CROCC_HUMAN
ID CROCC_HUMAN Reviewed; 2017 AA.
AC Q5TZA2; Q2VHY3; Q66GT7; Q7Z2L4; Q7Z5D7;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Rootletin;
DE AltName: Full=Ciliary rootlet coiled-coil protein;
GN Name=CROCC {ECO:0000312|EMBL:CAH70055.1};
GN Synonyms=KIAA0445 {ECO:0000312|EMBL:BAA32290.2};
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] {ECO:0000305, ECO:0000312|EMBL:ABA43896.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Ching Y.-P., Chan S.-F., Jeang K.-T., Jin D.-Y.;
RT "A centrosomal target of human T-cell leukemia virus type 1 oncoprotein
RT Tax.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAA32290.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-2017 (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:BAA32290.2};
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAP85633.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1572-2017 (ISOFORM 2).
RC TISSUE=Medulloblastoma {ECO:0000312|EMBL:AAP85633.1};
RX PubMed=12800201; DOI=10.1002/ijc.11208;
RA Behrends U., Schneider I., Roessler S., Frauenknecht H., Golbeck A.,
RA Lechner B., Eigenstetter G., Zobywalski C., Mueller-Weihrich S.,
RA Graubner U., Schmid I., Sackerer D., Spaeth M., Goetz C., Prantl F.,
RA Asmuss H.-P., Bise K., Mautner J.;
RT "Novel tumor antigens identified by autologous antibody screening of
RT childhood medulloblastoma cDNA libraries.";
RL Int. J. Cancer 106:244-251(2003).
RN [5] {ECO:0000305, ECO:0000312|EMBL:DAA05505.1}
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CEP250 AND NEK2, AND PHOSPHORYLATION.
RX PubMed=16203858; DOI=10.1083/jcb.200504107;
RA Bahe S., Stierhof Y.-D., Wilkinson C.J., Leiss F., Nigg E.A.;
RT "Rootletin forms centriole-associated filaments and functions in centrosome
RT cohesion.";
RL J. Cell Biol. 171:27-33(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1460 AND SER-1660, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1476, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27623382; DOI=10.1016/j.devcel.2016.07.013;
RA Nechipurenko I.V., Olivier-Mason A., Kazatskaya A., Kennedy J.,
RA McLachlan I.G., Heiman M.G., Blacque O.E., Sengupta P.;
RT "A Conserved role for girdin in basal body positioning and ciliogenesis.";
RL Dev. Cell 38:493-506(2016).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CEP44.
RX PubMed=31974111; DOI=10.1242/jcs.239616;
RA Hossain D., Shih S.Y., Xiao X., White J., Tsang W.Y.;
RT "Cep44 functions in centrosome cohesion by stabilizing rootletin.";
RL J. Cell Sci. 133:0-0(2020).
RN [11]
RP VARIANTS TRP-1216 AND CYS-1866.
RX PubMed=29961568; DOI=10.1016/j.ajhg.2018.06.001;
RG NIHR BioResource;
RG Care4Rare Canada Consortium;
RA Ito Y., Carss K.J., Duarte S.T., Hartley T., Keren B., Kurian M.A.,
RA Marey I., Charles P., Mendonca C., Nava C., Pfundt R., Sanchis-Juan A.,
RA van Bokhoven H., van Essen A., van Ravenswaaij-Arts C., Boycott K.M.,
RA Kernohan K.D., Dyack S., Raymond F.L.;
RT "De Novo Truncating Mutations in WASF1 Cause Intellectual Disability with
RT Seizures.";
RL Am. J. Hum. Genet. 103:144-153(2018).
CC -!- FUNCTION: Major structural component of the ciliary rootlet, a
CC cytoskeletal-like structure in ciliated cells which originates from the
CC basal body at the proximal end of a cilium and extends proximally
CC toward the cell nucleus (By similarity). Furthermore, is required for
CC the correct positioning of the cilium basal body relative to the cell
CC nucleus, to allow for ciliogenesis (PubMed:27623382). Contributes to
CC centrosome cohesion before mitosis (PubMed:16203858).
CC {ECO:0000250|UniProtKB:Q8CJ40, ECO:0000269|PubMed:16203858,
CC ECO:0000269|PubMed:27623382}.
CC -!- SUBUNIT: Homomer. Interacts with KLC3, NEK2 and the N-terminus of
CC CEP250. Interacts with CEP44 (PubMed:31974111).
CC {ECO:0000269|PubMed:16203858, ECO:0000269|PubMed:31974111}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:14654843}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:27623382}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:27623382, ECO:0000269|PubMed:31974111}. Note=In
CC ciliated cells, associated with ciliary rootlets. In non-ciliated
CC cells, localized between, around and at the proximal ends of the
CC centrioles. Dissociates from the centrioles at the onset of mitosis and
CC reassociates with them at anaphase. {ECO:0000269|PubMed:14654843}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:9455484};
CC IsoId=Q5TZA2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|Ref.1};
CC IsoId=Q5TZA2-2; Sequence=VSP_052069, VSP_052070;
CC -!- PTM: Phosphorylated by NEK2 which may regulate its association with
CC centrosomes. {ECO:0000269|PubMed:16203858}.
CC -!- SIMILARITY: Belongs to the rootletin family. {ECO:0000305}.
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DR EMBL; DQ139275; ABA43896.1; -; mRNA.
DR EMBL; BX284668; CAH70055.1; -; Genomic_DNA.
DR EMBL; AL049569; CAH70055.1; JOINED; Genomic_DNA.
DR EMBL; AL049569; CAI20363.1; -; Genomic_DNA.
DR EMBL; BX284668; CAI20363.1; JOINED; Genomic_DNA.
