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EMC10_XENLA
ID   EMC10_XENLA             Reviewed;         267 AA.
AC   A5D8P8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=ER membrane protein complex subunit 10;
DE   Flags: Precursor;
GN   Name=emc10;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fat body;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-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. Promotes angiogenesis and tissue repair in the heart after
CC       myocardial infarction. Stimulates cardiac endothelial cell migration
CC       and outgrowth via the activation of p38 MAPK, PAK and MAPK2 signaling
CC       pathways. {ECO:0000250|UniProtKB:Q5UCC4}.
CC   -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC       {ECO:0000250|UniProtKB:Q5UCC4}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q5UCC4}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q5UCC4}.
CC   -!- SIMILARITY: Belongs to the EMC10 family. {ECO:0000305}.
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DR   EMBL; BC141763; AAI41764.1; -; mRNA.
DR   RefSeq; NP_001092176.1; NM_001098706.1.
DR   AlphaFoldDB; A5D8P8; -.
DR   SMR; A5D8P8; -.
DR   GeneID; 100049769; -.
DR   KEGG; xla:100049769; -.
DR   CTD; 100049769; -.
DR   Xenbase; XB-GENE-6078962; emc10.L.
DR   OrthoDB; 1514526at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 100049769; Expressed in testis and 20 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: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; IPR029615; Emc10.
DR   PANTHER; PTHR21397:SF4; PTHR21397:SF4; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT   CHAIN           39..267
FT                   /note="ER membrane protein complex subunit 10"
FT                   /id="PRO_0000315052"
FT   TOPO_DOM        39..226
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        248..267
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5UCC4"
SQ   SEQUENCE   267 AA;  28642 MW;  D01D2F2D5723F3FB CRC64;
     MAAGCLGGQR AGPLSGTVLG NRWAWLIALP LLLAAAAAQG SVCRLKTGDG RESESCGTNL
     ELEHSFELDD SIDFKKRGSL FWSGTAEQSI SILQKQLTED ERNKLRDIAN LNGLYRIRIP
     RKLGISEEVN EYVTSFVRAC SMVESHLSDE ITVHTDISGN VIGVSIVTFP GSCNGAEVED
     VDLEMFNTTV HIQQPIAAAV PETAAFIERL EMEQAQKAKN PQEQKSFFAK YWMYIIPVVL
     FLMMSGASDA GNQGGNGGGG GGGGGGR
 
 
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