EMC3_HUMAN
ID EMC3_HUMAN Reviewed; 261 AA.
AC Q9P0I2; B2R4Z9; Q53GH8; Q6ZMC2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ER membrane protein complex subunit 3;
DE AltName: Full=Transmembrane protein 111;
GN Name=EMC3; Synonyms=TMEM111;
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] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Stomach cancer;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP PROTEIN SEQUENCE OF 2-13; 140-147 AND 181-197, CLEAVAGE OF INITIATOR
RP METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [7]
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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
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 [12]
RP FUNCTION, AND SUBUNIT.
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 [13]
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 [14] {ECO:0007744|PDB:6Z3W}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) OF THE EMC COMPLEX, AND
RP FUNCTION.
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 [15] {ECO:0007744|PDB:6WW7}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF THE EMC COMPLEX,
RP FUNCTION, TOPOLOGY, AND MUTAGENESIS OF ARG-31; MET-101; MET-106; MET-110;
RP MET-111; PHE-173 AND ARG-180.
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:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176,
CC PubMed:32439656). Preferentially accommodates proteins with
CC transmembrane domains that are weakly hydrophobic or contain
CC destabilizing features such as charged and aromatic residues
CC (PubMed:30415835, PubMed:29809151, PubMed:29242231). 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:30415835, PubMed:29809151). It is also required for the
CC post-translational insertion of tail-anchored/TA proteins in
CC endoplasmic reticulum membranes (PubMed:29809151, PubMed:29242231). 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:0000305}.
CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC {ECO:0000269|PubMed:22119785, ECO:0000269|PubMed:29242231,
CC ECO:0000269|PubMed:29809151, ECO:0000269|PubMed:32439656,
CC ECO:0000269|PubMed:32459176}.
CC -!- INTERACTION:
CC Q9P0I2; Q15006: EMC2; NbExp=7; IntAct=EBI-1054670, EBI-359031;
CC Q9P0I2; Q13126: MTAP; NbExp=3; IntAct=EBI-1054670, EBI-2547776;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22119785}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:32439656}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P0I2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P0I2-2; Sequence=VSP_014886;
CC -!- SIMILARITY: Belongs to the EMC3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD18807.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF157321; AAF67487.1; -; mRNA.
DR EMBL; AK172843; BAD18807.1; ALT_SEQ; mRNA.
DR EMBL; AK222953; BAD96673.1; -; mRNA.
DR EMBL; AK312008; BAG34946.1; -; mRNA.
DR EMBL; CH471055; EAW64047.1; -; Genomic_DNA.
DR EMBL; BC022807; AAH22807.1; -; mRNA.
DR CCDS; CCDS2594.1; -. [Q9P0I2-1]
DR RefSeq; NP_060917.1; NM_018447.3. [Q9P0I2-1]
DR PDB; 6WW7; EM; 3.40 A; C=1-261.
DR PDB; 6Z3W; EM; 6.40 A; C=1-261.
DR PDB; 7ADO; EM; 3.39 A; C=1-261.
DR PDB; 7ADP; EM; 3.60 A; C=1-261.
DR PDBsum; 6WW7; -.
DR PDBsum; 6Z3W; -.
DR PDBsum; 7ADO; -.
DR PDBsum; 7ADP; -.
DR AlphaFoldDB; Q9P0I2; -.
DR SMR; Q9P0I2; -.
DR BioGRID; 120936; 105.
DR ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant.
DR IntAct; Q9P0I2; 44.
DR MINT; Q9P0I2; -.
DR STRING; 9606.ENSP00000245046; -.
DR TCDB; 3.A.27.1.1; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR iPTMnet; Q9P0I2; -.
DR MetOSite; Q9P0I2; -.
DR PhosphoSitePlus; Q9P0I2; -.
DR BioMuta; EMC3; -.
DR DMDM; 71153383; -.
DR EPD; Q9P0I2; -.
DR jPOST; Q9P0I2; -.
DR MassIVE; Q9P0I2; -.
DR MaxQB; Q9P0I2; -.
DR PaxDb; Q9P0I2; -.
DR PeptideAtlas; Q9P0I2; -.
DR PRIDE; Q9P0I2; -.
DR ProteomicsDB; 83550; -. [Q9P0I2-1]
DR ProteomicsDB; 83551; -. [Q9P0I2-2]
DR TopDownProteomics; Q9P0I2-1; -. [Q9P0I2-1]
DR TopDownProteomics; Q9P0I2-2; -. [Q9P0I2-2]
DR Antibodypedia; 49265; 63 antibodies from 15 providers.
DR DNASU; 55831; -.
DR Ensembl; ENST00000245046.7; ENSP00000245046.2; ENSG00000125037.13. [Q9P0I2-1]
DR Ensembl; ENST00000470827.3; ENSP00000474771.2; ENSG00000125037.13. [Q9P0I2-1]
DR GeneID; 55831; -.
DR KEGG; hsa:55831; -.
DR MANE-Select; ENST00000245046.7; ENSP00000245046.2; NM_001394674.1; NP_001381603.1.
DR UCSC; uc003bun.4; human. [Q9P0I2-1]
DR CTD; 55831; -.
DR DisGeNET; 55831; -.
DR GeneCards; EMC3; -.
DR HGNC; HGNC:23999; EMC3.
DR HPA; ENSG00000125037; Low tissue specificity.
DR neXtProt; NX_Q9P0I2; -.
DR OpenTargets; ENSG00000125037; -.
DR PharmGKB; PA142670762; -.
DR VEuPathDB; HostDB:ENSG00000125037; -.
