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 27-MAR-2024, entry version 193.
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},
GN TTC35 {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:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176,
CC PubMed:32439656, 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: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: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=7; IntAct=EBI-359031, EBI-1054670;
CC Q15006; O43402: EMC8; NbExp=13; IntAct=EBI-359031, EBI-741841;
CC Q15006; Q9Y3B6: EMC9; NbExp=10; 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=9; 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_014673.4.
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; 8S9S; EM; 3.60 A; 2=1-297.
DR PDBsum; 6WW7; -.
DR PDBsum; 6Y4L; -.
DR PDBsum; 6Z3W; -.
DR PDBsum; 7ADO; -.
DR PDBsum; 7ADP; -.
DR PDBsum; 8EOI; -.
DR PDBsum; 8S9S; -.
DR AlphaFoldDB; Q15006; -.
DR EMDB; EMD-11732; -.
DR EMDB; EMD-11733; -.
DR EMDB; EMD-21929; -.
DR EMDB; EMD-28376; -.
DR EMDB; EMD-40245; -.
DR EMDB; EMD-40246; -.
DR SMR; Q15006; -.
DR BioGRID; 115046; 435.
DR ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant.
DR IntAct; Q15006; 130.
DR MINT; Q15006; -.
DR STRING; 9606.ENSP00000220853; -.
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 EPD; Q15006; -.
DR jPOST; Q15006; -.
DR MassIVE; Q15006; -.
DR MaxQB; Q15006; -.
DR PaxDb; 9606-ENSP00000220853; -.
DR PeptideAtlas; Q15006; -.
DR ProteomicsDB; 60357; -.
DR Pumba; Q15006; -.
DR Antibodypedia; 26545; 116 antibodies from 24 providers.
DR DNASU; 9694; -.
DR Ensembl; ENST00000220853.8; ENSP00000220853.3; ENSG00000104412.8.
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 CTD; 9694; -.
DR DisGeNET; 9694; -.
DR GeneCards; EMC2; -.
DR HGNC; HGNC:28963; EMC2.
DR HPA; ENSG00000104412; Low tissue specificity.
DR MIM; 607722; gene.
DR neXtProt; NX_Q15006; -.
DR OpenTargets; ENSG00000104412; -.
DR PharmGKB; PA162407224; -.
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; 312673at2759; -.
DR PhylomeDB; Q15006; -.
DR TreeFam; TF312997; -.
DR PathwayCommons; Q15006; -.
DR SignaLink; Q15006; -.
DR BioGRID-ORCS; 9694; 210 hits in 1178 CRISPR screens.
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 Genevisible; Q15006; HS.
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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR039856; EMC2-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12760:SF0; ER MEMBRANE PROTEIN COMPLEX SUBUNIT 2; 1.
DR PANTHER; PTHR12760; TETRATRICOPEPTIDE REPEAT PROTEIN; 1.
DR Pfam; PF14559; TPR_19; 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 Reference proteome; Repeat; TPR repeat; 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 E-
FT 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 E-
FT 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 K-
FT 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 TURN 5..7
FT /evidence="ECO:0007829|PDB:8EOI"
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 HELIX 247..274
FT /evidence="ECO:0007829|PDB:6Y4L"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6WW7"
FT HELIX 281..291
FT /evidence="ECO:0007829|PDB:7ADO"
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
//
