EMC5_BOVIN
ID EMC5_BOVIN Reviewed; 165 AA.
AC Q32LC4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=ER membrane protein complex subunit 5 {ECO:0000250|UniProtKB:Q8N4V1};
DE AltName: Full=Membrane magnesium transporter 1 {ECO:0000250|UniProtKB:Q8K273};
DE AltName: Full=Transmembrane protein 32 {ECO:0000312|EMBL:AAI09650.1};
GN Name=MMGT1 {ECO:0000250|UniProtKB:Q8K273};
GN Synonyms=EMC5 {ECO:0000250|UniProtKB:Q8N4V1},
GN TMEM32 {ECO:0000312|EMBL:AAI09650.1};
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] {ECO:0000312|EMBL:AAI09650.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI09650.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAI09650.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-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 similarity). By regulating the insertion
CC of various proteins in membranes, it is indirectly involved in many
CC cellular processes. May be involved in Mg(2+) transport (By
CC similarity). {ECO:0000250|UniProtKB:Q8K273,
CC ECO:0000250|UniProtKB:Q8N4V1}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q8N4V1}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8N4V1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8N4V1}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8K273}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8N4V1}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q8K273}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8N4V1}.
CC -!- SIMILARITY: Belongs to the membrane magnesium transporter (TC 1.A.67)
CC family. {ECO:0000305}.
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DR EMBL; BC109649; AAI09650.1; -; mRNA.
DR RefSeq; NP_001073098.1; NM_001079630.1.
DR AlphaFoldDB; Q32LC4; -.
DR STRING; 9913.ENSBTAP00000035380; -.
DR PaxDb; Q32LC4; -.
DR PRIDE; Q32LC4; -.
DR GeneID; 617557; -.
DR KEGG; bta:617557; -.
DR CTD; 93380; -.
DR eggNOG; KOG3918; Eukaryota.
DR InParanoid; Q32LC4; -.
DR OrthoDB; 1558871at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; IPR018937; MMgT.
DR Pfam; PF10270; MMgT; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; Magnesium; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..165
FT /note="ER membrane protein complex subunit 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000365623"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT TRANSMEM 4..22
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT TOPO_DOM 23..77
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT TRANSMEM 78..97
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT TOPO_DOM 98..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4V1"
SQ SEQUENCE 165 AA; 18950 MW; 5BA8B0E7F8FB6531 CRC64;
MAPSLWKGLV GIGLFALAHA AFSAAQHYFP SSGIKWKRKC EFLQSSSFQD KIFRSMYYVY
DRSYMRLTEK EDESLPIDIV LQTLLAFAVT CYGIVHIAGE FKDMDATSEL KNKTFDTLRN
HPSFYVYNHR GRVLFRPSDT TNSSNQDALS SNTSLKLRKL ESLRR