EMC1_SCHPO
ID EMC1_SCHPO Reviewed; 885 AA.
AC O13981; Q9USE4;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ER membrane protein complex subunit 1;
DE Flags: Precursor;
GN Name=emc1; ORFNames=SPAC25H1.07;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 265-445, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
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).
CC -!- FUNCTION: Part of the endoplasmic reticulum membrane protein complex
CC (EMC) that enables the energy-independent insertion into endoplasmic
CC reticulum membranes of newly synthesized membrane proteins.
CC Preferentially accommodates proteins with transmembrane domains that
CC are weakly hydrophobic or contain destabilizing features such as
CC charged and aromatic residues. Involved in the cotranslational
CC insertion of multi-pass membrane proteins in which stop-transfer
CC membrane-anchor sequences become ER membrane spanning helices (By
CC similarity). It is also required for the post-translational insertion
CC of tail-anchored/TA proteins in endoplasmic reticulum membranes. By
CC mediating the proper cotranslational insertion of N-terminal
CC transmembrane domains in an N-exo topology, with translocated N-
CC terminus in the lumen of the ER, controls the topology of multi-pass
CC membrane proteins (By similarity). {ECO:0000250|UniProtKB:P25574,
CC ECO:0000250|UniProtKB:Q8N766}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:P25574}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P25574}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P25574}.
CC -!- SIMILARITY: Belongs to the EMC1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB11603.1; -; Genomic_DNA.
DR EMBL; AB027822; BAA87126.1; -; Genomic_DNA.
DR PIR; T38387; T38387.
DR RefSeq; NP_593811.1; NM_001019240.2.
DR AlphaFoldDB; O13981; -.
DR SMR; O13981; -.
DR BioGRID; 279169; 89.
DR STRING; 4896.SPAC25H1.07.1; -.
DR MaxQB; O13981; -.
DR PaxDb; O13981; -.
DR PRIDE; O13981; -.
DR DNASU; 2542716; -.
DR EnsemblFungi; SPAC25H1.07.1; SPAC25H1.07.1:pep; SPAC25H1.07.
DR GeneID; 2542716; -.
DR KEGG; spo:SPAC25H1.07; -.
DR PomBase; SPAC25H1.07; emc1.
DR VEuPathDB; FungiDB:SPAC25H1.07; -.
DR eggNOG; KOG2103; Eukaryota.
DR HOGENOM; CLU_325206_0_0_1; -.
DR InParanoid; O13981; -.
DR OMA; SIFLPCY; -.
DR PhylomeDB; O13981; -.
DR PRO; PR:O13981; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0072546; C:EMC complex; ISO:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0045048; P:protein insertion into ER membrane; IC:PomBase.
DR InterPro; IPR026895; EMC1.
DR InterPro; IPR011678; EMC1_C.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR PANTHER; PTHR21573; PTHR21573; 1.
DR Pfam; PF07774; EMC1_C; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..885
FT /note="ER membrane protein complex subunit 1"
FT /id="PRO_0000350761"
FT TOPO_DOM 23..855
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..874
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 875..885
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 885 AA; 100925 MW; F9BCED182502F6BA CRC64;
MLRPLWPLFL TALFLNIYRA ASVLIDEAGK NDFEISLLGK VNDLVYDTKN EYLYAVSQKG
LLAKLNASNG DVIWRQSIAP ETSQLNYNPV TNFIITVDKD YLYIWNSKNG ILDRKIELAD
GKGKLFEVNK GFVYLNPHTR KFIELDLQAS FSISIERDLQ LDAISFLTYA EKNYVLFKRD
GQFVLQALDH NYAVYGPETV LNVPENAQLL VTEKDVIIYS SNGVIYGIHV SMADISQLLI
DEYKTFEWSS IPGKRHGYSI TVDSQSTPVT YLFVIIDSEF VLIDEYIHED TEALGYIHME
DNQTFSRVFA VANQIKFAPA TVITIPNQLS RPVFRLFTFA EGEISAIVIL DDGTFFSFSN
TELVWKREEA LAYAINPSIL PTTLLTSYQK SIQDEENSSV SFLNRWYRHF NQLIDFLKHP
HGFTSSSVLD DAFTTKIIIP TSTGSIFCLS SDPKQVHRIL WRYDFNINPE SVESWLLDIS
DEDPKFAFVH QWNDAFSFYI LNASDGSVIS QKSRDFKADE FYYVDNISKN LPNQIFAVKD
YKVLPLTGDN SIFEKISQEA NSIFVYTSET KVEGFSISAD LTMDVQWSYN LAEGEIVIAS
IRRNPHEIVA SFGRVLQNRE VMYKYLNPNL FALFSKCKND LVVYVMDSVT GSIVYQNKHQ
GIILFDKVYG VFSENWLVYS YQSDVPNLST KIISVELFEG SHSNEKIDSN EIYSRHNDYR
PYAFTKAYIF DREITTLGVT NTPQGITSRD VLLGLSSNQV AMIPQALLSP MRPVLRPNEK
ANDASFIPYE PIIPLNDDMV LSYNKRVYGV SQITSGITNF ESTTLVLSTG LDVFFTRTAP
SMPYDMLSSH FDKKQLMLTT FGILLAVLLT KPLVKKKQLN TKWYN
