EMC2A_XENLA
ID EMC2A_XENLA Reviewed; 297 AA.
AC Q6INS3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=ER membrane protein complex subunit 2-A {ECO:0000305};
DE AltName: Full=Tetratricopeptide repeat protein 35-A;
DE Short=TPR repeat protein 35-A;
GN Name=emc2-a; Synonyms=ttc35-a;
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=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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. By regulating
CC the insertion of various proteins in membranes, it is indirectly
CC involved in many cellular processes. {ECO:0000250|UniProtKB:Q15006}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000250|UniProtKB:Q15006}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15006}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15006}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15006}.
CC -!- SIMILARITY: Belongs to the EMC2 family. {ECO:0000305}.
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DR EMBL; BC072200; AAH72200.1; -; mRNA.
DR RefSeq; NP_001085171.1; NM_001091702.1.
DR RefSeq; XP_018121917.1; XM_018266428.1.
DR AlphaFoldDB; Q6INS3; -.
DR SMR; Q6INS3; -.
DR BioGRID; 101620; 1.
DR IntAct; Q6INS3; 1.
DR MaxQB; Q6INS3; -.
DR DNASU; 432254; -.
DR GeneID; 432254; -.
DR KEGG; xla:432254; -.
DR CTD; 432254; -.
DR Xenbase; XB-GENE-6255734; emc2.L.
DR OMA; LMEWAQN; -.
DR OrthoDB; 956854at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 432254; Expressed in brain and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0072546; C:EMC complex; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum 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; 1.25.40.10; -; 2.
DR InterPro; IPR039856; EMC2-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12760; PTHR12760; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..297
FT /note="ER membrane protein complex subunit 2-A"
FT /id="PRO_0000333733"
FT REPEAT 87..120
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 155..188
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 192..225
FT /note="TPR 3"
FT /evidence="ECO:0000255"
SQ SEQUENCE 297 AA; 34594 MW; 2245090BAA4BAA5C CRC64;
MSKVSDLFDV TWEDMRDKMK TWREENYRNS EHVIEVGEEL INEHASKLGD DIWIIYEQVM
IAALDCGRDD IAMSCLQELR RQFPGSHRVK RLTGLRFEAM ERYDDALQIY DRILQDDPTN
TAARKRKIAI RKAQGRNSEA IRELNEYLEQ FVGDQEAWHE LAELYINELD YAKAAFCLEE
LILTNPHNHF YYQQFAEVKY TQGGLENLEL SRKYFSQALK LNNHNMRALF GLYISSVHIA
SNPKASAKMK KDNVKYATWA ASQIKKAYQL AGRTMTDTQT SLKAVEDMLE TLQITQS