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EMC5_XENTR
ID   EMC5_XENTR              Reviewed;         132 AA.
AC   Q28HV5; B3DL23;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, 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};
GN   Name=mmgt1 {ECO:0000250|UniProtKB:Q8K273};
GN   Synonyms=emc5 {ECO:0000250|UniProtKB:Q8N4V1}; ORFNames=TEgg056o02.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2008) 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; CR760716; CAJ82266.1; -; mRNA.
DR   EMBL; BC167281; AAI67281.1; -; mRNA.
DR   EMBL; BC170697; AAI70697.1; -; mRNA.
DR   EMBL; BC170699; AAI70699.1; -; mRNA.
DR   RefSeq; NP_001016553.1; NM_001016553.2.
DR   AlphaFoldDB; Q28HV5; -.
DR   SMR; Q28HV5; -.
DR   STRING; 8364.ENSXETP00000047441; -.
DR   PaxDb; Q28HV5; -.
DR   Ensembl; ENSXETT00000047441; ENSXETP00000047441; ENSXETG00000024459.
DR   GeneID; 549307; -.
DR   KEGG; xtr:549307; -.
DR   CTD; 93380; -.
DR   Xenbase; XB-GENE-999449; mmgt1.
DR   eggNOG; KOG3918; Eukaryota.
DR   HOGENOM; CLU_122437_1_0_1; -.
DR   InParanoid; Q28HV5; -.
DR   OMA; YYSVQYE; -.
DR   OrthoDB; 1558871at2759; -.
DR   PhylomeDB; Q28HV5; -.
DR   TreeFam; TF323267; -.
DR   Proteomes; UP000008143; Chromosome 8.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000024459; Expressed in egg cell and 14 other tissues.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; 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:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015693; P:magnesium ion transport; 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   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..132
FT                   /note="ER membrane protein complex subunit 5"
FT                   /id="PRO_0000286441"
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..43
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT   TRANSMEM        44..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4V1"
FT   TOPO_DOM        64..132
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4V1"
SQ   SEQUENCE   132 AA;  14942 MW;  3D1D4D9AB42F2C72 CRC64;
     MASSIWKGLV GIGLFALAHA AFSAAQHRSY MRLTEKEDET LPIDIVLQTL LAFIVACYGI
     VHIAGEFKDM DATSELRNKT FDTLRNHPSF YVFNHRGRVM FQPPESEDCH RIQAPFSSNS
     SLKLSKLESM HR
 
 
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