OPA1_RAT
ID OPA1_RAT Reviewed; 960 AA.
AC Q2TA68; O08681; Q5MPP1; Q5MPP2; Q5QJE9; Q6B435; Q6R611;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Dynamin-like 120 kDa protein, mitochondrial;
DE EC=3.6.5.5;
DE AltName: Full=Optic atrophy protein 1 homolog;
DE Contains:
DE RecName: Full=Dynamin-like 120 kDa protein, form S1;
DE Flags: Precursor;
GN Name=Opa1 {ECO:0000312|EMBL:AAI11072.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAR04100.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE SPECIFICITY.
RC TISSUE=Retinal ganglion {ECO:0000269|PubMed:15505078};
RX PubMed=15505078; DOI=10.1167/iovs.03-1261;
RA Pesch U.E.A., Fries J.E., Bette S., Kalbacher H., Wissinger B.,
RA Alexander C., Kohler K.;
RT "OPA1, the disease gene for autosomal dominant optic atrophy, is
RT specifically expressed in ganglion cells and intrinsic neurons of the
RT retina.";
RL Invest. Ophthalmol. Vis. Sci. 45:4217-4225(2004).
RN [2] {ECO:0000312|EMBL:AAS79791.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:AAS79791.1};
RX PubMed=16249510; DOI=10.1167/iovs.03-1407;
RA Kamei S., Chen-Kuo-Chang M., Cazevieille C., Lenaers G., Olichon A.,
RA Belenguer P., Roussignol G., Renard N., Eybalin M., Michelin A.,
RA Delettre C., Brabet P., Hamel C.P.;
RT "Expression of the Opa1 mitochondrial protein in retinal ganglion cells:
RT its downregulation causes aggregation of the mitochondrial network.";
RL Invest. Ophthalmol. Vis. Sci. 46:4288-4294(2005).
RN [3] {ECO:0000312|EMBL:AAI11072.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver {ECO:0000312|EMBL:AAI11072.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAT92526.1}
RP PROTEIN SEQUENCE OF 302-312; 416-423; 446-460; 801-818 AND 825-834, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAB51724.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 556-960.
RC STRAIN=R21 {ECO:0000312|EMBL:AAB51724.1};
RC TISSUE=Spleen {ECO:0000312|EMBL:AAB51724.1};
RA Yuan X.J., Salgar S.K., Kunz H.W., Gill T.J. III;
RT "A novel gene in the rat genome.";
RL Rat Genome 2:150-153(1996).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAT92526.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 686-788.
RC STRAIN=OFA {ECO:0000312|EMBL:AAT92526.1}; TISSUE=Intestine;
RA Fabregas P.J., Nebot-Cegarra J., Capella G., Peinado M.A.;
RT "Differential gene expression in gut during rat fetal period.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305}
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16778770; DOI=10.1038/sj.emboj.7601184;
RA Ishihara N., Fujita Y., Oka T., Mihara K.;
RT "Regulation of mitochondrial morphology through proteolytic cleavage of
RT OPA1.";
RL EMBO J. 25:2966-2977(2006).
CC -!- FUNCTION: Dynamin-related GTPase that is essential for normal
CC mitochondrial morphology by regulating the equilibrium between
CC mitochondrial fusion and mitochondrial fission (PubMed:16778770).
CC Coexpression of isoform 1 with shorter alternative products is required
CC for optimal activity in promoting mitochondrial fusion. Binds lipid
CC membranes enriched in negatively charged phospholipids, such as
CC cardiolipin, and promotes membrane tubulation. The intrinsic GTPase
CC activity is low, and is strongly increased by interaction with lipid
CC membranes (By similarity). Plays a role in remodeling cristae and the
CC release of cytochrome c during apoptosis (By similarity). Proteolytic
CC processing in response to intrinsic apoptotic signals may lead to
CC disassembly of OPA1 oligomers and release of the caspase activator
CC cytochrome C (CYCS) into the mitochondrial intermembrane space (By
CC similarity). Plays a role in mitochondrial genome maintenance (By
CC similarity). {ECO:0000250|UniProtKB:O60313,
CC ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:16778770}.
CC -!- FUNCTION: [Dynamin-like 120 kDa protein, form S1]: Inactive form
CC produced by cleavage at S1 position by OMA1 following stress conditions
CC that induce loss of mitochondrial membrane potential, leading to
CC negative regulation of mitochondrial fusion.
CC {ECO:0000250|UniProtKB:O60313, ECO:0000250|UniProtKB:P58281}.
CC -!- FUNCTION: Isoforms that contain the alternative exon 4b (present in
CC isoform 2 and isoform 3, but not in isoform 1) are required for
CC mitochondrial genome maintenance, possibly by anchoring the
CC mitochondrial nucleoids to the inner mitochondrial membrane.
CC {ECO:0000250|UniProtKB:O60313}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC Evidence={ECO:0000250|UniProtKB:O60313};
CC -!- ACTIVITY REGULATION: Activated by guanine nucleotide exchange factor
CC RCC1L. {ECO:0000250|UniProtKB:O60313}.
