EMC10_RAT
ID EMC10_RAT Reviewed; 258 AA.
AC Q6AYH6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=ER membrane protein complex subunit 10;
DE Flags: Precursor;
GN Name=Emc10; Synonyms=Inm02;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP TISSUE SPECIFICITY, AND INDUCTION BY GLUCOSE.
RX PubMed=19570817; DOI=10.1677/joe-09-0086;
RA Wang X., Gong W., Liu Y., Yang Z., Zhou W., Wang M., Yang Z., Wen J.,
RA Hu R.;
RT "Molecular cloning of a novel secreted peptide, INM02, and regulation of
RT its expression by glucose.";
RL J. Endocrinol. 202:355-364(2009).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-182, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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 -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
CC pancreatic islets, testis and bladder. Present in the islets of
CC Langerhans (at protein level). {ECO:0000269|PubMed:19570817}.
CC -!- INDUCTION: By glucose in pancreatic islets.
CC {ECO:0000269|PubMed:19570817}.
CC -!- SIMILARITY: Belongs to the EMC10 family. {ECO:0000305}.
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DR EMBL; BC079041; AAH79041.1; -; mRNA.
DR RefSeq; NP_001004221.2; NM_001004221.2.
DR AlphaFoldDB; Q6AYH6; -.
DR SMR; Q6AYH6; -.
DR STRING; 10116.ENSRNOP00000026445; -.
DR GlyGen; Q6AYH6; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q6AYH6; -.
DR PaxDb; Q6AYH6; -.
DR PRIDE; Q6AYH6; -.
DR Ensembl; ENSRNOT00000119814; ENSRNOP00000077150; ENSRNOG00000019532.
DR GeneID; 292878; -.
DR KEGG; rno:292878; -.
DR UCSC; RGD:1303214; rat.
DR CTD; 284361; -.
DR RGD; 1303214; Emc10.
DR eggNOG; KOG4827; Eukaryota.
DR GeneTree; ENSGT00390000004520; -.
DR HOGENOM; CLU_065716_0_0_1; -.
DR InParanoid; Q6AYH6; -.
DR OMA; QFNDVLW; -.
DR OrthoDB; 1514526at2759; -.
DR PhylomeDB; Q6AYH6; -.
DR TreeFam; TF314052; -.
DR PRO; PR:Q6AYH6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019532; Expressed in pancreas and 19 other tissues.
DR Genevisible; Q6AYH6; RN.
DR GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
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:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; 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 1: Evidence at protein level;
KW Angiogenesis; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT CHAIN 26..258
FT /note="ER membrane protein complex subunit 10"
FT /id="PRO_0000315050"
FT TOPO_DOM 26..221
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
SQ SEQUENCE 258 AA; 26968 MW; CE5CE48D6DD40BD4 CRC64;
MVAAGAGVTQ LLVLLLMVAA VPSRARGSGC RVGAAARGVG ADGHEAEGCG TVALLLEHSF
EIGDGANFQK RGSLLWNQQD GTLSATQRQL SEEERGRLRD VAAVNGLYRV RVPRRPGTLD
GSEAGGHVSS FVPACSLVES HLSDQLTLHV DVAGNVVGLS VVVYPGGCRG SEVEDEDLEL
FNTSVHLRPP GTAPGPETAA FIERLEMEQA QKAKNPQEQK SFFAKYWMYI IPVVLFLMMS
GAPDAGGQGG GGGGGSSR
