EMC3_DICDI
ID EMC3_DICDI Reviewed; 314 AA.
AC Q54YN3;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=ER membrane protein complex subunit 3;
DE AltName: Full=Transmembrane protein 111;
GN Name=emc3; Synonyms=tmem111; ORFNames=DDB_G0278153;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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. It is
CC also required for the post-translational insertion of tail-anchored/TA
CC proteins in endoplasmic reticulum membranes. By mediating the proper
CC cotranslational insertion of N-terminal transmembrane domains in an N-
CC exo topology, with translocated N-terminus in the lumen of the ER,
CC controls the topology of multi-pass membrane proteins. By regulating
CC the insertion of various proteins in membranes, it is indirectly
CC involved in many cellular processes. {ECO:0000250|UniProtKB:Q9P0I2}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q9P0I2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9P0I2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9P0I2}.
CC -!- SIMILARITY: Belongs to the EMC3 family. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68249.1; -; Genomic_DNA.
DR RefSeq; XP_642169.1; XM_637077.1.
DR AlphaFoldDB; Q54YN3; -.
DR SMR; Q54YN3; -.
DR STRING; 44689.DDB0266861; -.
DR PaxDb; Q54YN3; -.
DR EnsemblProtists; EAL68249; EAL68249; DDB_G0278153.
DR GeneID; 8621376; -.
DR KEGG; ddi:DDB_G0278153; -.
DR dictyBase; DDB_G0278153; tmem111.
DR eggNOG; KOG3188; Eukaryota.
DR HOGENOM; CLU_060791_1_0_1; -.
DR InParanoid; Q54YN3; -.
DR OMA; WYFLTLF; -.
DR PhylomeDB; Q54YN3; -.
DR PRO; PR:Q54YN3; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0072546; C:EMC complex; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; ISS:UniProtKB.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR InterPro; IPR008568; EMC3.
DR InterPro; IPR002809; EMC3/TMCO1.
DR PANTHER; PTHR13116; PTHR13116; 1.
DR Pfam; PF01956; EMC3_TMCO1; 1.
DR SMART; SM01415; DUF106; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..314
FT /note="ER membrane protein complex subunit 3"
FT /id="PRO_0000350554"
FT TOPO_DOM 1..14
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TRANSMEM 15..38
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TOPO_DOM 39..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TRANSMEM 131..146
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TOPO_DOM 147..185
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TRANSMEM 186..204
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT TOPO_DOM 205..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT REGION 272..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 314 AA; 35794 MW; 5AA58BEE3D3D2661 CRC64;
MTESPIVLDV EIRNWVVIPI LIVLFIVSAL KLNISRIMQI NSGKPQDVEK TMQMQTINRV
RRLVSFYNRI PQKSFFIRKA YLCGTTGSKT NKGILSSIAP TQEDSNPMNM MFANSMFTDP
SGITDMLKGN IMHLIPQVTM MSWVNHFFSG FVACKLPFFP LTIRFKTFLQ RGIEMGSLDV
SYVSSLSWYF LCWFGSEGIN AILLGENMVS ADSQLLQSSI EPGPPTQQTP IHKIYASEKE
NIEMIRYDSL MTNIEDRFLD NIKKKTSFDF NQINKNNNNN NNNTSNIKPK PIKSNLSNSK
QSKRITYQKP SSLI
