ID   EMC4_XENTR              Reviewed;         180 AA.
AC   Q6PBF7;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=ER membrane protein complex subunit 4;
DE   AltName: Full=Transmembrane protein 85;
GN   Name=emc4; Synonyms=tmem85;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2003) 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; BC059737; AAH59737.1; -; mRNA.
DR   RefSeq; NP_988876.1; NM_203545.1.
DR   RefSeq; XP_012813476.1; XM_012958022.2.
DR   RefSeq; XP_012813477.1; XM_012958023.2.
DR   AlphaFoldDB; Q6PBF7; -.
DR   SMR; Q6PBF7; -.
DR   STRING; 8364.ENSXETP00000037044; -.
DR   PaxDb; Q6PBF7; -.
DR   DNASU; 394471; -.
DR   Ensembl; ENSXETT00000037044; ENSXETP00000037044; ENSXETG00000017003.
DR   GeneID; 394471; -.
DR   KEGG; xtr:394471; -.
DR   CTD; 51234; -.
DR   Xenbase; XB-GENE-965547; emc4.
DR   eggNOG; KOG3318; Eukaryota.
DR   HOGENOM; CLU_098404_0_1_1; -.
DR   InParanoid; Q6PBF7; -.
DR   OrthoDB; 1623701at2759; -.
DR   PhylomeDB; Q6PBF7; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000017003; Expressed in egg cell and 13 other tissues.
DR   ExpressionAtlas; Q6PBF7; baseline.
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..180
FT                   /note="ER membrane protein complex subunit 4"
FT                   /id="PRO_0000251918"
FT   TOPO_DOM        1..63
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        85..95
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        96..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        118..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
FT   TOPO_DOM        146..180
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5J8M3"
SQ   SEQUENCE   180 AA;  19918 MW;  E17163BE8E6B2092 CRC64;
     MATPSNLVAN RGRRFKWAIE FGSGGSRGRG ERGGLQDSMY PVGYSDKQVP DTSVQESDHI
     LVEKRCWDIA LGPLKQIPMN LFIMYMAGNT ISIFPIMMVC MMAWRPIQAL LATPATFKLL
     ESSGQRFLQG LVYLIGNLLG LALAVYKCQS MGLLPTHASD WLAFIEPPER MEYTGGGLLL