CALM_YEAST
ID CALM_YEAST Reviewed; 147 AA.
AC P06787; D6VQA8;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Calmodulin;
DE Short=CaM;
GN Name=CMD1; OrderedLocusNames=YBR109C; ORFNames=YBR0904;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3533275; DOI=10.1016/0092-8674(86)90599-4;
RA Davis T.N., Urdea M.S., Masiarz F.R., Thorner J.;
RT "Isolation of the yeast calmodulin gene: calmodulin is an essential
RT protein.";
RL Cell 47:423-431(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7918668; DOI=10.1016/0167-4889(94)90093-0;
RA Lukas T.J., Collinge M., Haiech J., Watterson D.M.;
RT "Gain of function mutations for yeast calmodulin and calcium dependent
RT regulation of protein kinase activity.";
RL Biochim. Biophys. Acta 1223:341-347(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP PROTEIN SEQUENCE OF 15-30 AND 128-145.
RX PubMed=3295478; DOI=10.1016/0076-6879(87)39090-1;
RA Davis T.N., Thorner J.;
RT "Isolation of the yeast calmodulin gene using synthetic oligonucleotide
RT probes.";
RL Methods Enzymol. 139:248-262(1987).
RN [8]
RP CALCIUM-BINDING DATA.
RX PubMed=1304352; DOI=10.1002/pro.5560010405;
RA Brockerhoff S.E., Edmonds C.G., Davis T.N.;
RT "Structural analysis of wild-type and mutant yeast calmodulins by limited
RT proteolysis and electrospray ionization mass spectrometry.";
RL Protein Sci. 1:504-516(1992).
RN [9]
RP MUTAGENESIS.
RX PubMed=2044154; DOI=10.1016/0092-8674(91)90547-c;
RA Geiser J.R., van Tuinen D., Brockerhoff S.E., Neff M.M., Davis T.N.;
RT "Can calmodulin function without binding calcium?";
RL Cell 65:949-959(1991).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SPC110.
RX PubMed=8247006; DOI=10.1128/mcb.13.12.7913-7924.1993;
RA Geiser J.R., Sundberg H.A., Chang B.H., Muller E.G., Davis T.N.;
RT "The essential mitotic target of calmodulin is the 110-kilodalton component
RT of the spindle pole body in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:7913-7924(1993).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE SPC110 COMPLEX.
RX PubMed=10339566; DOI=10.1073/pnas.96.11.6205;
RA Elliott S., Knop M., Schlenstedt G., Schiebel E.;
RT "Spc29p is a component of the Spc110p subcomplex and is essential for
RT spindle pole body duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6205-6210(1999).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP STRUCTURE BY NMR OF 1-78.
RX PubMed=8827436; DOI=10.1093/oxfordjournals.jbchem.a021346;
RA Ohki S.-Y., Miura K., Saito M., Nakashima K., Maekawa H., Yazawa M.,
RA Tsuda S., Hikichi K.;
RT "Secondary structure and Ca(2+)-binding property of the N-terminal half
RT domain of calmodulin from yeast Saccharomyces cerevisiae as studied by
RT NMR.";
RL J. Biochem. 119:1045-1055(1996).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels and other proteins by Ca(2+). Among the enzymes to be
CC stimulated by the calmodulin-Ca(2+) complex are a number of protein
CC kinases and phosphatases. Component of the spindle pole body (SPB)
CC required for the proper execution of spindle pole body (SPB)
CC duplication. {ECO:0000269|PubMed:10339566}.
CC -!- SUBUNIT: Component of the SPC110 complex containing at least CMD1,
CC SPC29, SPC42 and SCP110. Interacts with SPC110.
CC {ECO:0000269|PubMed:10339566, ECO:0000269|PubMed:8247006}.
CC -!- INTERACTION:
CC P06787; P23287: CNA1; NbExp=4; IntAct=EBI-3976, EBI-12771;
CC P06787; Q04439: MYO5; NbExp=8; IntAct=EBI-3976, EBI-11687;
CC P06787; P32380: SPC110; NbExp=5; IntAct=EBI-3976, EBI-12369;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:8247006}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: This protein has three functional calcium-binding sites.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M14760; AAA34504.1; -; Genomic_DNA.
DR EMBL; AF081667; AAC68888.1; -; Genomic_DNA.
DR EMBL; X78993; CAA55612.1; -; Genomic_DNA.
DR EMBL; Z35978; CAA85064.1; -; Genomic_DNA.
DR EMBL; AY558184; AAS56510.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07228.1; -; Genomic_DNA.
DR PIR; A25060; MCBY.
DR RefSeq; NP_009667.1; NM_001178457.1.
DR PDB; 1F54; NMR; -; A=2-78.
DR PDB; 1F55; NMR; -; A=2-78.
DR PDB; 1LKJ; NMR; -; A=2-147.
DR PDB; 2LHH; NMR; -; A=2-121.
DR PDB; 2LHI; NMR; -; A=2-147.
