CCD66_HUMAN
ID CCD66_HUMAN Reviewed; 948 AA.
AC A2RUB6; B3KWL8; Q4VC34; Q8N949;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 4.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Coiled-coil domain-containing protein 66 {ECO:0000305};
GN Name=CCDC66 {ECO:0000312|HGNC:HGNC:27709};
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] (ISOFORMS 2 AND 4).
RC TISSUE=Brain, and Teratocarcinoma;
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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP ARG-383 AND GLN-460.
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115 AND THR-121, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19777273; DOI=10.1007/s10048-009-0223-z;
RA Dekomien G., Vollrath C., Petrasch-Parwez E., Boeve M.H., Akkad D.A.,
RA Gerding W.M., Epplen J.T.;
RT "Progressive retinal atrophy in Schapendoes dogs: mutation of the newly
RT identified CCDC66 gene.";
RL Neurogenetics 11:163-174(2010).
RN [6]
RP FUNCTION, INTERACTION WITH CEP290 AND PCM1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF 208-GLU--PHE-948.
RX PubMed=28235840; DOI=10.1242/jcs.196832;
RA Conkar D., Culfa E., Odabasi E., Rauniyar N., Yates J.R. III,
RA Firat-Karalar E.N.;
RT "The centriolar satellite protein CCDC66 interacts with CEP290 and
RT functions in cilium formation and trafficking.";
RL J. Cell Sci. 130:1450-1462(2017).
RN [7]
RP INTERACTION WITH ARMC9; TOGARAM1; CSPP1 AND CEP104.
RX PubMed=32453716; DOI=10.1172/jci131656;
RG University of Washington Center for Mendelian Genomics;
RG Genomics England Research Consortium;
RA Latour B.L., Van De Weghe J.C., Rusterholz T.D., Letteboer S.J., Gomez A.,
RA Shaheen R., Gesemann M., Karamzade A., Asadollahi M., Barroso-Gil M.,
RA Chitre M., Grout M.E., van Reeuwijk J., van Beersum S.E., Miller C.V.,
RA Dempsey J.C., Morsy H., Bamshad M.J., Nickerson D.A., Neuhauss S.C.,
RA Boldt K., Ueffing M., Keramatipour M., Sayer J.A., Alkuraya F.S.,
RA Bachmann-Gagescu R., Roepman R., Doherty D.;
RT "Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes Joubert
RT syndrome.";
RL J. Clin. Invest. 130:4423-4439(2020).
RN [8]
RP VARIANTS ARG-383; GLN-460; GLN-592 AND TYR-681.
RX PubMed=21680557; DOI=10.1093/hmg/ddr282;
RA Gerding W.M., Schreiber S., Schulte-Middelmann T., de Castro Marques A.,
RA Atorf J., Akkad D.A., Dekomien G., Kremers J., Dermietzel R., Gal A.,
RA Ruelicke T., Ibrahim S., Epplen J.T., Petrasch-Parwez E.;
RT "Ccdc66 null mutation causes retinal degeneration and dysfunction.";
RL Hum. Mol. Genet. 20:3620-3631(2011).
CC -!- FUNCTION: Microtubule-binding protein required for ciliogenesis
CC (PubMed:28235840). May function in ciliogenesis by mediating the
CC transport of proteins like BBS4 to the cilium, but also through the
CC organization of the centriolar satellites (PubMed:28235840). Plays a
CC role in retina morphogenesis and/or homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:Q6NS45, ECO:0000269|PubMed:28235840}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC CEP290 (PubMed:28235840). Interacts with PCM1 (PubMed:28235840).
CC Interacts with ARMC9, TOGARAM1, CSPP1 and CEP104 (PubMed:32453716).
CC {ECO:0000250|UniProtKB:Q6NS45, ECO:0000269|PubMed:28235840,
CC ECO:0000269|PubMed:32453716}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:28235840}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriolar
CC satellite {ECO:0000269|PubMed:28235840}. Cell projection, cilium
CC {ECO:0000269|PubMed:28235840}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:28235840}. Photoreceptor inner segment
CC {ECO:0000269|PubMed:19777273}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000269|PubMed:19777273}. Note=Restricted to the
CC centrosomes and the spindle microtubules during mitosis
CC (PubMed:28235840). Enriched in the inner segment of the photoreceptor
CC (PubMed:19777273). {ECO:0000269|PubMed:19777273,
CC ECO:0000269|PubMed:28235840}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A2RUB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2RUB6-2; Sequence=VSP_031586, VSP_031587;
CC Name=3;
CC IsoId=A2RUB6-3; Sequence=VSP_036545;
CC Name=4;
CC IsoId=A2RUB6-4; Sequence=VSP_036545, VSP_036546;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level)
CC (PubMed:28235840). Expressed in retina, mainly in photoreceptors but
CC also in outer plexiform and ganglion cell layers (at protein level)
CC (PubMed:19777273). {ECO:0000269|PubMed:19777273,
CC ECO:0000269|PubMed:28235840}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47509.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI32828.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04607.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK095688; BAC04607.1; ALT_FRAME; mRNA.
