EMC9_RAT
ID EMC9_RAT Reviewed; 206 AA.
AC Q5U1W7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=ER membrane protein complex subunit 9;
DE AltName: Full=Protein FAM158A;
GN Name=Emc9; Synonyms=Fam158a;
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=Ovary;
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).
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. {ECO:0000250|UniProtKB:Q9Y3B6}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC). EMC8 and
CC EMC9 are mutually exclusive subunits of the EMC complex.
CC {ECO:0000250|UniProtKB:Q9Y3B6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y3B6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Y3B6}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9Y3B6}.
CC -!- SIMILARITY: Belongs to the EMC8/EMC9 family. {ECO:0000305}.
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DR EMBL; BC086432; AAH86432.1; -; mRNA.
DR RefSeq; NP_001008297.1; NM_001008296.1.
DR AlphaFoldDB; Q5U1W7; -.
DR SMR; Q5U1W7; -.
DR STRING; 10116.ENSRNOP00000026001; -.
DR PaxDb; Q5U1W7; -.
DR Ensembl; ENSRNOT00000026001; ENSRNOP00000026001; ENSRNOG00000019162.
DR GeneID; 290224; -.
DR KEGG; rno:290224; -.
DR UCSC; RGD:1308113; rat.
DR CTD; 51016; -.
DR RGD; 1308113; Emc9.
DR eggNOG; KOG3289; Eukaryota.
DR GeneTree; ENSGT00390000006738; -.
DR HOGENOM; CLU_087337_0_1_1; -.
DR InParanoid; Q5U1W7; -.
DR OMA; QANACAS; -.
DR OrthoDB; 1284861at2759; -.
DR PhylomeDB; Q5U1W7; -.
DR TreeFam; TF313860; -.
DR PRO; PR:Q5U1W7; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000019162; Expressed in heart and 19 other tissues.
DR Genevisible; Q5U1W7; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR GO; GO:0032977; F:membrane insertase activity; IEA:Ensembl.
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 CDD; cd08060; MPN_UPF0172; 1.
DR InterPro; IPR005366; EMC8/9.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR12941; PTHR12941; 1.
DR Pfam; PF03665; UPF0172; 1.
DR PROSITE; PS50249; MPN; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome.
FT CHAIN 1..206
FT /note="ER membrane protein complex subunit 9"
FT /id="PRO_0000328441"
FT DOMAIN 4..139
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 206 AA; 22941 MW; 91DFFE555B58C702 CRC64;
MGEVEISARA YGKMCLHASR YPHAAVNGLL LAPATRSGEC LCLTDCVPLF HSHLALSVML
EVALNQVDVW ATQAGLVVAG YYHANAVLDD QSPGPLALKI AGRIAEFFPN AVLIMLDNKK
LVTWPRVPPV IVLENQGLQW VPKDKNLVMW RDWEESRQMV GALLEGRAHQ HLVDFDCHLD
DIRQDWTNQR LNTQITQWSG STDGHA