ID   EMC2_HUMAN              Reviewed;         297 AA.
AC   Q15006; Q8WUE1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   10-JUN-2026, entry version 202.
DE   RecName: Full=ER membrane protein complex subunit 2 {ECO:0000305};
DE   AltName: Full=Tetratricopeptide repeat protein 35 {ECO:0000312|HGNC:HGNC:28963};
DE            Short=TPR repeat protein 35 {ECO:0000312|HGNC:HGNC:28963};
GN   Name=EMC2 {ECO:0000312|HGNC:HGNC:28963};
GN   Synonyms=KIAA0103 {ECO:0000312|EMBL:BAA03493.1}, TTC35
GN   {ECO:0000312|HGNC:HGNC:28963};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA   Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA   Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. III. The
RT   coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:37-43(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Urinary bladder;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-255, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [6]
RP   IDENTIFICATION IN THE EMC COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=22119785; DOI=10.1038/ncb2383;
RA   Christianson J.C., Olzmann J.A., Shaler T.A., Sowa M.E., Bennett E.J.,
RA   Richter C.M., Tyler R.E., Greenblatt E.J., Harper J.W., Kopito R.R.;
RT   "Defining human ERAD networks through an integrative mapping strategy.";
RL   Nat. Cell Biol. 14:93-105(2012).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [9]
RP   FUNCTION.
RX   PubMed=30415835; DOI=10.1016/j.cell.2018.10.009;
RA   Chitwood P.J., Juszkiewicz S., Guna A., Shao S., Hegde R.S.;
RT   "EMC Is Required to Initiate Accurate Membrane Protein Topogenesis.";
RL   Cell 175:1507-1519(2018).
RN   [10]
RP   FUNCTION.
RX   PubMed=29809151; DOI=10.7554/elife.37018;
RA   Shurtleff M.J., Itzhak D.N., Hussmann J.A., Schirle Oakdale N.T.,
RA   Costa E.A., Jonikas M., Weibezahn J., Popova K.D., Jan C.H., Sinitcyn P.,
RA   Vembar S.S., Hernandez H., Cox J., Burlingame A.L., Brodsky J.L., Frost A.,
RA   Borner G.H., Weissman J.S.;
RT   "The ER membrane protein complex interacts cotranslationally to enable
RT   biogenesis of multipass membrane proteins.";
RL   Elife 7:0-0(2018).
RN   [11]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=29242231; DOI=10.1126/science.aao3099;
RA   Guna A., Volkmar N., Christianson J.C., Hegde R.S.;
RT   "The ER membrane protein complex is a transmembrane domain insertase.";
RL   Science 359:470-473(2018).
RN   [12]
RP   FUNCTION, SUBUNIT, INTERACTION WITH WNK1, AND UBIQUITINATION.
RX   PubMed=33964204; DOI=10.1016/j.molcel.2021.04.013;
RA   Pleiner T., Hazu M., Tomaleri G.P., Januszyk K., Oania R.S.,
RA   Sweredoski M.J., Moradian A., Guna A., Voorhees R.M.;
RT   "WNK1 is an assembly factor for the human ER membrane protein complex.";
RL   Mol. Cell 81:2693-2704(2021).
RN   [13] {ECO:0007744|PDB:6Y4L, ECO:0007744|PDB:6Z3W}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 11-274 IN COMPLEX WITH EMC9,
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) OF THE EMC COMPLEX,
RP   FUNCTION, SUBUNIT, TOPOLOGY, AND MUTAGENESIS OF ILE-61; MET-95; ALA-122;
RP   189-HIS--TYR-191 AND 193-GLN-GLN-194.
RX   PubMed=32459176; DOI=10.7554/elife.57887;
RA   O'Donnell J.P., Phillips B.P., Yagita Y., Juszkiewicz S., Wagner A.,
RA   Malinverni D., Keenan R.J., Miller E.A., Hegde R.S.;
RT   "The architecture of EMC reveals a path for membrane protein insertion.";
RL   Elife 9:0-0(2020).
RN   [14] {ECO:0007744|PDB:6WW7}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF THE EMC COMPLEX,
RP   FUNCTION, TOPOLOGY, AND MUTAGENESIS OF ARG-28; GLU-156; GLU-160; TYR-171;
RP   GLU-180; TYR-200; ARG-227 AND TRP-259.
