ID   EMC7_MACFA              Reviewed;         242 AA.
AC   Q4R5V2;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=ER membrane protein complex subunit 7;
DE   Flags: Precursor;
GN   Name=EMC7; ORFNames=QtsA-20627;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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:Q9NPA0}.
CC   -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC       {ECO:0000250|UniProtKB:Q9NPA0}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9NPA0}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q9NPA0}.
CC   -!- SIMILARITY: Belongs to the EMC7 family. {ECO:0000305}.
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DR   EMBL; AB169441; BAE01523.1; -; mRNA.
DR   RefSeq; NP_001271760.1; NM_001284831.1.
DR   AlphaFoldDB; Q4R5V2; -.
DR   SMR; Q4R5V2; -.
DR   STRING; 9541.XP_005559136.1; -.
DR   GeneID; 101866934; -.
DR   CTD; 56851; -.
DR   VEuPathDB; HostDB:ENSMFAG00000038054; -.
DR   eggNOG; KOG3306; Eukaryota.
DR   OMA; EMENMQM; -.
DR   OrthoDB; 1348328at2759; -.
DR   Proteomes; UP000233100; Chromosome 7.
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:0030246; F:carbohydrate binding; IEA:InterPro.
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; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR039163; EMC7.
DR   InterPro; IPR019008; EMC7_beta_sandwich.
DR   PANTHER; PTHR13605; PTHR13605; 1.
DR   Pfam; PF09430; DUF2012; 1.
DR   SUPFAM; SSF49452; SSF49452; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPA0"
FT   CHAIN           24..242
FT                   /note="ER membrane protein complex subunit 7"
FT                   /id="PRO_0000240861"
FT   TOPO_DOM        24..159
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPA0"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPA0"
FT   REGION          217..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   242 AA;  26445 MW;  071930A99A40929E CRC64;
     MAAALWGFFP VLLLLLLSGD VQSSEVPGAA AEGSGGSGVG IGDRFKIEGR AVVPGVKPQD
     WISAARVLVD GEEHVGFLKT DGSFVVHDIP SGSYVVEVVS PAYRFDPVRV DITSKGKMRA
     RYVNHIKTSE VVRLPYPLQM KSSGPPSYFI KRESWGWTDF LMNPMVMMMV LPLLIFVLLP
     KVVNTSDPDM RREMEQSMNM LNSNHELPDV SEFMTRLFSS KSSGKSSSGS SKTGKSGAGK
     RR