EMC10_DANRE
ID EMC10_DANRE Reviewed; 257 AA.
AC A7E2M3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=ER membrane protein complex subunit 10;
DE Flags: Precursor;
GN Name=emc10; ORFNames=zgc:171980;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Larval eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-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; BC150420; AAI50421.1; -; mRNA.
DR RefSeq; NP_001095859.2; NM_001102389.2.
DR AlphaFoldDB; A7E2M3; -.
DR SMR; A7E2M3; -.
DR STRING; 7955.ENSDARP00000071497; -.
DR PaxDb; A7E2M3; -.
DR PeptideAtlas; A7E2M3; -.
DR GeneID; 565829; -.
DR KEGG; dre:565829; -.
DR CTD; 284361; -.
DR ZFIN; ZDB-GENE-030131-9045; emc10.
DR eggNOG; KOG4827; Eukaryota.
DR InParanoid; A7E2M3; -.
DR OrthoDB; 1514526at2759; -.
DR PhylomeDB; A7E2M3; -.
DR PRO; PR:A7E2M3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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: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..23
FT /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT CHAIN 24..257
FT /note="ER membrane protein complex subunit 10"
FT /id="PRO_0000315051"
FT TOPO_DOM 24..218
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5UCC4"
SQ SEQUENCE 257 AA; 28244 MW; 32B83FA6C8BC078F CRC64;
MAPIRVLSLV LPILSTVTLL LTQFGECNNG RRSGDAVDTD FSGFSVPLEH SFEVDDVPRF
RLRGALQFRG GRENSVYLSQ NQLSEKDRNT LKDVAAVDGL YRIRVPRVSL QVDRQTERQY
EGYLTAFVRA CALVESHLSD VITLHTDVSG YVIGISIVTI PGSCRGIEVE DEVDLEVFNT
TISVMAPVTA PVPETAPYIE RMEMEMEKKG KNPQEQKSFF AKYWMYIVPL VLFLMMSGAQ
DQSGGGAGGG AANGGGR