RX   PubMed=32439656; DOI=10.1126/science.abb5008;
RA   Pleiner T., Tomaleri G.P., Januszyk K., Inglis A.J., Hazu M.,
RA   Voorhees R.M.;
RT   "Structural basis for membrane insertion by the human ER membrane protein
RT   complex.";
RL   Science 369:433-436(2020).
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       (PubMed:29242231, PubMed:29809151, PubMed:30415835, PubMed:32439656,
CC       PubMed:32459176, PubMed:33964204). Preferentially accommodates proteins
CC       with transmembrane domains that are weakly hydrophobic or contain
CC       destabilizing features such as charged and aromatic residues
CC       (PubMed:29242231, PubMed:29809151, PubMed:30415835). Involved in the
CC       cotranslational insertion of multi-pass membrane proteins in which
CC       stop-transfer membrane-anchor sequences become ER membrane spanning
CC       helices (PubMed:29809151, PubMed:30415835). It is also required for the
CC       post-translational insertion of tail-anchored/TA proteins in
CC       endoplasmic reticulum membranes (PubMed:29242231, PubMed:29809151). By
CC       mediating the proper cotranslational insertion of N-terminal
CC       transmembrane domains in an N-exo topology, with translocated N-
CC       terminus in the lumen of the ER, controls the topology of multi-pass
CC       membrane proteins like the G protein-coupled receptors
CC       (PubMed:30415835). By regulating the insertion of various proteins in
CC       membranes, it is indirectly involved in many cellular processes
CC       (Probable). {ECO:0000269|PubMed:29242231, ECO:0000269|PubMed:29809151,
CC       ECO:0000269|PubMed:30415835, ECO:0000269|PubMed:32439656,
CC       ECO:0000269|PubMed:32459176, ECO:0000269|PubMed:33964204, ECO:0000305}.
CC   -!- SUBUNIT: Component of the ER membrane protein complex (EMC)
CC       (PubMed:22119785, PubMed:29242231, PubMed:32439656, PubMed:32459176,
CC       PubMed:33964204). Interacts with WNK1 (via amphipathic alpha-helix
CC       region); promoting the ER membrane protein complex assembly by
CC       preventing EMC2 ubiquitination (PubMed:33964204).
CC       {ECO:0000269|PubMed:22119785, ECO:0000269|PubMed:29242231,
CC       ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176,
CC       ECO:0000269|PubMed:33964204}.
CC   -!- INTERACTION:
CC       Q15006; Q53Y03: COX4NB; NbExp=3; IntAct=EBI-359031, EBI-10235116;
CC       Q15006; Q9P0I2: EMC3; NbExp=12; IntAct=EBI-359031, EBI-1054670;
CC       Q15006; O43402: EMC8; NbExp=17; IntAct=EBI-359031, EBI-741841;
CC       Q15006; Q9Y3B6: EMC9; NbExp=14; IntAct=EBI-359031, EBI-748366;
CC       Q15006; Q96GW1: HSP90B1; NbExp=3; IntAct=EBI-359031, EBI-12885352;
CC       Q15006; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-359031, EBI-747204;
CC       Q15006; Q8N4V1: MMGT1; NbExp=13; IntAct=EBI-359031, EBI-6163737;
CC       Q15006; Q9Y5F1: PCDHB12; NbExp=3; IntAct=EBI-359031, EBI-12012016;
CC       Q15006; Q7L8J4: SH3BP5L; NbExp=3; IntAct=EBI-359031, EBI-747389;
CC       Q15006; Q9UHA2: SS18L2; NbExp=3; IntAct=EBI-359031, EBI-10962400;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:22119785}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176}; Cytoplasmic
CC       side {ECO:0000269|PubMed:22119785, ECO:0000269|PubMed:32439656}.
CC       Note=May also localize to the nuclear envelope.
CC       {ECO:0000250|UniProtKB:Q9CRD2}.
CC   -!- PTM: Ubiquitinated when soluble in the cytoplasm, leading to its
CC       degradation by the proteasome (PubMed:33964204). Interaction with EMC2
CC       prevents its ubiquitination and degradation (PubMed:33964204).
CC       {ECO:0000269|PubMed:33964204}.
CC   -!- SIMILARITY: Belongs to the EMC2 family. {ECO:0000305}.