DR PDB; 6OQQ; X-ray; 2.10 A; B/D=1-147.
DR PDBsum; 1F54; -.
DR PDBsum; 1F55; -.
DR PDBsum; 1LKJ; -.
DR PDBsum; 2LHH; -.
DR PDBsum; 2LHI; -.
DR PDBsum; 6OQQ; -.
DR AlphaFoldDB; P06787; -.
DR BMRB; P06787; -.
DR SMR; P06787; -.
DR BioGRID; 32813; 1010.
DR ComplexPortal; CPX-1419; Spindle pole body central plaque complex.
DR ComplexPortal; CPX-1470; Myosin class I complex, MYO5 variant.
DR ComplexPortal; CPX-1500; Myosin class I complex, MYO3 variant.
DR ComplexPortal; CPX-1501; Myosin class V complex, MYO4 variant.
DR ComplexPortal; CPX-2225; Myosin class V complex, MYO2 variant.
DR DIP; DIP-536N; -.
DR IntAct; P06787; 68.
DR MINT; P06787; -.
DR STRING; 4932.YBR109C; -.
DR ChEMBL; CHEMBL1667687; -.
DR iPTMnet; P06787; -.
DR MaxQB; P06787; -.
DR PaxDb; P06787; -.
DR PRIDE; P06787; -.
DR TopDownProteomics; P06787; -.
DR EnsemblFungi; YBR109C_mRNA; YBR109C; YBR109C.
DR GeneID; 852406; -.
DR KEGG; sce:YBR109C; -.
DR SGD; S000000313; CMD1.
DR VEuPathDB; FungiDB:YBR109C; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000162930; -.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P06787; -.
DR OMA; SCDRHPP; -.
DR BioCyc; YEAST:G3O-29071-MON; -.
DR Reactome; R-SCE-111932; CaMK IV-mediated phosphorylation of CREB.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR Reactome; R-SCE-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-SCE-203615; eNOS activation.
DR Reactome; R-SCE-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-SCE-4086398; Ca2+ pathway.
DR Reactome; R-SCE-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SCE-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR Reactome; R-SCE-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-SCE-9619229; Activation of RAC1 downstream of NMDARs.
DR EvolutionaryTrace; P06787; -.
DR PRO; PR:P06787; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P06787; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:ComplexPortal.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005823; C:central plaque of spindle pole body; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0045160; C:myosin I complex; IPI:ComplexPortal.
DR GO; GO:0031475; C:myosin V complex; IC:ComplexPortal.
DR GO; GO:0005509; F:calcium ion binding; IDA:SGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:SGD.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:SGD.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR GO; GO:0007114; P:cell budding; IMP:SGD.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0016237; P:lysosomal microautophagy; IMP:SGD.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IMP:SGD.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IC:ComplexPortal.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:SGD.
DR GO; GO:1903525; P:regulation of membrane tubulation; IDA:SGD.
DR GO; GO:0010968; P:regulation of microtubule nucleation; IC:ComplexPortal.
DR GO; GO:0051300; P:spindle pole body organization; IMP:SGD.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR GO; GO:0030050; P:vesicle transport along actin filament; IC:ComplexPortal.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR039030; Calmodulin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23050:SF401; PTHR23050:SF401; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..147
FT /note="Calmodulin"
FT /id="PRO_0000198328"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 117..147
FT /note="EF-hand 4"
FT /evidence="ECO:0000305"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 21
FT /note="D->A: Highly reduced affinity for Ca(2+)."
FT /evidence="ECO:0000269|PubMed:2044154"
FT MUTAGEN 32
FT /note="E->V: Highly reduced affinity for Ca(2+)."
FT /evidence="ECO:0000269|PubMed:2044154"
FT MUTAGEN 57
FT /note="D->A: Highly reduced affinity for Ca(2+)."
FT /evidence="ECO:0000269|PubMed:2044154"
FT MUTAGEN 68
FT /note="E->V: Highly reduced affinity for Ca(2+)."
FT /evidence="ECO:0000269|PubMed:2044154"
FT MUTAGEN 94
FT /note="D->A: Highly reduced affinity for Ca(2+)."
FT /evidence="ECO:0000269|PubMed:2044154"
FT MUTAGEN 105
FT /note="E->V: Highly reduced affinity for Ca(2+)."
FT /evidence="ECO:0000269|PubMed:2044154"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:6OQQ"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6OQQ"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:6OQQ"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1LKJ"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:6OQQ"
SQ SEQUENCE 147 AA; 16135 MW; 819ED1AD5D9400D3 CRC64;
MSSNLTEEQI AEFKEAFALF DKDNNGSISS SELATVMRSL GLSPSEAEVN DLMNEIDVDG
NHQIEFSEFL ALMSRQLKSN DSEQELLEAF KVFDKNGDGL ISAAELKHVL TSIGEKLTDA
EVDDMLREVS DGSGEINIQQ FAALLSK
