EMC1_XENLA
ID EMC1_XENLA Reviewed; 987 AA.
AC Q6NRB9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ER membrane protein complex subunit 1;
DE Flags: Precursor;
GN Name=emc1;
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=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) 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. {ECO:0000250|UniProtKB:Q8N766}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q8N766}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8N766}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q8N766}.
CC -!- SIMILARITY: Belongs to the EMC1 family. {ECO:0000305}.
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DR EMBL; BC070840; AAH70840.1; -; mRNA.
DR RefSeq; NP_001084811.1; NM_001091342.1.
DR AlphaFoldDB; Q6NRB9; -.
DR SMR; Q6NRB9; -.
DR PRIDE; Q6NRB9; -.
DR DNASU; 431852; -.
DR GeneID; 431852; -.
DR KEGG; xla:431852; -.
DR CTD; 431852; -.
DR Xenbase; XB-GENE-1010285; emc1.L.
DR OrthoDB; 1017611at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 431852; Expressed in camera-type eye and 20 other tissues.
DR GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; 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 Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR026895; EMC1.
DR InterPro; IPR011678; EMC1_C.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR21573; PTHR21573; 1.
DR Pfam; PF07774; EMC1_C; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT CHAIN 22..987
FT /note="ER membrane protein complex subunit 1"
FT /id="PRO_0000248601"
FT TOPO_DOM 22..956
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT TRANSMEM 957..977
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT TOPO_DOM 978..987
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT CARBOHYD 812
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 815
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 225..235
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT DISULFID 337..364
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
SQ SEQUENCE 987 AA; 110767 MW; A71D19EB3B7FE917 CRC64;
MAADLCWLSL LLASLALSGA VYEDQVGKFD WRQEYVGRIK FASLESGLGA KKLIAVTDKN
IIAALNSRTG DLLWRHVDKD TSEGTVDALM MIGQDAITVS GGRLLRSWET NIGALNWEAA
LEPGSFQAVS FAGSQDTARY VAVLKNSALS LYFLSNGHLK WSESLPESDT VQYQLLYSPY
KGSVHVVGLV PHSHLTILTF SLEDGSISHQ VRVLTPWLRT LHGTCGVIGE GVLVCGDVPM
ASVHIVSLLS GEETTRYSVQ SLDIELAEDP TQLDVITAPQ NGIGGSLSQF FLQIAPRRFL
LMHYHDGVLT PLRDFSQVSL VNFATTGEKT VVAVMQCKTE GNPKSGAESE YLTGQNCAQE
PWYCPGHTYS INLYMADSGR RLLETTMSFT LDQICVRPDS FYLQTFLRKD DSVGYRALVQ
TEDNQLLFLQ QPGKLIWLRE ESLADVVTME TVDLPLTGAQ AELEGEFGKK ADGLIGMVLK
RLSSQLILLQ SWSAHLWKMF CDARKPRSQI RNEINVDTLA RDDFNLQKMM VMVTASGKLF
GIESSSGSIL WKFYLHGVHP GSSFKLLVQR TTAHFPHPPQ CTLLVKDKVT EKSAMYVFNP
IFGKLSQLAP PPLQRPILQS LLLPIMDNDY AKVLLLLDDQ HKVIAFPATK YVLQQLQELH
STIFFYLVDV EKGKLSGLRL NKDLSTEEIW EVLLPADQQR ITVVKGKRSN EHVHSQGRVM
GDRSVLYKYL NPNLLVLVTE STDTHPERCF IGIYLIDGVT GRIIHSSVQR RARGPVQIIH
SENWVVYQYW NSKARRNELT VLELYEGTEQ YNSTNFSSLD RPLLPHVLQQ SYIFPSAIRA
MQATITERGI TSRHILIGLP SGAILSLPKA LLDPRRPEIP NEYTREENLI PYTPDIQIHA
ERFINYNQTI SRMRGIYTAP SGLESTCLVV AYGLDLYQTR VYPSKQFDVL KDDYDYILIS
SVLIGLVFAT MITKRLAQVK LLNRAWR
