LCA5_HUMAN
ID LCA5_HUMAN Reviewed; 697 AA.
AC Q86VQ0; E1P542; Q9BWX7;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Lebercilin {ECO:0000303|PubMed:17546029};
DE AltName: Full=Leber congenital amaurosis 5 protein;
GN Name=LCA5; Synonyms=C6orf152;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-24.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-24.
RC TISSUE=Testis;
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 INVOLVEMENT IN LCA5.
RX PubMed=18000884; DOI=10.1002/humu.9513;
RA Gerber S., Hanein S., Perrault I., Delphin N., Aboussair N., Leowski C.,
RA Dufier J.-L., Roche O., Munnich A., Kaplan J., Rozet J.-M.;
RT "Mutations in LCA5 are an uncommon cause of Leber congenital amaurosis
RT (LCA) type II.";
RL Hum. Mutat. 28:1245-1245(2007).
RN [5]
RP SUBCELLULAR LOCATION, INVOLVEMENT IN LCA5, AND TISSUE SPECIFICITY.
RX PubMed=17546029; DOI=10.1038/ng2066;
RA den Hollander A.I., Koenekoop R.K., Mohamed M.D., Arts H.H., Boldt K.,
RA Towns K.V., Sedmak T., Beer M., Nagel-Wolfrum K., McKibbin M.,
RA Dharmaraj S., Lopez I., Ivings L., Williams G.A., Springell K., Woods C.G.,
RA Jafri H., Rashid Y., Strom T.M., van der Zwaag B., Gosens I.,
RA Kersten F.F.J., van Wijk E., Veltman J.A., Zonneveld M.N.,
RA van Beersum S.E.C., Maumenee I.H., Wolfrum U., Cheetham M.E., Ueffing M.,
RA Cremers F.P.M., Inglehearn C.F., Roepman R.;
RT "Mutations in LCA5, encoding the ciliary protein lebercilin, cause Leber
RT congenital amaurosis.";
RL Nat. Genet. 39:889-895(2007).
RN [6]
RP INVOLVEMENT IN LCA5.
RX PubMed=18334959;
RA Ramprasad V.L., Soumittra N., Nancarrow D., Sen P., McKibbin M.,
RA Williams G.A., Arokiasamy T., Lakshmipathy P., Inglehearn C.F.,
RA Kumaramanickavel G.;
RT "Identification of a novel splice-site mutation in the lebercilin (LCA5)
RT gene causing Leber congenital amaurosis.";
RL Mol. Vis. 14:481-486(2008).
RN [7]
RP INTERACTION WITH OFD1.
RX PubMed=19800048; DOI=10.1016/j.ajhg.2009.09.002;
RA Coene K.L., Roepman R., Doherty D., Afroze B., Kroes H.Y., Letteboer S.J.,
RA Ngu L.H., Budny B., van Wijk E., Gorden N.T., Azhimi M.,
RA Thauvin-Robinet C., Veltman J.A., Boink M., Kleefstra T., Cremers F.P.,
RA van Bokhoven H., de Brouwer A.P.;
RT "OFD1 is mutated in X-linked Joubert syndrome and interacts with LCA5-
RT encoded lebercilin.";
RL Am. J. Hum. Genet. 85:465-481(2009).
RN [8]
RP INTERACTION WITH NINL.
RX PubMed=18826961; DOI=10.1093/hmg/ddn312;
RA van Wijk E., Kersten F.F.J., Kartono A., Mans D.A., Brandwijk K.,
RA Letteboer S.J.F., Peters T.A., Maerker T., Yan X., Cremers C.W.R.J.,
RA Cremers F.P.M., Wolfrum U., Roepman R., Kremer H.;
RT "Usher syndrome and Leber congenital amaurosis are molecularly linked via a
RT novel isoform of the centrosomal ninein-like protein.";
RL Hum. Mol. Genet. 18:51-64(2009).
RN [9]
RP INTERACTION WITH FAM161A.
RX PubMed=22940612; DOI=10.1093/hmg/dds368;
RA Di Gioia S.A., Letteboer S.J., Kostic C., Bandah-Rozenfeld D.,
RA Hetterschijt L., Sharon D., Arsenijevic Y., Roepman R., Rivolta C.;
RT "FAM161A, associated with retinitis pigmentosa, is a component of the
RT cilia-basal body complex and interacts with proteins involved in
RT ciliopathies.";
RL Hum. Mol. Genet. 21:5174-5184(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH COMPONENTS OF THE IFT COMPLEX B.
RX PubMed=21606596; DOI=10.1172/jci45627;
RA Boldt K., Mans D.A., Won J., van Reeuwijk J., Vogt A., Kinkl N.,
RA Letteboer S.J., Hicks W.L., Hurd R.E., Naggert J.K., Texier Y.,
RA den Hollander A.I., Koenekoop R.K., Bennett J., Cremers F.P.,
RA Gloeckner C.J., Nishina P.M., Roepman R., Ueffing M.;
RT "Disruption of intraflagellar protein transport in photoreceptor cilia
RT causes Leber congenital amaurosis in humans and mice.";
RL J. Clin. Invest. 121:2169-2180(2011).
