ID   EMC4_PONAB              Reviewed;         183 AA.
AC   Q5RC35;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=ER membrane protein complex subunit 4;
DE   AltName: Full=Transmembrane protein 85;
GN   Name=EMC4; Synonyms=TMEM85;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-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}. 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}.
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DR   EMBL; CR858446; CAH90675.1; -; mRNA.
DR   RefSeq; NP_001125367.1; NM_001131895.1.
DR   AlphaFoldDB; Q5RC35; -.
DR   SMR; Q5RC35; -.
DR   STRING; 9601.ENSPPYP00000007150; -.
DR   Ensembl; ENSPPYT00000007446; ENSPPYP00000007150; ENSPPYG00000006310.
DR   GeneID; 100172270; -.
DR   KEGG; pon:100172270; -.
DR   CTD; 51234; -.
DR   eggNOG; KOG3318; Eukaryota.
DR   GeneTree; ENSGT00390000006970; -.
DR   HOGENOM; CLU_098404_0_1_1; -.
DR   InParanoid; Q5RC35; -.
DR   OMA; QQTFKVI; -.
DR   OrthoDB; 1623701at2759; -.
DR   TreeFam; TF313750; -.
DR   Proteomes; UP000001595; Chromosome 15.
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:0032977; F:membrane insertase activity; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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   Acetylation; Apoptosis; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   CHAIN           2..183
FT                   /note="ER membrane protein complex subunit 4"
FT                   /id="PRO_0000251916"
FT   TOPO_DOM        2..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        88..98
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        99..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        121..127
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        149..183
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   REGION          20..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
SQ   SEQUENCE   183 AA;  20087 MW;  96888D46FF22DEDE CRC64;
     MTAQGGLVAN RGRRFKWAIE LSGPGGGSRG RSDRGSGQGD SLYPVGYLDK QVPDTSVQET
     DRILVEKRCW DIALGPLKQI PMNLFIMYMA GNTISIFPTM MVCMMAWRPI QALMAISATF
     KMLESSSQKF LQGLVYLIGN LMGLALAVYK CQSMGLLPTH ASDWLAFIEP PERMEFSGGG
     LLL