ID   EMC6_DANRE              Reviewed;         110 AA.
AC   Q6P0F0; Q7ZV31;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=ER membrane protein complex subunit 6;
DE   AltName: Full=Transmembrane protein 93;
GN   Name=emc6; Synonyms=tmem93; ORFNames=zgc:77320;
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].
RC   STRAIN=SJD; TISSUE=Embryo;
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: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; BC046024; AAH46024.1; -; mRNA.
DR   EMBL; BC065646; AAH65646.1; -; mRNA.
DR   RefSeq; NP_956350.2; NM_200056.2.
DR   AlphaFoldDB; Q6P0F0; -.
DR   SMR; Q6P0F0; -.
DR   STRING; 7955.ENSDARP00000051134; -.
DR   PaxDb; Q6P0F0; -.
DR   Ensembl; ENSDART00000051135; ENSDARP00000051134; ENSDARG00000035282.
DR   GeneID; 337220; -.
DR   KEGG; dre:337220; -.
DR   CTD; 83460; -.
DR   ZFIN; ZDB-GENE-030131-9164; emc6.
DR   eggNOG; KOG4455; Eukaryota.
DR   GeneTree; ENSGT00390000003917; -.
DR   HOGENOM; CLU_110781_3_0_1; -.
DR   InParanoid; Q6P0F0; -.
DR   OMA; FIYGMVH; -.
DR   OrthoDB; 1547548at2759; -.
DR   PhylomeDB; Q6P0F0; -.
DR   TreeFam; TF332611; -.
DR   PRO; PR:Q6P0F0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 5.
DR   Bgee; ENSDARG00000035282; Expressed in mature ovarian follicle and 28 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: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..110
FT                   /note="ER membrane protein complex subunit 6"
FT                   /id="PRO_0000254158"
FT   TOPO_DOM        1..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT   TRANSMEM        29..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT   TOPO_DOM        45..50
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT   TOPO_DOM        72..89
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT   TRANSMEM        90..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT   TOPO_DOM        107..110
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BV81"
FT   CONFLICT        63
FT                   /note="S -> P (in Ref. 1; AAH46024)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   110 AA;  12076 MW;  5BF9DF52E574D01B CRC64;
     MASVAAKREG PQFISEVSVR GNGAVLDYCR TSVSALSGAT AGILGLTGLY GFVFYFLASF
     LLSLLLILKA GRRWNKCFKS RRLLFTGGLV GGLFTYVLFW TFLYGMVHVY