EMC6_DICDI
ID EMC6_DICDI Reviewed; 123 AA.
AC Q1ZXH4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=ER membrane protein complex subunit 6;
DE AltName: Full=Transmembrane protein 93;
GN Name=emc6; Synonyms=tmem93; ORFNames=DDB_G0280399;
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:Q9BV81}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q9BV81}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9BV81}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9BV81}.
CC -!- SIMILARITY: Belongs to the EMC6 family. {ECO:0000305}.
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DR EMBL; AAFI02000035; EAS66878.1; -; Genomic_DNA.
DR RefSeq; XP_001134562.1; XM_001134562.1.
DR AlphaFoldDB; Q1ZXH4; -.
DR SMR; Q1ZXH4; -.
DR STRING; 44689.DDB0231544; -.
DR PaxDb; Q1ZXH4; -.
DR EnsemblProtists; EAS66878; EAS66878; DDB_G0280399.
DR GeneID; 8622457; -.
DR KEGG; ddi:DDB_G0280399; -.
DR dictyBase; DDB_G0280399; tmem93.
DR eggNOG; KOG4455; Eukaryota.
DR HOGENOM; CLU_110781_3_0_1; -.
DR InParanoid; Q1ZXH4; -.
DR OMA; FIYGMVH; -.
DR PhylomeDB; Q1ZXH4; -.
DR PRO; PR:Q1ZXH4; -.
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:0000045; P:autophagosome assembly; IBA:GO_Central.
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; IPR008504; Emc6.
DR InterPro; IPR029008; EMC6-like.
DR PANTHER; PTHR20994; PTHR20994; 1.
DR Pfam; PF07019; EMC6; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..123
FT /note="ER membrane protein complex subunit 6"
FT /id="PRO_0000327388"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TRANSMEM 42..57
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TOPO_DOM 58..63
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TOPO_DOM 85..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TRANSMEM 103..119
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT TOPO_DOM 120..123
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BV81"
SQ SEQUENCE 123 AA; 14433 MW; 086DC3E2574B0BC2 CRC64;
MLHPQQMQEQ QQQQQEAQAA SIIPEHYEME YIQRNNKTVS FCQIPISILG GAIAGVIGFS
GVYGFLFYFF IYITFCSLFT LKENKNLHLY FPNPRSIWFD SIGAGLMPYI LFWTFLYNII
HIY