EMR1_SCHPO
ID EMR1_SCHPO Reviewed; 61 AA.
AC Q4ZGE1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=ERMES regulator 1 {ECO:0000303|PubMed:33483504};
GN Name=emr1 {ECO:0000303|PubMed:33483504};
GN ORFNames=SPAC8C9.19 {ECO:0000312|PomBase:SPAC8C9.19};
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, INTERACTION WITH THE ERMES COMPLEX; MDM12 AND MDM34, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND TOPOLOGY.
RX PubMed=33483504; DOI=10.1038/s41467-020-20866-x;
RA Rasul F., Zheng F., Dong F., He J., Liu L., Liu W., Cheema J.Y., Wei W.,
RA Fu C.;
RT "Emr1 regulates the number of foci of the endoplasmic reticulum-
RT mitochondria encounter structure complex.";
RL Nat. Commun. 12:521-521(2021).
CC -!- FUNCTION: Mediates the formation of endoplasmic reticulum (ER)-
CC mitochondria encounter structure (ERMES) foci, thereby contributing to
CC the formation of ER-mitochondrial contact sites.
CC {ECO:0000269|PubMed:33483504}.
CC -!- SUBUNIT: Interacts with the ER-mitochondria encounter structure (ERMES)
CC complex (PubMed:33483504). Interacts with mdm12 (PubMed:33483504).
CC Interacts with mdm34 (PubMed:33483504). {ECO:0000269|PubMed:33483504}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:33483504}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:33483504}.
CC -!- DISRUPTION PHENOTYPE: Decreases the number of ER-mitochondria encounter
CC structure (ERMES) foci in cells (PubMed:33483504). Abnormal
CC mitochondrial organization within cells, manifesting as fragmented or
CC aggregated mitochondria, spherical mitochondria, or absence of
CC mitochondria (PubMed:33483504). Decreases the level of
CC phosphatidylethanolamine (PE) in cells (PubMed:33483504). Decreases
CC growth on glucose (fermentable) and glycerol (non-fermentable) carbon
CC sources (PubMed:33483504). Simultaneous disruption of ept1, psd2 or
CC psd3 leads to decreased growth on glucose carbon source
CC (PubMed:33483504). {ECO:0000269|PubMed:33483504}.
CC -!- SIMILARITY: Belongs to the EMR1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAI94397.2; -; Genomic_DNA.
DR RefSeq; XP_001713088.2; XM_001713036.2.
DR AlphaFoldDB; Q4ZGE1; -.
DR SMR; Q4ZGE1; -.
DR BioGRID; 858058; 2.
DR MaxQB; Q4ZGE1; -.
DR PaxDb; Q4ZGE1; -.
DR EnsemblFungi; SPAC8C9.19.1; SPAC8C9.19.1:pep; SPAC8C9.19.
DR PomBase; SPAC8C9.19; -.
DR VEuPathDB; FungiDB:SPAC8C9.19; -.
DR eggNOG; ENOG502SE6C; Eukaryota.
DR HOGENOM; CLU_196188_0_0_1; -.
DR InParanoid; Q4ZGE1; -.
DR OMA; FIEARTD; -.
DR PRO; PR:Q4ZGE1; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; IDA:PomBase.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:PomBase.
DR GO; GO:0120010; P:intermembrane phospholipid transfer; IMP:PomBase.
DR GO; GO:0007008; P:outer mitochondrial membrane organization; IMP:PomBase.
DR InterPro; IPR035195; Emr1.
DR Pfam; PF17237; DUF5310; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..61
FT /note="ERMES regulator 1"
FT /id="PRO_0000343165"
FT TOPO_DOM 1..20
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:33483504"
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:33483504"
SQ SEQUENCE 61 AA; 7102 MW; D4762124357EE32D CRC64;
MLPNLRRIFA SFRTEEEERS YSRKAFFHLI GYITCSVLFS WLVRKKVISS PVVSSPIHAL
S