DR EMBL; AK125303; BAG54180.1; -; mRNA.
DR EMBL; AC098478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047509; AAH47509.1; ALT_INIT; mRNA.
DR EMBL; BC132827; AAI32828.2; ALT_INIT; mRNA.
DR CCDS; CCDS33770.2; -. [A2RUB6-3]
DR CCDS; CCDS46852.1; -. [A2RUB6-1]
DR RefSeq; NP_001012524.4; NM_001012506.4. [A2RUB6-3]
DR RefSeq; NP_001135419.1; NM_001141947.1. [A2RUB6-1]
DR RefSeq; XP_016861723.1; XM_017006234.1.
DR RefSeq; XP_016861724.1; XM_017006235.1.
DR AlphaFoldDB; A2RUB6; -.
DR SMR; A2RUB6; -.
DR BioGRID; 130082; 26.
DR IntAct; A2RUB6; 17.
DR MINT; A2RUB6; -.
DR STRING; 9606.ENSP00000378167; -.
DR iPTMnet; A2RUB6; -.
DR PhosphoSitePlus; A2RUB6; -.
DR BioMuta; CCDC66; -.
DR EPD; A2RUB6; -.
DR jPOST; A2RUB6; -.
DR MassIVE; A2RUB6; -.
DR MaxQB; A2RUB6; -.
DR PaxDb; A2RUB6; -.
DR PeptideAtlas; A2RUB6; -.
DR PRIDE; A2RUB6; -.
DR ProteomicsDB; 507; -. [A2RUB6-1]
DR ProteomicsDB; 508; -. [A2RUB6-2]
DR ProteomicsDB; 509; -. [A2RUB6-3]
DR ProteomicsDB; 510; -. [A2RUB6-4]
DR TopDownProteomics; A2RUB6-4; -. [A2RUB6-4]
DR Antibodypedia; 31476; 108 antibodies from 17 providers.
DR DNASU; 285331; -.
DR Ensembl; ENST00000326595.11; ENSP00000326050.7; ENSG00000180376.17. [A2RUB6-3]
DR Ensembl; ENST00000394672.8; ENSP00000378167.3; ENSG00000180376.17. [A2RUB6-1]
DR GeneID; 285331; -.
DR KEGG; hsa:285331; -.
DR MANE-Select; ENST00000394672.8; ENSP00000378167.3; NM_001141947.3; NP_001135419.1.
DR UCSC; uc003dhu.4; human. [A2RUB6-1]
DR CTD; 285331; -.
DR DisGeNET; 285331; -.
DR GeneCards; CCDC66; -.
DR HGNC; HGNC:27709; CCDC66.
DR HPA; ENSG00000180376; Low tissue specificity.
DR MIM; 619287; gene.
DR neXtProt; NX_A2RUB6; -.
DR OpenTargets; ENSG00000180376; -.
DR PharmGKB; PA143485418; -.
DR VEuPathDB; HostDB:ENSG00000180376; -.
DR eggNOG; ENOG502R1PQ; Eukaryota.
DR GeneTree; ENSGT00390000012411; -.
DR HOGENOM; CLU_016964_0_0_1; -.
DR InParanoid; A2RUB6; -.
DR OMA; QVEYNAS; -.
DR OrthoDB; 1468611at2759; -.
DR PhylomeDB; A2RUB6; -.
DR TreeFam; TF350489; -.
DR PathwayCommons; A2RUB6; -.
DR SignaLink; A2RUB6; -.
DR BioGRID-ORCS; 285331; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; CCDC66; human.
DR GenomeRNAi; 285331; -.
DR Pharos; A2RUB6; Tbio.
DR PRO; PR:A2RUB6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; A2RUB6; protein.
DR Bgee; ENSG00000180376; Expressed in calcaneal tendon and 151 other tissues.
DR ExpressionAtlas; A2RUB6; baseline and differential.
