ODAD1_HUMAN
ID ODAD1_HUMAN Reviewed; 670 AA.
AC Q96M63; Q6ZRL4; Q96M06; Q9UFG8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Outer dynein arm-docking complex subunit 1;
DE AltName: Full=Coiled-coil domain-containing protein 114;
GN Name=ODAD1 {ECO:0000312|HGNC:HGNC:26560}; Synonyms=CCDC114;
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=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 234-670 (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INVOLVEMENT IN CILD20.
RX PubMed=23261303; DOI=10.1016/j.ajhg.2012.11.002;
RA Onoufriadis A., Paff T., Antony D., Shoemark A., Micha D., Kuyt B.,
RA Schmidts M., Petridi S., Dankert-Roelse J.E., Haarman E.G., Daniels J.M.,
RA Emes R.D., Wilson R., Hogg C., Scambler P.J., Chung E.M., Pals G.,
RA Mitchison H.M.;
RT "Splice-Site mutations in the axonemal outer dynein arm docking complex
RT gene CCDC114 cause primary ciliary dyskinesia.";
RL Am. J. Hum. Genet. 92:88-98(2013).
RN [6]
RP FUNCTION, AND INVOLVEMENT IN CILD20.
RX PubMed=23261302; DOI=10.1016/j.ajhg.2012.11.003;
RA Knowles M.R., Leigh M.W., Ostrowski L.E., Huang L., Carson J.L.,
RA Hazucha M.J., Yin W., Berg J.S., Davis S.D., Dell S.D., Ferkol T.W.,
RA Rosenfeld M., Sagel S.D., Milla C.E., Olivier K.N., Turner E.H.,
RA Lewis A.P., Bamshad M.J., Nickerson D.A., Shendure J., Zariwala M.A.;
RT "Exome sequencing identifies mutations in CCDC114 as a cause of primary
RT ciliary dyskinesia.";
RL Am. J. Hum. Genet. 92:99-106(2013).
RN [7]
RP INTERACTION WITH ODAD3, AND SUBCELLULAR LOCATION.
RX PubMed=25192045; DOI=10.1016/j.ajhg.2014.08.005;
RG UK10K Consortium;
RA Hjeij R., Onoufriadis A., Watson C.M., Slagle C.E., Klena N.T.,
RA Dougherty G.W., Kurkowiak M., Loges N.T., Diggle C.P., Morante N.F.,
RA Gabriel G.C., Lemke K.L., Li Y., Pennekamp P., Menchen T., Konert F.,
RA Marthin J.K., Mans D.A., Letteboer S.J., Werner C., Burgoyne T.,
RA Westermann C., Rutman A., Carr I.M., O'Callaghan C., Moya E., Chung E.M.,
RA Sheridan E., Nielsen K.G., Roepman R., Bartscherer K., Burdine R.D.,
RA Lo C.W., Omran H., Mitchison H.M.;
RT "CCDC151 mutations cause primary ciliary dyskinesia by disruption of the
RT outer dynein arm docking complex formation.";
RL Am. J. Hum. Genet. 95:257-274(2014).
RN [8]
RP INTERACTION WITH ODAD4, AND SUBUNIT.
RX PubMed=27486780; DOI=10.1016/j.ajhg.2016.06.014;
RA Wallmeier J., Shiratori H., Dougherty G.W., Edelbusch C., Hjeij R.,
RA Loges N.T., Menchen T., Olbrich H., Pennekamp P., Raidt J., Werner C.,
RA Minegishi K., Shinohara K., Asai Y., Takaoka K., Lee C., Griese M.,
RA Memari Y., Durbin R., Kolb-Kokocinski A., Sauer S., Wallingford J.B.,
RA Hamada H., Omran H.;
RT "TTC25 deficiency results in defects of the outer dynein arm docking
RT machinery and primary ciliary dyskinesia with left-right body asymmetry
RT randomization.";
RL Am. J. Hum. Genet. 99:460-469(2016).
RN [9]
RP INTERACTION WITH DNAH9.
