGLNL FMAENIDNRK VYMIMRGRDG RLQKETSGSG GFEKMQPVAV
KTFQVQWVEM KTEFEKKKAS TERVEPQHPV QTEGEDIMET VLAMVESFNC DLRKELGLTQ
DQEIPRKAPR VESAETEENI VKNLEKLQIA KDPEEPTTAA SEGGNTYGYQ ELDDTMSEGL
LEKEAESKHQ DANEPEPVKN VTYEPDVAAM DKKKKRRELK SRLNKINAQI DELEKRRMER
AGKKQVVSSS VPSEEAAQVE APASPALAEN TNQISNEETP KIDIFEGYNG SFLFGTNTSK
EWIVEDIRNH MVGKLLKAFW PRIQNVEEMN GELFKKLIAN ARKCETEILE ASNDRDEYYR
LMQLTVDQIL KKTLKKDQRA TEHNHQQPTQ SSDELAKNHE KN


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