EMC1_PONAB
ID EMC1_PONAB Reviewed; 996 AA.
AC Q5R7K6; Q5RBK7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=ER membrane protein complex subunit 1;
DE Flags: Precursor;
GN Name=EMC1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-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; CR858637; CAH90853.1; -; mRNA.
DR EMBL; CR860109; CAH92254.1; -; mRNA.
DR RefSeq; NP_001126319.1; NM_001132847.1.
DR AlphaFoldDB; Q5R7K6; -.
DR SMR; Q5R7K6; -.
DR STRING; 9601.ENSPPYP00000002080; -.
DR GeneID; 100173298; -.
DR KEGG; pon:100173298; -.
DR CTD; 23065; -.
DR eggNOG; KOG2103; Eukaryota.
DR InParanoid; Q5R7K6; -.
DR OrthoDB; 1017611at2759; -.
DR Proteomes; UP000001595; 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..22
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT CHAIN 23..996
FT /note="ER membrane protein complex subunit 1"
FT /id="PRO_0000248599"
FT TOPO_DOM 23..965
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT TRANSMEM 966..986
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT TOPO_DOM 987..996
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT CARBOHYD 916
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 227..237
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT DISULFID 338..368
FT /evidence="ECO:0000250|UniProtKB:Q8N766"
FT CONFLICT 661
FT /note="V -> F (in Ref. 1; CAH90853)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="R -> Q (in Ref. 1; CAH90853)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="A -> V (in Ref. 1; CAH90853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 996 AA; 112112 MW; DB279A6C0D53BE5E CRC64;
MAAEWASRFW LWAALLIPVA AVYEDQVGKF DWRQQYVGKL KFASLEFSPG SKKLVVATEK
NVIAALNSRT GEILWRHVDK GTAEGAVDAM LLHGQDVITV SNGGRIMRSW ETNIGGLNWE
ITLDTGSFQA LGLVGLQESV RYIAVLKKTT LALHHLSSGH LKWVEHLPES DSIHYQMVYS
YGSGVVWALG VVPFSHVNIV KFNVEDGEIV QQVRVSTPWL QHLSGACGVV DEAVLVCPDP
SSRSLQTLAL ETEWELRQIP LQSLDLEFGS GFQPRVLPTQ PNPVDASRAQ FFLHLSPSHY
ALLQYHYGIL SLLKNFPQTA LVSFATTGEK TVAAVMACRN EVQKTSNSED GSMGSFSEKS
SSKDSLACFN QTYTINLYLV ETGRRLLDTT TTFSLEQSGT RPERLYIQVF LKKDDSVGYR
ALVQTEDHLL LFLQQLAGKV VLWSREESLA EVVCLEMVDL PLTGAQAELE GEFGKKAAIQ
DGLLGMFLKR LSSQLILLQA WTSHLWKMFY DARKPRSQIK NEINIDTLAR DEFNLQKMMV
MVTASGKLFG IESSSGTILW KQYLPSVKPD SSFKLMVQRT TAHFPHPPQC TLLVKDKESG
MSSLYVFNPI FGKWSQVAPP VLKRPILQSL LLPVMDQDYA KVLLLIDDEY KVTAFPATRN
VLRQLHELAP SIFFYLVDAE QGRLCGYRLR KDLTTELSWE LTIPPEVRRI VKVKGKRSSE
HVHSQGRVMG DRSVLYKSLN PNLLAVVTES TDAHHERTFI GIFLIDGVTG RIIHSSAQKK
AKGPVHIVHS ENWVVYQYWN TKARRNEFTV LELYEGTEQY NATAFSSLDR PQLPQVLQQS
YIFPSSISAM EATITERGIT SRHLLIGLPS GAILSLPKAL LDPRRPEIPT EQSREENLIP
YSPDVQIHAE RFINYNQTVS RMRGIYTAPS GLESTCLVVA YGLDIYQTRV YPSKQFDVLK
DDYDYVLISS VLFGLVFATM ITKRLAQVKL LNRAWR
