ID   EMC4_SALSA              Reviewed;         188 AA.
AC   B5XB24; B5X7E9;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=ER membrane protein complex subunit 4;
DE   AltName: Full=Transmembrane protein 85;
GN   Name=emc4; Synonyms=tmem85;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thyroid;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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 like the G
CC       protein-coupled receptors. By regulating the insertion of various
CC       proteins in membranes, it is indirectly involved in many cellular
CC       processes. {ECO:0000250|UniProtKB:Q5J8M3}.
CC   -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC       {ECO:0000250|UniProtKB:Q5J8M3}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q5J8M3}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q5J8M3}. Note=Could also be a single-pass
CC       transmembrane protein with cytosolic N-terminus and lumenal C-terminus.
CC       {ECO:0000250|UniProtKB:Q5J8M3}.
CC   -!- SIMILARITY: Belongs to the EMC4 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; BT046968; ACI66769.1; -; mRNA.
DR   EMBL; BT048243; ACI68044.1; -; mRNA.
DR   RefSeq; NP_001134568.1; NM_001141096.1.
DR   AlphaFoldDB; B5XB24; -.
DR   SMR; B5XB24; -.
DR   STRING; 8030.ENSSSAP00000093077; -.
DR   GeneID; 100196067; -.
DR   KEGG; sasa:100196067; -.
DR   OrthoDB; 1623701at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa07.
DR   Bgee; ENSSSAG00000071911; Expressed in testis and 16 other tissues.
DR   GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of 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; IPR009445; TMEM85/Emc4.
DR   PANTHER; PTHR19315; PTHR19315; 1.
DR   Pfam; PF06417; DUF1077; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..188
FT                   /note="ER membrane protein complex subunit 4"
FT                   /id="PRO_0000375880"
FT   TOPO_DOM        1..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        93..103
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        104..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        126..132
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        154..188
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   CONFLICT        173
FT                   /note="I -> V (in Ref. 1; ACI66769)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   188 AA;  20582 MW;  EA1DEC9410B9FE0F CRC64;
     MASPGGQGGG AVSTRGAGAR RMKWALELSL GNARGRGDRQ SNQGDVMYPI GYSDKPVPDT
     SIQETDKNLV EKRCWDVALG PLKQIPMNLF IMYMSGNTIS IFPIMMVCMM AWRPIQALMS
     MSATFKLLEN SNQQWLQGLV YSVGNLLGSA LAIYKCQSMG LLPTHSSDWL AFIEPPQRME
     IMGGGMVL