ID   EMC4_DANRE              Reviewed;         189 AA.
AC   Q6P011;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=ER membrane protein complex subunit 4;
DE   AltName: Full=Transmembrane protein 85;
GN   Name=emc4; Synonyms=tmem85; ORFNames=zgc:77852;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SIMILARITY: Belongs to the EMC4 family. {ECO:0000305}.
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DR   EMBL; BC065880; AAH65880.1; -; mRNA.
DR   RefSeq; NP_991221.1; NM_205658.1.
DR   AlphaFoldDB; Q6P011; -.
DR   SMR; Q6P011; -.
DR   STRING; 7955.ENSDARP00000057377; -.
DR   PaxDb; Q6P011; -.
DR   GeneID; 402956; -.
DR   KEGG; dre:402956; -.
DR   CTD; 51234; -.
DR   ZFIN; ZDB-GENE-040426-1891; emc4.
DR   eggNOG; KOG3318; Eukaryota.
DR   InParanoid; Q6P011; -.
DR   OrthoDB; 1623701at2759; -.
DR   PhylomeDB; Q6P011; -.
DR   PRO; PR:Q6P011; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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.
DR   PIRSF; PIRSF017207; UCP017207_TM-p85; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..189
FT                   /note="ER membrane protein complex subunit 4"
FT                   /id="PRO_0000375879"
FT   TOPO_DOM        1..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        94..104
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        105..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        127..133
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        155..189
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          30..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   189 AA;  20692 MW;  76FBDA03B6030B8E CRC64;
     MTSSAGQGGG ALSTRGGAAT KRMKWAVELS LGNSRSRSDR QGKDGDVMYP VGYSDKPVPD
     TSVQEADRNL VEKRCWDVAL GPLKQIPMNL FIMYMSGNTI SIFPIMMVCM MAWRPIQALM
     SMSATFKLLE SSSQQWLQGL VYLIGNLLGS ALAIYKCQSM GLLPTHSSDW LAFIEPPQRL
     EIMGGGMVM