ID   EMC3_BOVIN              Reviewed;         261 AA.
AC   Q3ZCB8;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=ER membrane protein complex subunit 3;
DE   AltName: Full=Transmembrane protein 111;
GN   Name=EMC3; Synonyms=TMEM111;
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=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-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:Q9P0I2}.
CC   -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC       {ECO:0000250|UniProtKB:Q9P0I2}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9P0I2}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9P0I2}.
CC   -!- SIMILARITY: Belongs to the EMC3 family. {ECO:0000305}.
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DR   EMBL; BC102575; AAI02576.1; -; mRNA.
DR   RefSeq; NP_001030228.1; NM_001035056.1.
DR   AlphaFoldDB; Q3ZCB8; -.
DR   SMR; Q3ZCB8; -.
DR   STRING; 9913.ENSBTAP00000005064; -.
DR   PaxDb; Q3ZCB8; -.
DR   PRIDE; Q3ZCB8; -.
DR   Ensembl; ENSBTAT00000005064; ENSBTAP00000005064; ENSBTAG00000003882.
DR   GeneID; 508371; -.
DR   KEGG; bta:508371; -.
DR   CTD; 55831; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003882; -.
DR   VGNC; VGNC:28464; EMC3.
DR   eggNOG; KOG3188; Eukaryota.
DR   GeneTree; ENSGT00390000005780; -.
DR   InParanoid; Q3ZCB8; -.
DR   OMA; WYFLTLF; -.
DR   OrthoDB; 1482782at2759; -.
DR   Proteomes; UP000009136; Chromosome 22.
DR   Bgee; ENSBTAG00000003882; Expressed in semitendinosus and 104 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:0032977; F:membrane insertase activity; IEA:Ensembl.
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; IPR008568; EMC3.
DR   InterPro; IPR002809; EMC3/TMCO1.
DR   PANTHER; PTHR13116; PTHR13116; 1.
DR   Pfam; PF01956; EMC3_TMCO1; 1.
DR   PIRSF; PIRSF010045; DUF850_TM_euk; 1.
DR   SMART; SM01415; DUF106; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT   CHAIN           2..261
FT                   /note="ER membrane protein complex subunit 3"
FT                   /id="PRO_0000249456"
FT   TOPO_DOM        2..14
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT   TRANSMEM        15..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT   TOPO_DOM        39..114
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT   TRANSMEM        115..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT   TOPO_DOM        131..168
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT   TRANSMEM        169..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0I2"
FT   TOPO_DOM        188..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0I2"
SQ   SEQUENCE   261 AA;  29920 MW;  700C8B661C3C0AD8 CRC64;
     MAGPELLLDS NIRLWVVLPI VIITFFVGMI RHYVSILLQS DKKLTQEQVS DSQVLIRSRV
     LRENGKYIPK QSFLTRKYYF NNPEDGFFKK TKRKVVPPSP VTDPTMLTDM MKGNVTNVLP
     MILIGGWINM TFSGFVTTKV PFPLTLRFKP MLQQGIELLT LDASWVSSAS WYFLNVFGLR
     SIYSLILGQD NAADQSRMMQ EQMTGAAMAM PADTNKAFKT EWEALELTDH QWALDDVEEE
     LMAKDLHFEG MFKKELQTSI F