RX PubMed=30471718; DOI=10.1016/j.ajhg.2018.10.020;
RA Loges N.T., Antony D., Maver A., Deardorff M.A., Guelec E.Y., Gezdirici A.,
RA Noethe-Menchen T., Hoeben I.M., Jelten L., Frank D., Werner C., Tebbe J.,
RA Wu K., Goldmuntz E., Cuturilo G., Krock B., Ritter A., Hjeij R., Bakey Z.,
RA Pennekamp P., Dworniczak B., Brunner H., Peterlin B., Tanidir C.,
RA Olbrich H., Omran H., Schmidts M.;
RT "Recessive DNAH9 loss-of-function mutations cause laterality defects and
RT subtle respiratory ciliary-beating defects.";
RL Am. J. Hum. Genet. 103:995-1008(2018).
RN [10]
RP INTERACTION WITH MNS1.
RX PubMed=30148830; DOI=10.1371/journal.pgen.1007602;
RA Ta-Shma A., Hjeij R., Perles Z., Dougherty G.W., Abu Zahira I.,
RA Letteboer S.J.F., Antony D., Darwish A., Mans D.A., Spittler S.,
RA Edelbusch C., Cindric S., Noethe-Menchen T., Olbrich H., Stuhlmann F.,
RA Aprea I., Pennekamp P., Loges N.T., Breuer O., Shaag A., Rein A.J.J.T.,
RA Gulec E.Y., Gezdirici A., Abitbul R., Elias N., Amirav I., Schmidts M.,
RA Roepman R., Elpeleg O., Omran H.;
RT "Homozygous loss-of-function mutations in MNS1 cause laterality defects and
RT likely male infertility.";
RL PLoS Genet. 14:e1007602-e1007602(2018).
CC -!- FUNCTION: Component of the outer dynein arm-docking complex (ODA-DC)
CC that mediates outer dynein arms (ODA) binding onto the doublet
CC microtubule. Involved in mediating assembly of both ODAs and their
CC axonemal docking complex onto ciliary microtubules (By similarity).
CC {ECO:0000250|UniProtKB:F1N2N9, ECO:0000269|PubMed:27486780,
CC ECO:0000305|PubMed:23261302, ECO:0000305|PubMed:23261303}.
CC -!- SUBUNIT: Component of the outer dynein arm-docking complex along with
CC ODAD2, ODAD3, ODAD4 and CLXN (PubMed:27486780, PubMed:25192045).
CC Interacts with ODAD3 (PubMed:25192045). Interacts with ODAD4; this
CC interaction may facilitate the recruitment and/or attachment of outer
CC dynein arm docking complex proteins, including ODAD1, ODAD3, and ODAD4
CC to ciliary axonemes (PubMed:27486780). Interacts with DNAH9
CC (PubMed:30471718, PubMed:25192045, PubMed:27486780). Interacts with
CC MNS1 (PubMed:30148830). Interacts with PIERCE1 and PIERCE2; the
CC interactions link the outer dynein arms docking complex (ODA-DC) to the
CC internal microtubule inner proteins (MIP) in cilium axoneme (By
CC similarity). {ECO:0000250|UniProtKB:F1N2N9,
CC ECO:0000269|PubMed:25192045, ECO:0000269|PubMed:27486780,
CC ECO:0000269|PubMed:30148830, ECO:0000269|PubMed:30471718}.
CC -!- INTERACTION:
CC Q96M63; Q8TAB5: C1orf216; NbExp=6; IntAct=EBI-10173858, EBI-747505;
CC Q96M63; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-10173858, EBI-2514791;
CC Q96M63; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-10173858, EBI-16429135;
CC Q96M63; O14964: HGS; NbExp=9; IntAct=EBI-10173858, EBI-740220;
CC Q96M63; Q07866: KLC1; NbExp=3; IntAct=EBI-10173858, EBI-721019;
CC Q96M63; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10173858, EBI-739832;
CC Q96M63; A5D8V7: ODAD3; NbExp=3; IntAct=EBI-10173858, EBI-8466445;
CC Q96M63; A5D8V7-2: ODAD3; NbExp=3; IntAct=EBI-10173858, EBI-10173824;
CC Q96M63; Q5VU62: TPM3; NbExp=3; IntAct=EBI-10173858, EBI-10184033;
CC Q96M63; Q99757: TXN2; NbExp=3; IntAct=EBI-10173858, EBI-2932492;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:23261303, ECO:0000269|PubMed:25192045}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96M63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96M63-4; Sequence=VSP_036212;
CC Name=3;
CC IsoId=Q96M63-5; Sequence=VSP_036213, VSP_036214;
CC -!- DISEASE: Ciliary dyskinesia, primary, 20 (CILD20) [MIM:615067]: A
CC disorder characterized by abnormalities of motile cilia. Respiratory
CC infections leading to chronic inflammation and bronchiectasis are
CC recurrent, due to defects in the respiratory cilia. Patients may
CC exhibit randomization of left-right body asymmetry and situs inversus,
CC due to dysfunction of monocilia at the embryonic node. Primary ciliary
CC dyskinesia associated with situs inversus is referred to as Kartagener
CC syndrome. Unlike other forms of CILD characterized by reduced
CC fertility, patients with CILD20 do not appear to be infertile.