CC -!- SUBUNIT: Oligomeric complex consisting of membrane-bound and soluble
CC forms of OPA1. Interacts with CHCHD3 and IMMT; these interactions occur
CC preferentially with soluble OPA1 forms. Interacts with RCC1L; this
CC interaction is direct (By similarity). Binds PARL (By similarity).
CC Interacts with PRELID1 (By similarity). {ECO:0000250|UniProtKB:O60313,
CC ECO:0000250|UniProtKB:P58281}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16778770}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:P58281}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:O60313}. Note=Detected at contact sites between
CC endoplasmic reticulum and mitochondrion membranes.
CC {ECO:0000250|UniProtKB:O60313}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms may exist. {ECO:0000305};
CC Name=1 {ECO:0000303|PubMed:15505078};
CC IsoId=Q2TA68-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:15505078};
CC IsoId=Q2TA68-2; Sequence=VSP_052186, VSP_052187;
CC Name=3 {ECO:0000303|PubMed:15505078}; Synonyms=7
CC {ECO:0000303|PubMed:16778770};
CC IsoId=Q2TA68-3; Sequence=VSP_052187;
CC -!- TISSUE SPECIFICITY: Expressed in brain as well as retinal ganglion,
CC starbust amacrine and horizontal cells of the retina. Absent from nerve
CC fibers and photoreceptor cells of the retina.
CC {ECO:0000269|PubMed:15505078}.
CC -!- PTM: PARL-dependent proteolytic processing releases an antiapoptotic
CC soluble form not required for mitochondrial fusion. Cleaved by OMA1 at
CC position S1 following stress conditions.
CC {ECO:0000250|UniProtKB:O60313}.
CC -!- PTM: [Isoform 2]: Cleavage at position S2 is mediated by YME1L.
CC Cleavage may occur in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln
CC (LQQQIQ). {ECO:0000305|PubMed:16778770}.
CC -!- PTM: [Isoform 3]: Cleavage at position S2 is mediated by YME1L.
CC Cleavage may occur in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln
CC (LQQQIQ). {ECO:0000305|PubMed:16778770}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51724.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY333988; AAR04100.1; -; mRNA.
DR EMBL; AY660011; AAV97815.1; -; mRNA.
DR EMBL; AY660012; AAV97816.1; -; mRNA.
DR EMBL; AY510274; AAS79791.1; -; mRNA.
DR EMBL; BC111071; AAI11072.1; -; mRNA.
DR EMBL; U93197; AAB51724.1; ALT_INIT; mRNA.
DR EMBL; AY683458; AAT92526.1; -; mRNA.
DR RefSeq; NP_598269.3; NM_133585.3. [Q2TA68-1]
DR RefSeq; XP_006248560.1; XM_006248498.1. [Q2TA68-3]
DR AlphaFoldDB; Q2TA68; -.
DR SMR; Q2TA68; -.
DR BioGRID; 251124; 4.
DR IntAct; Q2TA68; 3.
DR MINT; Q2TA68; -.
DR STRING; 10116.ENSRNOP00000059078; -.
DR iPTMnet; Q2TA68; -.
DR PhosphoSitePlus; Q2TA68; -.
DR SwissPalm; Q2TA68; -.
DR jPOST; Q2TA68; -.
DR PRIDE; Q2TA68; -.
DR Ensembl; ENSRNOT00000111984; ENSRNOP00000079139; ENSRNOG00000001717. [Q2TA68-3]
DR GeneID; 171116; -.
DR KEGG; rno:171116; -.
DR UCSC; RGD:708423; rat. [Q2TA68-1]
DR CTD; 4976; -.
DR RGD; 708423; Opa1.
DR VEuPathDB; HostDB:ENSRNOG00000001717; -.
DR eggNOG; KOG0447; Eukaryota.
DR GeneTree; ENSGT00550000074851; -.
DR HOGENOM; CLU_012302_0_0_1; -.
DR InParanoid; Q2TA68; -.
DR OMA; IRKQWKL; -.
DR OrthoDB; 609213at2759; -.
DR Reactome; R-RNO-169911; Regulation of Apoptosis.
DR PRO; PR:Q2TA68; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001717; Expressed in heart and 19 other tissues.
DR Genevisible; Q2TA68; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0030061; C:mitochondrial crista; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:1901612; F:cardiolipin binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0036444; P:calcium import into the mitochondrion; IMP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:1905232; P:cellular response to L-glutamate; IEP:RGD.
DR GO; GO:0090398; P:cellular senescence; ISS:ParkinsonsUK-UCL.
DR GO; GO:0090102; P:cochlea development; IEP:RGD.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:RGD.
DR GO; GO:0097749; P:membrane tubulation; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0000002; P:mitochondrial genome maintenance; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:RGD.
DR GO; GO:0007005; P:mitochondrion organization; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:ParkinsonsUK-UCL.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; IMP:RGD.
DR GO; GO:1900006; P:positive regulation of dendrite development; IMP:RGD.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:RGD.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IMP:RGD.
