EPR1_SCHPO
ID EPR1_SCHPO Reviewed; 380 AA.
AC O14213;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ER-phagy receptor 1 {ECO:0000303|Ref.5};
DE AltName: Full=Meiotically up-regulated gene 185 protein {ECO:0000303|PubMed:16303567};
GN Name=epr1 {ECO:0000303|Ref.5};
GN Synonyms=mug185 {ECO:0000303|PubMed:16303567}; ORFNames=SPAC6B12.08;
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 FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [5]
RP INTERACTION WITH ATG8; SCS2 AND SCS22, DISRUPTION PHENOTYPE, DOMAIN,
RP MUTAGENESIS OF PHE-352; VAL-355 AND PHE-362, FUNCTION, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX DOI=10.1016/j.molcel.2020.07.019;
RA Zhao D., Zou C.X., Liu X.M., Jiang Z.D., Yu Z.Q., Suo F., Du T.Y.,
RA Dong M.Q., He W., Du L.L.;
RT "A UPR-induced soluble ER-phagy receptor acts with VAPs to confer ER stress
RT resistance.";
RL Mol. Cell 79:1-15(2020).
CC -!- FUNCTION: Reticulophagy receptor required for autophagosomal
CC sequestration of endoplasmic reticulum (ER) membranes during ER stress
CC (Ref.5). Confers resistance to ER stress by promoting the autophagic
CC degradation of the ER (ER-phagy or reticulophagy) (Ref.5). Acts as a
CC bridging molecule to mediate the association between atg8 on the
CC autophagic membrane and the vesicle-associated membrane protein-
CC associated proteins (VAPs) scs2 and scs22 on the ER (Ref.5). May play a
CC role in meiosis (PubMed:16303567). {ECO:0000269|PubMed:16303567,
CC ECO:0000269|Ref.5}.
CC -!- SUBUNIT: Interacts (via the AIM motif) with atg8 (Ref.5). Interacts
CC (via the FFAT motif) with the vesicle-associated membrane protein-
CC associated protein (VAP) family proteins scs2 and scs22 (Ref.5).
CC {ECO:0000269|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16823372, ECO:0000269|Ref.5}. Preautophagosomal
CC structure {ECO:0000269|Ref.5}. Note=Accumulates at the
CC preautophagosomal structure when autophagy occurs. {ECO:0000269|Ref.5}.
CC -!- INDUCTION: Expression is up-regulated during ER stress by the unfolded
CC protein response (UPR) regulator ire1. {ECO:0000269|Ref.5}.
CC -!- DOMAIN: The atg8-interaction motif (AIM) is required for the
CC association with atg8. {ECO:0000269|Ref.5}.
CC -!- DOMAIN: The FFAT motif (AIM) is required for the association with the
CC vesicle-associated membrane protein-associated proteins (VAPs) scs2 and
CC scs22. {ECO:0000269|Ref.5}.
CC -!- DISRUPTION PHENOTYPE: Does not affect growth neither nitrogen
CC starvation-induced ER-phagy, but abolishes DTT-induced ER-phagy.
CC {ECO:0000269|Ref.5}.
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DR EMBL; CU329670; CAB11069.1; -; Genomic_DNA.
DR PIR; T39015; T39015.
DR RefSeq; NP_593763.1; NM_001019193.2.
DR AlphaFoldDB; O14213; -.
DR SMR; O14213; -.
DR BioGRID; 279379; 11.
DR IntAct; O14213; 1.
DR STRING; 4896.SPAC6B12.08.1; -.
DR iPTMnet; O14213; -.
DR MaxQB; O14213; -.
DR PaxDb; O14213; -.
DR PRIDE; O14213; -.
DR EnsemblFungi; SPAC6B12.08.1; SPAC6B12.08.1:pep; SPAC6B12.08.
DR GeneID; 2542938; -.
DR KEGG; spo:SPAC6B12.08; -.
DR PomBase; SPAC6B12.08; epr1.
DR VEuPathDB; FungiDB:SPAC6B12.08; -.
DR eggNOG; KOG0717; Eukaryota.
DR HOGENOM; CLU_062676_0_0_1; -.
DR InParanoid; O14213; -.
DR OMA; KWHEKDY; -.
DR PhylomeDB; O14213; -.
DR PRO; PR:O14213; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; EXP:PomBase.
DR GO; GO:0000407; C:phagophore assembly site; EXP:PomBase.
DR GO; GO:0140506; F:endoplasmic reticulum-autophagosome adaptor activity; IPI:PomBase.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044804; P:autophagy of nucleus; IMP:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0061709; P:reticulophagy; IMP:PomBase.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Meiosis; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..380
FT /note="ER-phagy receptor 1"
FT /id="PRO_0000278521"
FT DOMAIN 9..74
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT ZN_FING 270..294
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 307..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 352..355
FT /note="AIM"
FT /evidence="ECO:0000269|Ref.5"
FT MOTIF 361..367
FT /note="FFAT"
FT /evidence="ECO:0000269|Ref.5"
FT COMPBIAS 319..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 352
FT /note="F->A: Impairs the interaction with atg8."
FT /evidence="ECO:0000269|Ref.5"
FT MUTAGEN 355
FT /note="V->A: Impairs the interaction with atg8."
FT /evidence="ECO:0000269|Ref.5"
FT MUTAGEN 362
FT /note="F->A: Impairs the interaction with scs2 and scs22
FT and abolishes the ER localization."
FT /evidence="ECO:0000269|Ref.5"
SQ SEQUENCE 380 AA; 45131 MW; 290423100FD866CB CRC64;
MNNPFKDMDC YEILQVNHDS DLQEIKANYR KLALQYHPDR NPGIEDYNEI FSQINAAYNI
LSNDDKRKWH EKDYLRNQYS VQIEDVLQHL QTIEKIPFES TSAFVERLRQ DEKIAGSTDD
LPTLGDTTWL WTYAKPIYQK WLRFSTKKSF EWEALYNEEE ESDAATRRLM KRQNQRQIQY
CIQRYNELVR DLIGKACDLD PRRKNVVKLS DGERYNSLQE ASRKQSERDR RQYQETFKNQ
SIASWTIIDQ EETSSDDESL SKEIVNSNPI MCMVCNKNFR SQNQLENHEN SKKHKKNLRK
MNQEIKKHAK EAQKNAESNK QPEDAPSESP YSNKVSSSDF YTRSFEEIEK TFTFVEISDN
EFYTASEDGF LNEDDKLDQD