CC {ECO:0000269|PubMed:23261302, ECO:0000269|PubMed:23261303}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ODA1/DCC2 family. {ECO:0000305}.
CC -!- CAUTION: Although the CILD20 variant corresponding to dbSNP:rs147718607
CC could create a Ala to Thr substitution at position 248, the variation
CC causes an intronic insertion, resulting in a frameshift and premature
CC truncation. It should therefore not be considered as a single amino
CC acid polymorphism (SAP) (PubMed:23261303).
CC {ECO:0000305|PubMed:23261303}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71448.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=BAC87296.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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DR EMBL; AK057357; BAB71448.1; ALT_SEQ; mRNA.
DR EMBL; AK057488; BAB71508.1; -; mRNA.
DR EMBL; AK128144; BAC87296.1; ALT_SEQ; mRNA.
DR EMBL; AC008392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007730; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC117431; AAI17432.1; -; mRNA.
DR EMBL; BC117433; AAI17434.1; -; mRNA.
DR EMBL; AL122083; CAB59257.1; -; mRNA.
DR CCDS; CCDS12714.2; -. [Q96M63-1]
DR PIR; T34564; T34564.
DR RefSeq; NP_653178.3; NM_144577.3. [Q96M63-1]
DR RefSeq; XP_011525817.1; XM_011527515.2.
DR RefSeq; XP_011525818.1; XM_011527516.2.
DR AlphaFoldDB; Q96M63; -.
DR SMR; Q96M63; -.
DR BioGRID; 125015; 57.
DR IntAct; Q96M63; 9.
DR STRING; 9606.ENSP00000318429; -.
DR iPTMnet; Q96M63; -.
DR PhosphoSitePlus; Q96M63; -.
DR BioMuta; CCDC114; -.
DR DMDM; 221222533; -.
DR MassIVE; Q96M63; -.
DR PaxDb; Q96M63; -.
DR PeptideAtlas; Q96M63; -.
DR PRIDE; Q96M63; -.
DR ProteomicsDB; 77300; -. [Q96M63-1]
DR ProteomicsDB; 77301; -. [Q96M63-4]
DR ProteomicsDB; 77302; -. [Q96M63-5]
DR Antibodypedia; 49648; 70 antibodies from 15 providers.
DR DNASU; 93233; -.
DR Ensembl; ENST00000315396.7; ENSP00000318429.7; ENSG00000105479.16. [Q96M63-1]
DR GeneID; 93233; -.
DR KEGG; hsa:93233; -.
DR UCSC; uc002pir.3; human. [Q96M63-1]
DR CTD; 93233; -.
DR DisGeNET; 93233; -.
DR GeneCards; ODAD1; -.
DR GeneReviews; ODAD1; -.
DR HGNC; HGNC:26560; ODAD1.
DR HPA; ENSG00000105479; Group enriched (brain, choroid plexus, fallopian tube, testis).
DR MalaCards; ODAD1; -.
DR MIM; 615038; gene.
DR MIM; 615067; phenotype.
DR neXtProt; NX_Q96M63; -.
DR OpenTargets; ENSG00000105479; -.
DR Orphanet; 244; Primary ciliary dyskinesia.
DR VEuPathDB; HostDB:ENSG00000105479; -.
DR eggNOG; ENOG502QSIU; Eukaryota.
DR GeneTree; ENSGT00940000153116; -.
DR HOGENOM; CLU_027546_3_1_1; -.
