ID   EMC2_PONAB              Reviewed;         297 AA.
AC   Q5R882;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=ER membrane protein complex subunit 2 {ECO:0000305};
DE   AltName: Full=Tetratricopeptide repeat protein 35 {ECO:0000250|UniProtKB:Q15006};
DE            Short=TPR repeat protein 35 {ECO:0000250|UniProtKB:Q15006};
GN   Name=EMC2 {ECO:0000250|UniProtKB:Q15006};
GN   Synonyms=TTC35 {ECO:0000250|UniProtKB:Q15006};
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=Kidney;
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: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}. Note=May also localize to the nuclear
CC       envelope. {ECO:0000250|UniProtKB:Q9CRD2}.
CC   -!- SIMILARITY: Belongs to the EMC2 family. {ECO:0000305}.
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DR   EMBL; CR859872; CAH92028.1; -; mRNA.
DR   RefSeq; NP_001127498.1; NM_001134026.1.
DR   RefSeq; XP_009242301.1; XM_009244026.1.
DR   AlphaFoldDB; Q5R882; -.
DR   SMR; Q5R882; -.
DR   STRING; 9601.ENSPPYP00000021116; -.
DR   Ensembl; ENSPPYT00000021959; ENSPPYP00000021116; ENSPPYG00000018820.
DR   GeneID; 100174573; -.
DR   KEGG; pon:100174573; -.
DR   CTD; 9694; -.
DR   eggNOG; KOG3060; Eukaryota.
DR   GeneTree; ENSGT00390000011922; -.
DR   HOGENOM; CLU_052388_1_0_1; -.
DR   InParanoid; Q5R882; -.
DR   OMA; YILTCAE; -.
DR   OrthoDB; 956854at2759; -.
DR   TreeFam; TF312997; -.
DR   Proteomes; UP000001595; Chromosome 8.
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: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   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR039856; EMC2-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR12760; PTHR12760; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; Membrane; Reference proteome; Repeat;
KW   TPR repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q15006"
FT   CHAIN           2..297
FT                   /note="ER membrane protein complex subunit 2"
FT                   /id="PRO_0000333730"
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"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15006"
FT   MOD_RES         255
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15006"
SQ   SEQUENCE   297 AA;  34819 MW;  C86703AEC22DE36A CRC64;
     MAKVSELYDV TWEEMRDKMR KWREENSRNS EQIVEVGEEL INEYGSKLGD DIWIIYEQVM
     IAALDYGRDD LALFCLQELR RQFPGSHRVK RLTGMRFEAM ERYDDAIQLY DRILQEDPTN
     TAARKRKIAI RKAQGKNVEA IRELNEYLEQ FVGDQEAWHE LAELYINEHD YAKAAFCLEE
     LMMTNPHNHL YCQQYAEVKY TQGGLENLEL SRKYFAQALK LNNRNMRALF GLYMSASHIA
     SNPKASAKTK KDNMKYASWA ASQINRAYQF AGRSKKETKY SLKAVEDMLE TLQITQS