RN [12]
RP VARIANT LCA5 GLY-218.
RX PubMed=28418496; DOI=10.1167/iovs.17-21424;
RA Li L., Chen Y., Jiao X., Jin C., Jiang D., Tanwar M., Ma Z., Huang L.,
RA Ma X., Sun W., Chen J., Ma Y., M'hamdi O., Govindarajan G., Cabrera P.E.,
RA Li J., Gupta N., Naeem M.A., Khan S.N., Riazuddin S., Akram J.,
RA Ayyagari R., Sieving P.A., Riazuddin S.A., Hejtmancik J.F.;
RT "Homozygosity Mapping and Genetic Analysis of Autosomal Recessive Retinal
RT Dystrophies in 144 Consanguineous Pakistani Families.";
RL Invest. Ophthalmol. Vis. Sci. 58:2218-2238(2017).
CC -!- FUNCTION: Involved in intraflagellar protein (IFT) transport in
CC photoreceptor cilia. {ECO:0000250|UniProtKB:Q80ST9}.
CC -!- SUBUNIT: Interacts with NINL (PubMed:18826961). Interacts with OFD1
CC (PubMed:19800048). Interacts with FAM161A (PubMed:22940612). Interacts
CC with components of the IFT complex B (PubMed:21606596).
CC {ECO:0000269|PubMed:18826961, ECO:0000269|PubMed:19800048,
CC ECO:0000269|PubMed:21606596, ECO:0000269|PubMed:22940612}.
CC -!- INTERACTION:
CC Q86VQ0; Q96CN9: GCC1; NbExp=3; IntAct=EBI-6658186, EBI-746252;
CC Q86VQ0; Q9P2K3: RCOR3; NbExp=3; IntAct=EBI-6658186, EBI-743428;
CC Q86VQ0; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-6658186, EBI-1504830;
CC Q86VQ0; O43805: SSNA1; NbExp=3; IntAct=EBI-6658186, EBI-2515299;
CC Q86VQ0; Q9UMX1: SUFU; NbExp=3; IntAct=EBI-6658186, EBI-740595;
CC Q86VQ0; Q9UBB9: TFIP11; NbExp=4; IntAct=EBI-6658186, EBI-1105213;
CC Q86VQ0; P40222: TXLNA; NbExp=3; IntAct=EBI-6658186, EBI-359793;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17546029}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:17546029}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:17546029}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:17546029}. Cell projection, cilium
CC {ECO:0000269|PubMed:21606596}. Note=In non- ciliated cells, localizes
CC to the centrosome and its associated microtubule array
CC (PubMed:17546029). Colocalizes with IFT complex A and B proteins in the
CC connecting cilium in primary cilia of hTERT-RPE1 cells
CC (PubMed:21606596). {ECO:0000269|PubMed:17546029,
CC ECO:0000269|PubMed:21606596}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17546029}.
CC -!- DISEASE: Leber congenital amaurosis 5 (LCA5) [MIM:604537]: A severe
CC dystrophy of the retina, typically becoming evident in the first years
CC of life. Visual function is usually poor and often accompanied by
CC nystagmus, sluggish or near-absent pupillary responses, photophobia,
CC high hyperopia and keratoconus. {ECO:0000269|PubMed:17546029,
CC ECO:0000269|PubMed:18000884, ECO:0000269|PubMed:18334959,
CC ECO:0000269|PubMed:28418496}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the LCA5 family. {ECO:0000305}.
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DR EMBL; AL391840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48705.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48706.1; -; Genomic_DNA.
DR EMBL; BC050327; AAH50327.1; -; mRNA.
DR CCDS; CCDS4990.1; -.
DR RefSeq; NP_001116241.1; NM_001122769.2.
DR RefSeq; NP_859065.2; NM_181714.3.
DR RefSeq; XP_005248722.1; XM_005248665.4.
DR RefSeq; XP_011533806.1; XM_011535504.1.
DR AlphaFoldDB; Q86VQ0; -.
DR SMR; Q86VQ0; -.
DR BioGRID; 127950; 125.
DR IntAct; Q86VQ0; 119.
DR STRING; 9606.ENSP00000376686; -.
DR iPTMnet; Q86VQ0; -.
DR PhosphoSitePlus; Q86VQ0; -.
DR BioMuta; LCA5; -.
DR DMDM; 71658798; -.
DR EPD; Q86VQ0; -.
DR jPOST; Q86VQ0; -.
DR MassIVE; Q86VQ0; -.
DR MaxQB; Q86VQ0; -.
DR PaxDb; Q86VQ0; -.
DR PeptideAtlas; Q86VQ0; -.
DR PRIDE; Q86VQ0; -.
DR ProteomicsDB; 70054; -.
DR Antibodypedia; 31597; 135 antibodies from 24 providers.
DR DNASU; 167691; -.
DR Ensembl; ENST00000369846.9; ENSP00000358861.4; ENSG00000135338.14.
DR Ensembl; ENST00000392959.5; ENSP00000376686.1; ENSG00000135338.14.
DR GeneID; 167691; -.
DR KEGG; hsa:167691; -.