DR GO; GO:0014042; P:positive regulation of neuron maturation; IMP:RGD.
DR GO; GO:0051259; P:protein complex oligomerization; ISO:RGD.
DR GO; GO:1904643; P:response to curcumin; IEP:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; IEP:RGD.
DR GO; GO:0007601; P:visual perception; ISS:ParkinsonsUK-UCL.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR033047; Opa1.
DR InterPro; IPR045817; OPA1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR PANTHER; PTHR11566:SF67; PTHR11566:SF67; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF19434; OPA1_C; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Coiled coil;
KW Direct protein sequencing; GTP-binding; Hydrolase; Lipid-binding; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Sensory transduction; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..87
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:16778770"
FT CHAIN 88..960
FT /note="Dynamin-like 120 kDa protein, mitochondrial"
FT /id="PRO_0000257994"
FT CHAIN 195..960
FT /note="Dynamin-like 120 kDa protein, form S1"
FT /evidence="ECO:0000269|PubMed:16778770,
FT ECO:0000305|PubMed:16778770"
FT /id="PRO_0000257995"
FT TOPO_DOM 88..96
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:16778770"
FT TRANSMEM 97..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..960
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:16778770"
FT DOMAIN 285..561
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 295..302
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 321..324
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 398..401
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 467..470
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 501..504
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 210..254
FT /evidence="ECO:0000255"
FT COILED 895..960
FT /evidence="ECO:0000255"
FT BINDING 295..302
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 398..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 467..470
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 194..195
FT /note="Cleavage at site S1"
FT /evidence="ECO:0000269|PubMed:16778770"
FT MOD_RES 228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60313"
FT VAR_SEQ 158
FT /note="S -> PKLVSEVIEASEPLLLLS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15505078"
FT /id="VSP_052186"
FT VAR_SEQ 209
FT /note="V -> GLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQKRKV (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15505078"
FT /id="VSP_052187"
FT CONFLICT 187
FT /note="T -> S (in Ref. 1; AAR04100)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="R -> P (in Ref. 2; AAS79791)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="E -> G (in Ref. 6; AAT92526)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="E -> G (in Ref. 6; AAT92526)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="L -> P (in Ref. 6; AAT92526)"
FT /evidence="ECO:0000305"
FT MOTIF Q2TA68-2:234..239
FT /note="LQQQIQ motif"
FT /evidence="ECO:0000269|PubMed:16778770"
FT MOTIF Q2TA68-3:217..222
FT /note="LQQQIQ motif"
FT /evidence="ECO:0000269|PubMed:16778770"
SQ SEQUENCE 960 AA; 111307 MW; 0C4BE54FCD7A53B3 CRC64;
MWRAGRAALA CEVCQSLVKH SSGVQRNVPL QKLHLVSRSI YRSHHPALKL QRPQLRTSFQ
QFSSLTNLSL HKLKLSPTKY GYQPRRNFWP ARLAARLLKL RYIILGSAVG GGYTAKKTFD
EWKDMIPDLS DYKWIVPDFI WEIDEYIDLE KIRKALPSSE DLANFAPDLD KIAESLSLLK
DFFTAGTPGE TAFRATDHGS ESDKHYRKVS DKEKIDQLQE ELLHTQLKYQ RILERLEKEN
KELRKLVLQK DDKGIHHRKL KKSLIDMYSE VLDVLSDYDA SYNTQDHLPR VVVVGDQSAG
KTSVLEMIAQ ARIFPRGSGE MMTRSPVKVT LSEGPHHVAL FKDSSREFDL TKEEDLAALR
HEIELRMRKN VKEGCTVSPE TISLNVKGPG LQRMVLVDLP GVINTVTSGM APDTKETIFS
ISKAYMQNPN AIILCIQDGS VDAERSIVTD LVSQMDPHGR RTIFVLTKVD LAEKNVASPS
RIQQIIEGKL FPMKALGYFA VVTGKGNSSE SIEAIREYEE EFFQNSKLLK TSMLKAHQVT
TRNLSLAVSD CFWKMVRESV EQQADSFKAT RFNLETEWKN NYPRLRELDR NELFEKAKNE
ILDEVISLSQ VTPKHWEEIL QQSLWERVST HVIENIYLPA AQTMNSGTFN TTVDIKLKQW
TDKQLPNKAV EVAWETLQDE FSRFMTEPKG KEHDDIFDKL KEAVKEESIK RHKWNDFAED
SLRVIQHNAL EDRSISDKQQ WDAAIYFMEE ALQGRLKDTE NAIENMIGPD WKKRWIYWKN
RTQEQCVHNE TKNELEKMLK VNDEHPAYLA SDEITTVRKN LESRGVEVDP SLIKDTWHQV
YRRHFLKTAL NHCNLCRRGF YYYQRHFIDS ELECNDVVLF WRIQRMLAIT ANTLRQQLTN
TEVRRLEKNV KEVLEDFAED GEKKVKLLTG KRVQLAEDLK KVREIQEKLD AFIEALHQEK
