EMC1_CHICK
ID EMC1_CHICK Reviewed; 983 AA.
AC Q5ZL00;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=ER membrane protein complex subunit 1;
DE Flags: Precursor;
GN Name=EMC1; ORFNames=RCJMB04_8i12;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719934; CAG31593.1; -; mRNA.
DR RefSeq; NP_001012856.1; NM_001012838.1.
DR AlphaFoldDB; Q5ZL00; -.
DR SMR; Q5ZL00; -.
DR STRING; 9031.ENSGALP00000006311; -.
DR PaxDb; Q5ZL00; -.
DR PRIDE; Q5ZL00; -.
DR GeneID; 419470; -.
DR KEGG; gga:419470; -.
DR CTD; 23065; -.
DR VEuPathDB; HostDB:geneid_419470; -.
DR eggNOG; KOG2103; Eukaryota.
DR InParanoid; Q5ZL00; -.
DR OrthoDB; 1017611at2759; -.
DR PhylomeDB; Q5ZL00; -.
DR PRO; PR:Q5ZL00; -.
DR Proteomes; UP000000539; Unplaced.
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..16
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT CHAIN 17..983
FT /note="ER membrane protein complex subunit 1"
FT /id="PRO_0000248600"
FT TOPO_DOM 17..952
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT TRANSMEM 953..973
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT TOPO_DOM 974..983
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 903
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 221..231
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT DISULFID 332..360
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
SQ SEQUENCE 983 AA; 109912 MW; 612C3E123BC099D1 CRC64;
MAAGLWALLL PLAAAVYEDQ VGKFDWRQQY VGKLKFASLE AAQGSKKLLV GTEKNVVAAL
NSRSGEILWR HADKATPEGA IDAMLIHGQD AITVSSAGRI LRSWETNIGG LNWETSLDTG
SFQTASLVGL QDAVKYVAVL KKAAISLHYL SNGHQKWVEH LPESENTQYQ MLYSRGAGVI
HVLGVVPQSH LKVLTLSVED GEVIEQTKVA APWLKSLNGA CGVVGEAVLV CADTATHSLY
VCSLETEQEM KQIPLQSLDL EFADGFQPRV LATQPSVINA SRTQFFLQLS PGHFSLLQCK
QGLLSHLRDF QQAALVSFAT TGEKTVAAVL TCRNELKPAS SDGLHGNALE DSQKQEALTC
SNQTYNINLY LVETGQRLLD TTITFNLEQN GAKPEQLYIQ VFLKKDDSVG YRALVQTEDH
MLMFLQQPGK VVWSREESLA EVVSLEMVDL PLTGAQAELE GEFGKKADGL LGMFLKRLSS
QLILLQAWTA HLWKMFYDAR KPRSQIKNEI NIDNLARDEF NLQKMMVMVT ASGKLFGIES
SSGTILWKQY LRNVRPGASL KLMVQRTTAH FPHPPQCTLL VKDKETKMSF LYVFNPIFGK
RSQVAPPVLK RPVLQTLLLP IMDQDYAKVL LLIDDEYKVT AFPATKNVLR QLEEMAHSIF
FYLVDAEQGK LSGFRLKKDL TTEESWQVAI PTEVQRIVTV KGKRSSEHVH SQGRVMGDRS
VLYKSLNPNL LAVVTESTDT HHERTFVGIY LIDGVTGRII HSSVQKKAKG PVHIVHSENW
VVYQYWNTKA RRNEFTVLEL YEGTEQYNAT AFSSLDRPLL PQVLQQSYIF PSAISAMEAT
ITERGITSRH LLIGLPSGAI LSLPKALLDP RRPEIPTEQS REENLIPYSP DVQIHAERFI
NYNQTVSQIR GIYTSPSGLE STCLVVAYGL DIYQTRVYPS KQFDVLKDDY DYVLISSVLF
GLVFATMITK RLAQVKLLNR AWR