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DR   EMBL; D14659; BAA03493.1; -; mRNA.
DR   EMBL; CR457402; CAG33683.1; -; mRNA.
DR   EMBL; BC020753; AAH20753.1; -; mRNA.
DR   EMBL; BC021667; AAH21667.1; -; mRNA.
DR   CCDS; CCDS6309.1; -.
DR   RefSeq; NP_055488.1; NM_014673.5.
DR   PDB; 6WW7; EM; 3.40 A; B=1-297.
DR   PDB; 6Y4L; X-ray; 2.20 A; A=10-274.
DR   PDB; 6Z3W; EM; 6.40 A; B=1-297.
DR   PDB; 7ADO; EM; 3.39 A; B=1-297.
DR   PDB; 7ADP; EM; 3.60 A; B=1-297.
DR   PDB; 8EOI; EM; 3.40 A; B=3-293.
DR   PDB; 8J0N; EM; 3.47 A; B=1-297.
DR   PDB; 8J0O; EM; 3.32 A; B=1-297.
DR   PDB; 8S9S; EM; 3.60 A; 2=1-297.
DR   PDB; 9C7V; EM; 6.60 A; 2=1-297.
DR   PDBsum; 6WW7; -.
DR   PDBsum; 6Y4L; -.
DR   PDBsum; 6Z3W; -.
DR   PDBsum; 7ADO; -.
DR   PDBsum; 7ADP; -.
DR   PDBsum; 8EOI; -.
DR   PDBsum; 8J0N; -.
DR   PDBsum; 8J0O; -.
DR   PDBsum; 8S9S; -.
DR   PDBsum; 9C7V; -.
DR   AlphaFoldDB; Q15006; -.
DR   EMDB; EMD-11732; -.
DR   EMDB; EMD-11733; -.
DR   EMDB; EMD-21929; -.
DR   EMDB; EMD-28376; -.
DR   EMDB; EMD-35906; -.
DR   EMDB; EMD-35907; -.
DR   EMDB; EMD-40245; -.
DR   EMDB; EMD-40246; -.
DR   EMDB; EMD-45295; -.
DR   SMR; Q15006; -.
DR   BioGRID; 115046; 461.
DR   ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant.
DR   ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant.
DR   CORUM; Q15006; -.
DR   FunCoup; Q15006; 2357.
DR   IntAct; Q15006; 180.
DR   MINT; Q15006; -.
DR   NDEx; IQUERY-CP-EMC2; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000220853; -.
DR   ChEMBL; CHEMBL6066426; -.
DR   TCDB; 3.A.27.1.1; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR   GlyGen; Q15006; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q15006; -.
DR   PhosphoSitePlus; Q15006; -.
DR   SwissPalm; Q15006; -.
DR   BioMuta; EMC2; -.
DR   DMDM; 3183217; -.
DR   jPOST; Q15006; -.
DR   MassIVE; Q15006; -.
DR   PaxDb; 9606-ENSP00000220853; -.
DR   PeptideAtlas; Q15006; -.
DR   ProteomicsDB; 60357; -.
DR   Pumba; Q15006; -.
DR   Antibodypedia; 26545; 108 antibodies from 23 providers.
DR   DNASU; 9694; -.
DR   Ensembl; ENST00000220853.8; ENSP00000220853.3; ENSG00000104412.9.
DR   GeneID; 9694; -.
DR   KEGG; hsa:9694; -.
DR   MANE-Select; ENST00000220853.8; ENSP00000220853.3; NM_014673.5; NP_055488.1.
DR   UCSC; uc003ymw.2; human.
DR   AGR; HGNC:28963; -.
DR   ClinPGx; PA162407224; -.
DR   CTD; 9694; -.
DR   DisGeNET; 9694; -.
DR   GeneCards; EMC2; -.
DR   HGNC; HGNC:28963; EMC2.
DR   HPA; ENSG00000104412; Low tissue specificity.
DR   MIM; 607722; gene.
DR   OpenTargets; ENSG00000104412; -.
DR   VEuPathDB; HostDB:ENSG00000104412; -.
DR   eggNOG; KOG3060; Eukaryota.
DR   GeneTree; ENSGT00390000011922; -.
DR   HOGENOM; CLU_052388_1_0_1; -.
DR   InParanoid; Q15006; -.
