ID   EMC7_BOVIN              Reviewed;         241 AA.
AC   A5PJA8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=ER membrane protein complex subunit 7;
DE   Flags: Precursor;
GN   Name=EMC7;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) 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; BC142029; AAI42030.1; -; mRNA.
DR   RefSeq; NP_001092613.1; NM_001099143.2.
DR   AlphaFoldDB; A5PJA8; -.
DR   SMR; A5PJA8; -.
DR   STRING; 9913.ENSBTAP00000009709; -.
DR   PaxDb; A5PJA8; -.
DR   PRIDE; A5PJA8; -.
DR   GeneID; 615423; -.
DR   KEGG; bta:615423; -.
DR   CTD; 56851; -.
DR   eggNOG; KOG3306; Eukaryota.
DR   InParanoid; A5PJA8; -.
DR   OrthoDB; 1348328at2759; -.
DR   Proteomes; UP000009136; 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: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..22
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPA0"
FT   CHAIN           23..241
FT                   /note="ER membrane protein complex subunit 7"
FT                   /id="PRO_0000300093"
FT   TOPO_DOM        23..158
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPA0"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPA0"
FT   REGION          217..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   241 AA;  26560 MW;  F6B9CE8AD24E46A5 CRC64;
     MAATLWAFFS VLLLLLSRDA QSSEVSGSTS DGSGGSGVGT GDRFKIEGRA VVPGVKPQDW
     ISAARVLVDG EEHVGFLKTD GSFVVHDIPS GSYVVEVISP AYRFDPVRVD ITSKGKMRAR
     YVNYIKTSEV VRLPYPLQMK SSGPPSYFIK RESWGWTDFL MNPMVMMMVL PLLIFVLLPK
     VVNTSDPDMR REMEQSMNML NSNHELPDVS EFMTRLFSSK SSDKSSSGSS KTGKSGAGKR
     R