DR Genevisible; A2RUB6; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0090543; C:Flemming body; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
DR GO; GO:1903564; P:regulation of protein localization to cilium; IMP:UniProtKB.
DR GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
DR InterPro; IPR039183; CCD66.
DR InterPro; IPR040467; CCDC66_dom.
DR PANTHER; PTHR22736; PTHR22736; 1.
DR Pfam; PF15236; CCDC66; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disulfide bond; Phosphoprotein; Reference proteome.
FT CHAIN 1..948
FT /note="Coiled-coil domain-containing protein 66"
FT /id="PRO_0000320037"
FT REGION 458..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 467..558
FT /evidence="ECO:0000255"
FT COMPBIAS 690..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NS45"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NS45"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036545"
FT VAR_SEQ 231..948
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036546"
FT VAR_SEQ 272..287
FT /note="DEQVALKKKEKEVSEK -> VLQTVQAWYQHLLGFW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031586"
FT VAR_SEQ 288..948
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031587"
FT VARIANT 383
FT /note="Q -> R (in dbSNP:rs1491170)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:21680557"
FT /id="VAR_039111"
FT VARIANT 460
FT /note="R -> Q (in dbSNP:rs7637449)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:21680557"
FT /id="VAR_039112"
FT VARIANT 592
FT /note="E -> K (in dbSNP:rs4681904)"
FT /id="VAR_039113"
FT VARIANT 592
FT /note="E -> Q (in dbSNP:rs4681904)"
FT /evidence="ECO:0000269|PubMed:21680557"
FT /id="VAR_080466"
FT VARIANT 681
FT /note="C -> Y (in dbSNP:rs758090911)"
FT /evidence="ECO:0000269|PubMed:21680557"
FT /id="VAR_080467"
FT MUTAGEN 208..948
FT /note="Missing: Loss of association with microtubules and
FT localization to centrosomes."
FT /evidence="ECO:0000269|PubMed:28235840"
FT CONFLICT 104
FT /note="C -> Y (in Ref. 1; BAC04607)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="T -> TS (in Ref. 3; AAI32828)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 948 AA; 109411 MW; 2F7516E4C32C0310 CRC64;
MNLGDGLKLE TELLDGKTKL ILSPYEHKSK ISVKMGNKAK IAKCPLRTKT GHILKSTQDT
CIGSEKLLQK KPVGSETSQA KGEKNGMTFS STKDLCKQCI DKDCLHIQKE ISPATPNMQK
TRNTVNTSLV GKQKPHKKHI TAENMKSSLV CLTQDQLQQI LMTVNQGNRS LSLTENGKEA
KSQYSLYLNS ISNQPKDENI MGLFKKTEMV SSVPAENKSV LNEHQETSKQ CEQKIAIENE
WKPADIFSTL GERECDRSSL EAKKAQWRKE LDEQVALKKK EKEVSEKWND PWKKSESDKI
IWEKHQILDQ SRETVLLEHP FSAVKQELQR KWIEELNKQI EDDRQRKIEE KIIYSKGEEH
DRWAMHFDSL KSYPGSQSQL FSQSTHKQPE YFCVSPDTQE LADVSSVCTP TTGSQVEPSE
EEHIAKPIKD VVMANSKKTN FLRSMTALLD PAQIEERDRR RQKQLEHQKA ITAQVEEKRR
KKQLEEEQRK KEEQEEELRL AQEREEMQKQ YEEDILKQKQ KEEIMTLKTN ELFQTMQRAQ
ELAQRLKQEQ RIRELAQKGH DTSRLIKNLG VDTIQMEYNA SNISNSRHDS DEISGKMNTY
MNSTTSKKDT GVQTDDLNIG IFTNAESHCG SLMERDITNC SSPEISAELI GQFSTKKNKQ
ELTQDKGASL EKENNRCNDQ CNQFTRIEKQ TKHMKKYPKR PDWNINKPPK RYIPASEKYP
KQLQKQREEK KVRRQMELLH LVEKNNPGHL SQNRGISPEI FHSSHQETES KLRWHLVKKE
EEPLNIHSFS KERSPSSPVP VVKNRTQQTQ NTLHLPLKNS SYERENLISG SNQTELSSGI
SESSHFIPYV RTNEIYYLDP DAPLSGPSTQ DPQYQNSQDC GQKRQLFDSD CVRDPLLNPN
MVKNRDRQQA ILKGLSELRQ GLLQKQKELE SSLLPLAENQ EESFGSSF