DR eggNOG; KOG3188; Eukaryota.
DR GeneTree; ENSGT00390000005780; -.
DR HOGENOM; CLU_060791_0_0_1; -.
DR InParanoid; Q9P0I2; -.
DR OMA; WYFLTLF; -.
DR OrthoDB; 1482782at2759; -.
DR PhylomeDB; Q9P0I2; -.
DR PathwayCommons; Q9P0I2; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR SignaLink; Q9P0I2; -.
DR BioGRID-ORCS; 55831; 495 hits in 1091 CRISPR screens.
DR ChiTaRS; EMC3; human.
DR GenomeRNAi; 55831; -.
DR Pharos; Q9P0I2; Tbio.
DR PRO; PR:Q9P0I2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9P0I2; protein.
DR Bgee; ENSG00000125037; Expressed in triceps brachii and 205 other tissues.
DR ExpressionAtlas; Q9P0I2; baseline and differential.
DR Genevisible; Q9P0I2; HS.
DR GO; GO:0072546; C:EMC complex; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; IDA:ComplexPortal.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
DR InterPro; IPR008568; EMC3.
DR InterPro; IPR002809; EMC3/TMCO1.
DR PANTHER; PTHR13116; PTHR13116; 1.
DR Pfam; PF01956; EMC3_TMCO1; 1.
DR PIRSF; PIRSF010045; DUF850_TM_euk; 1.
DR SMART; SM01415; DUF106; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..261
FT /note="ER membrane protein complex subunit 3"
FT /id="PRO_0000211406"
FT TOPO_DOM 2..14
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:32439656"
FT TRANSMEM 15..38
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:32439656"
FT TOPO_DOM 39..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32439656"
FT TRANSMEM 115..130
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:32439656"
FT TOPO_DOM 131..168
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:32439656"
FT TRANSMEM 169..187
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:32439656"
FT TOPO_DOM 188..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32439656"
FT VAR_SEQ 220..261
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_014886"
FT MUTAGEN 31
FT /note="R->A,E: No effect on EMC assembly but decreased
FT membrane insertion of hydrophobic transmembrane helices-
FT containing proteins by the EMC."
FT /evidence="ECO:0000269|PubMed:32439656"
FT MUTAGEN 31
FT /note="R->K: No effect on EMC assembly and no effect on
FT membrane insertion of hydrophobic transmembrane helices-
FT containing proteins by the EMC."
FT /evidence="ECO:0000269|PubMed:32439656"
FT MUTAGEN 101
FT /note="M->S: No effect on EMC assembly but decreased
FT membrane insertion of hydrophobic transmembrane helices-
FT containing proteins by the EMC; when associated S-106, S-
FT 110 and S-111."
FT /evidence="ECO:0000269|PubMed:32439656"
FT MUTAGEN 106
FT /note="M->S: No effect on EMC assembly but decreased
FT membrane insertion of hydrophobic transmembrane helices-
FT containing proteins by the EMC; when associated S-101, S-
FT 110 and S-111."
FT /evidence="ECO:0000269|PubMed:32439656"
FT MUTAGEN 110
FT /note="M->S: No effect on EMC assembly but decreased
FT membrane insertion of hydrophobic transmembrane helices-
FT containing proteins by the EMC; when associated S-101, S-
FT 106 and S-111."
FT /evidence="ECO:0000269|PubMed:32439656"
FT MUTAGEN 111
FT /note="M->S: No effect on EMC assembly but decreased
FT membrane insertion of hydrophobic transmembrane helices-
FT containing proteins by the EMC; when associated S-101, S-
FT 106 and S-110."
FT /evidence="ECO:0000269|PubMed:32439656"
FT MUTAGEN 173
FT /note="F->A: No effect on EMC assembly and no effect on
FT membrane insertion of hydrophobic transmembrane helices-
FT containing proteins by the EMC."
FT /evidence="ECO:0000269|PubMed:32439656"
FT MUTAGEN 180
FT /note="R->A,E: No effect on EMC assembly but decreased
FT membrane insertion of hydrophobic transmembrane helices-
FT containing proteins by the EMC."
FT /evidence="ECO:0000269|PubMed:32439656"
FT MUTAGEN 180
FT /note="R->K: No effect on EMC assembly and no effect on
FT membrane insertion of hydrophobic transmembrane helices-
FT containing proteins by the EMC."
FT /evidence="ECO:0000269|PubMed:32439656"
FT CONFLICT 29
FT /note="M -> T (in Ref. 2; BAD18807)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="V -> I (in Ref. 3; BAD96673)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="Y -> H (in Ref. 2; BAD18807)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="G -> D (in Ref. 2; BAD18807)"
FT /evidence="ECO:0000305"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 18..38
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 46..64
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6WW7"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:6WW7"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:7ADO"
SQ SEQUENCE 261 AA; 29952 MW; 0FB279E54D6C1FCC CRC64;
MAGPELLLDS NIRLWVVLPI VIITFFVGMI RHYVSILLQS DKKLTQEQVS DSQVLIRSRV
LRENGKYIPK QSFLTRKYYF NNPEDGFFKK TKRKVVPPSP MTDPTMLTDM MKGNVTNVLP
MILIGGWINM TFSGFVTTKV PFPLTLRFKP MLQQGIELLT LDASWVSSAS WYFLNVFGLR
SIYSLILGQD NAADQSRMMQ EQMTGAAMAM PADTNKAFKT EWEALELTDH QWALDDVEEE
LMAKDLHFEG MFKKELQTSI F