DR InParanoid; Q96M63; -.
DR OMA; HCDGSMI; -.
DR OrthoDB; 648380at2759; -.
DR PhylomeDB; Q96M63; -.
DR TreeFam; TF323742; -.
DR PathwayCommons; Q96M63; -.
DR SignaLink; Q96M63; -.
DR BioGRID-ORCS; 93233; 37 hits in 1073 CRISPR screens.
DR GenomeRNAi; 93233; -.
DR Pharos; Q96M63; Tbio.
DR PRO; PR:Q96M63; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96M63; protein.
DR Bgee; ENSG00000105479; Expressed in oviduct epithelium and 116 other tissues.
DR ExpressionAtlas; Q96M63; baseline and differential.
DR Genevisible; Q96M63; HS.
DR GO; GO:0005930; C:axoneme; IDA:SYSCILIA_CCNET.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0036157; C:outer dynein arm; IMP:UniProtKB.
DR GO; GO:0120228; C:outer dynein arm docking complex; ISS:UniProtKB.
DR GO; GO:0003341; P:cilium movement; IMP:SYSCILIA_CCNET.
DR GO; GO:0036158; P:outer dynein arm assembly; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Ciliopathy; Cilium; Coiled coil;
KW Cytoplasm; Cytoskeleton; Kartagener syndrome; Phosphoprotein;
KW Primary ciliary dyskinesia; Reference proteome.
FT CHAIN 1..670
FT /note="Outer dynein arm-docking complex subunit 1"
FT /id="PRO_0000288807"
FT REGION 454..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..155
FT /evidence="ECO:0000255"
FT COILED 183..224
FT /evidence="ECO:0000255"
FT COILED 302..381
FT /evidence="ECO:0000255"
FT COMPBIAS 561..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1H228"
FT VAR_SEQ 1..207
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036212"
FT VAR_SEQ 492..539
FT /note="ELQEQAEAQRQKDLAAAAAKLDGTLSVDLASTQRAGSSTVLVPTRHPH ->
FT RVGPAGVGPGLSVCRGPVHLPCRWSSRSRRRRSARRTWPPPPRSWTAP (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_036213"
FT VAR_SEQ 540..670
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_036214"
FT VARIANT 329
FT /note="R -> H (in dbSNP:rs35361179)"
FT /id="VAR_032501"
FT VARIANT 468
FT /note="P -> L (in dbSNP:rs35461177)"
FT /id="VAR_032502"
FT CONFLICT 224
FT /note="H -> Y (in Ref. 2; BC007730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 75046 MW; A2CC0E7F18AB7ACF CRC64;
MEGERRAYSK EVHQRINKQL EEIRRLEEVR GDLQVQISAA QNQVKRLRDS QRLENMDRLL
KGRAQVQAEI EELQEQTRAL DKQIQEWETR IFTHSKNVRS PGFILDQKVK IRRRIRILEN
QLDRVTCHFD NQLVRNAALR EELDLLRIDR NRYLNVDRKL KKEIHHLHHL VSTLILSSTS
AYAVREEAKA KMGLLRERAE KEEAQSEMEA QVLQRQILHL EQLHHFLKLK NNDRQPDPDV
LEKREKQAGE VAEGVWKTSQ ERLVLCYEDA LNKLSQLMGE SDPDLLVQKY LEIEERNFAE
FNFINEQNLE LEHVQEEIKE MQEALVSARA SKDDQHLLQE QQQKVLQQRM DKVHSEAERL
EARFQDVRGQ LEKLKADIQL LFTKAHCDSS MIDDLLGVKT SMGDRDMGLF LSLIEKRLVE
LLTVQAFLHA QSFTSLADAA LLVLGQSLED LPKKMAPLQP PDTLEDPPGF EASDDYPMSR
EELLSQVEKL VELQEQAEAQ RQKDLAAAAA KLDGTLSVDL ASTQRAGSST VLVPTRHPHA
IPGSILSHKT SRDRGSLGHV TFGGLSSSTG HLPSHITHGD PNTGHVTFGS TSASSGGHVT
FRPVSASSYL GSTGYVGSSR GGENTEGGVE SGGTASDSSG GLGSSRDHVS STGPASSTGP
GSSTSKDSRG