DR MANE-Select; ENST00000369846.9; ENSP00000358861.4; NM_001122769.3; NP_001116241.1.
DR UCSC; uc003pix.4; human.
DR CTD; 167691; -.
DR DisGeNET; 167691; -.
DR GeneCards; LCA5; -.
DR HGNC; HGNC:31923; LCA5.
DR HPA; ENSG00000135338; Low tissue specificity.
DR MalaCards; LCA5; -.
DR MIM; 604537; phenotype.
DR MIM; 611408; gene.
DR neXtProt; NX_Q86VQ0; -.
DR OpenTargets; ENSG00000135338; -.
DR Orphanet; 65; Leber congenital amaurosis.
DR Orphanet; 364055; Severe early-childhood-onset retinal dystrophy.
DR PharmGKB; PA142671563; -.
DR VEuPathDB; HostDB:ENSG00000135338; -.
DR eggNOG; ENOG502QQG3; Eukaryota.
DR GeneTree; ENSGT00560000077266; -.
DR HOGENOM; CLU_017042_0_0_1; -.
DR InParanoid; Q86VQ0; -.
DR OMA; SGKSNPF; -.
DR OrthoDB; 344288at2759; -.
DR PhylomeDB; Q86VQ0; -.
DR TreeFam; TF323306; -.
DR PathwayCommons; Q86VQ0; -.
DR SignaLink; Q86VQ0; -.
DR BioGRID-ORCS; 167691; 5 hits in 1073 CRISPR screens.
DR GeneWiki; LCA5; -.
DR GenomeRNAi; 167691; -.
DR Pharos; Q86VQ0; Tbio.
DR PRO; PR:Q86VQ0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q86VQ0; protein.
DR Bgee; ENSG00000135338; Expressed in mucosa of paranasal sinus and 148 other tissues.
DR ExpressionAtlas; Q86VQ0; baseline and differential.
DR Genevisible; Q86VQ0; HS.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR026684; Lebercilin.
DR InterPro; IPR026188; Lebercilin-like.
DR InterPro; IPR028933; Lebercilin_dom.
DR PANTHER; PTHR16650; PTHR16650; 1.
DR PANTHER; PTHR16650:SF10; PTHR16650:SF10; 1.
DR Pfam; PF15619; Lebercilin; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Leber congenital amaurosis; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..697
FT /note="Lebercilin"
FT /id="PRO_0000089546"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 103..297
FT /evidence="ECO:0000255"
FT COILED 389..485
FT /evidence="ECO:0000255"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80ST9"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 24
FT /note="L -> S (in dbSNP:rs2655655)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_023094"
FT VARIANT 26
FT /note="D -> A (in dbSNP:rs34068461)"
FT /id="VAR_038989"
FT VARIANT 66
FT /note="R -> Q (in dbSNP:rs35338066)"
FT /id="VAR_038990"
FT VARIANT 218
FT /note="R -> G (in LCA5; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:28418496"
FT /id="VAR_081583"
FT VARIANT 546
FT /note="A -> P (in dbSNP:rs35415141)"
FT /id="VAR_038991"
FT VARIANT 656
FT /note="G -> D (in dbSNP:rs1875845)"
FT /id="VAR_038992"
FT CONFLICT 15
FT /note="K -> E (in Ref. 3; AAH50327)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="P -> R (in Ref. 3; AAH50327)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="D -> G (in Ref. 3; AAH50327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 697 AA; 80554 MW; A8F8AB1A565EB633 CRC64;
MGERAGSPGT DQERKAGKHH YSYLSDFETP QSSGRSSLVS SSPASVRRKN PKRQTSDGQV
HHQAPRKPSP KGLPNRKGVR VGFRSQSLNR EPLRKDTDLV TKRILSARLL KINELQNEVS
ELQVKLAELL KENKSLKRLQ YRQEKALNKF EDAENEISQL IFRHNNEITA LKERLRKSQE
KERATEKRVK DTESELFRTK FSLQKLKEIS EARHLPERDD LAKKLVSAEL KLDDTERRIK
ELSKNLELST NSFQRQLLAE RKRAYEAHDE NKVLQKEVQR LYHKLKEKER ELDIKNIYSN
RLPKSSPNKE KELALRKNAA CQSDFADLCT KGVQTMEDFK PEEYPLTPET IMCYENKWEE
PGHLTLDLQS QKQDRHGEAG ILNPIMEREE KFVTDEELHV VKQEVEKLED EWEREELDKK
QKEKASLLER EEKPEWETGR YQLGMYPIQN MDKLQGEEEE RLKREMLLAK LNEIDRELQD
SRNLKYPVLP LLPDFESKLH SPERSPKTYR FSESSERLFN GHHLQDISFS TPKGEGQNSG
NVRSPASPNE FAFGSYVPSF AKTSERSNPF SQKSSFLDFQ RNSMEKLSKD GVDLITRKEK
KANLMEQLFG ASGSSTISSK SSDPNSVASS KGDIDPLNFL PGNKGSRDQE HDEDEGFFLS
EGRSFNPNRH RLKHADDKPA VKAADSVEDE IEEVALR