DR   OMA; MSDQEGW; -.
DR   OrthoDB; 124397at2759; -.
DR   PAN-GO; Q15006; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; Q15006; -.
DR   PathwayCommons; Q15006; -.
DR   SignaLink; Q15006; -.
DR   Agora; ENSG00000104412; -.
DR   BioGRID-ORCS; 9694; 210 hits in 1178 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; EMC2; human.
DR   GeneWiki; TTC35; -.
DR   GenomeRNAi; 9694; -.
DR   Pharos; Q15006; Tbio.
DR   PRO; PR:Q15006; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q15006; protein.
DR   Bgee; ENSG00000104412; Expressed in calcaneal tendon and 209 other cell types or tissues.
DR   ExpressionAtlas; Q15006; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0072546; C:EMC complex; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; IDA:UniProtKB.
DR   GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
DR   FunFam; 1.25.40.10:FF:000074; ER membrane protein complex subunit 2; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR039856; EMC2-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR055217; TPR_EMC2.
DR   InterPro; IPR019734; TPR_rpt.
DR   PANTHER; PTHR12760; TETRATRICOPEPTIDE REPEAT PROTEIN; 1.
DR   Pfam; PF22890; TPR_EMC2; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Endoplasmic reticulum; Membrane;
KW   Proteomics identification; Reference proteome; Repeat; TPR repeat;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..297
FT                   /note="ER membrane protein complex subunit 2"
FT                   /id="PRO_0000106353"
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:0007744|PubMed:22814378"
FT   MOD_RES         255
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MUTAGEN         28
FT                   /note="R->A: Loss of interaction with EMC5."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         61
FT                   /note="I->K: No effect on transmembrane domain binding of
FT                   tail-anchored proteins; when associated with K-95 and
FT                   E-122."
FT                   /evidence="ECO:0000269|PubMed:32459176"
FT   MUTAGEN         95
FT                   /note="M->K: No effect on transmembrane domain binding of
FT                   tail-anchored proteins; when associated with K-61 and
FT                   E-122."
FT                   /evidence="ECO:0000269|PubMed:32459176"
FT   MUTAGEN         122
FT                   /note="A->E: No effect on transmembrane domain binding of
FT                   tail-anchored proteins; when associated with K-61 and
FT                   K-95."
FT                   /evidence="ECO:0000269|PubMed:32459176"
FT   MUTAGEN         156
FT                   /note="E->A: Loss of interaction with EMC5."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         160
FT                   /note="E->A: Loss of interaction with EMC5."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         171
FT                   /note="Y->A: Decreased interaction with EMC5 and EMC8."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         180
FT                   /note="E->A: Decreased interaction with EMC3."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         189..191
FT                   /note="HLY->EEK: Decreased transmembrane domain binding of
FT                   tail-anchored proteins."
FT                   /evidence="ECO:0000269|PubMed:32459176"
FT   MUTAGEN         193..194
FT                   /note="QQ->EK: No effect on transmembrane domain binding of
FT                   tail-anchored proteins."
FT                   /evidence="ECO:0000269|PubMed:32459176"
FT   MUTAGEN         200
FT                   /note="Y->A: Decreased interaction with EMC5 and EMC8."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         227
FT                   /note="R->A: Loss of interaction with EMC5 and EMC8."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   MUTAGEN         259
FT                   /note="W->A: Decreased interaction with EMC3."
FT                   /evidence="ECO:0000269|PubMed:32439656"
FT   CONFLICT        145
FT                   /note="N -> S (in Ref. 3; AAH20753)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..8
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           13..25
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           30..43
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           45..48
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           52..66
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           69..82
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           87..99
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           103..116
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           121..133
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           137..150
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           155..167
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           171..184
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           189..202
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           205..221
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   HELIX           226..240
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   STRAND          242..244
FT                   /evidence="ECO:0007829|PDB:8J0O"
FT   HELIX           247..274
FT                   /evidence="ECO:0007829|PDB:6Y4L"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:6WW7"
FT   HELIX           278..296
FT                   /evidence="ECO:0007829|PDB:8J0O"
SQ   SEQUENCE   297 AA;  34834 MW;  CA5903AEC3B3E36A CRC64;
     MAKVSELYDV TWEEMRDKMR KWREENSRNS EQIVEVGEEL INEYASKLGD 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
//