DR EMBL; AB007914; BAA32290.2; -; mRNA.
DR EMBL; AF527734; AAP85633.1; -; mRNA.
DR EMBL; BK005505; DAA05505.1; -; mRNA.
DR CCDS; CCDS30616.1; -. [Q5TZA2-1]
DR RefSeq; NP_055490.4; NM_014675.4.
DR PDB; 6L5H; X-ray; 1.30 A; A/B=1108-1200.
DR PDB; 6L5J; X-ray; 2.77 A; A/B/C/D=1108-1317.
DR PDBsum; 6L5H; -.
DR PDBsum; 6L5J; -.
DR AlphaFoldDB; Q5TZA2; -.
DR BioGRID; 115048; 42.
DR DIP; DIP-61715N; -.
DR IntAct; Q5TZA2; 27.
DR MINT; Q5TZA2; -.
DR STRING; 9606.ENSP00000364691; -.
DR GlyGen; Q5TZA2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5TZA2; -.
DR PhosphoSitePlus; Q5TZA2; -.
DR SwissPalm; Q5TZA2; -.
DR BioMuta; CROCC; -.
DR DMDM; 74746681; -.
DR EPD; Q5TZA2; -.
DR jPOST; Q5TZA2; -.
DR MassIVE; Q5TZA2; -.
DR MaxQB; Q5TZA2; -.
DR PaxDb; Q5TZA2; -.
DR PeptideAtlas; Q5TZA2; -.
DR PRIDE; Q5TZA2; -.
DR ProteomicsDB; 65215; -. [Q5TZA2-1]
DR ProteomicsDB; 65216; -. [Q5TZA2-2]
DR Antibodypedia; 14565; 35 antibodies from 15 providers.
DR DNASU; 9696; -.
DR Ensembl; ENST00000375541.10; ENSP00000364691.4; ENSG00000058453.17. [Q5TZA2-1]
DR GeneID; 9696; -.
DR KEGG; hsa:9696; -.
DR MANE-Select; ENST00000375541.10; ENSP00000364691.4; NM_014675.5; NP_055490.4.
DR UCSC; uc001azt.2; human. [Q5TZA2-1]
DR CTD; 9696; -.
DR DisGeNET; 9696; -.
DR GeneCards; CROCC; -.
DR HGNC; HGNC:21299; CROCC.
DR HPA; ENSG00000058453; Low tissue specificity.
DR MIM; 615776; gene.
DR neXtProt; NX_Q5TZA2; -.
DR OpenTargets; ENSG00000058453; -.
DR PharmGKB; PA134911945; -.
DR VEuPathDB; HostDB:ENSG00000058453; -.
DR eggNOG; ENOG502QQF0; Eukaryota.
DR GeneTree; ENSGT00940000155758; -.
DR HOGENOM; CLU_000920_1_0_1; -.
DR InParanoid; Q5TZA2; -.
DR OrthoDB; 76868at2759; -.
DR PhylomeDB; Q5TZA2; -.
DR TreeFam; TF101138; -.
DR PathwayCommons; Q5TZA2; -.
DR SignaLink; Q5TZA2; -.
DR SIGNOR; Q5TZA2; -.
DR BioGRID-ORCS; 9696; 50 hits in 1083 CRISPR screens.
DR ChiTaRS; CROCC; human.
DR GeneWiki; Rootletin; -.
DR GenomeRNAi; 9696; -.
DR Pharos; Q5TZA2; Tbio.
DR PRO; PR:Q5TZA2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5TZA2; protein.
DR Bgee; ENSG00000058453; Expressed in right uterine tube and 148 other tissues.
DR ExpressionAtlas; Q5TZA2; baseline and differential.
DR Genevisible; Q5TZA2; HS.
DR GO; GO:0097729; C:9+2 motile cilium; IEA:Ensembl.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0035253; C:ciliary rootlet; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0120219; C:subapical part of cell; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0019894; F:kinesin binding; ISS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR GO; GO:0019725; P:cellular homeostasis; IEA:Ensembl.
DR GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; IDA:UniProtKB.
DR GO; GO:0032053; P:ciliary basal body organization; IEA:Ensembl.
DR GO; GO:0010669; P:epithelial structure maintenance; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0051656; P:establishment of organelle localization; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:1903566; P:positive regulation of protein localization to cilium; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0033365; P:protein localization to organelle; IMP:UniProtKB.
DR InterPro; IPR026733; Rootletin.
DR PANTHER; PTHR23159:SF17; PTHR23159:SF17; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..2017
FT /note="Rootletin"
FT /id="PRO_0000239943"
FT REGION 464..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1962..2017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..262
FT /evidence="ECO:0000255"
FT COILED 318..444
FT /evidence="ECO:0000255"
FT COILED 546..1058
FT /evidence="ECO:0000255"
FT COILED 1091..1438
FT /evidence="ECO:0000255"
FT COILED 1505..1704
FT /evidence="ECO:0000255"
FT COMPBIAS 464..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1498
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1963..1987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1991..2006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ40"
FT MOD_RES 1476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ40"
FT MOD_RES 1486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ40"
FT MOD_RES 1490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ40"
FT MOD_RES 1496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ40"
FT MOD_RES 1575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ40"
FT MOD_RES 1660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..697
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12800201, ECO:0000303|Ref.1"
FT /id="VSP_052069"
FT VAR_SEQ 1984..1990
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12800201, ECO:0000303|Ref.1"
FT /id="VSP_052070"
FT VARIANT 7
FT /note="G -> R (in dbSNP:rs6586566)"
FT /id="VAR_061626"
FT VARIANT 372
FT /note="R -> Q (in dbSNP:rs57442576)"
FT /id="VAR_061627"
FT VARIANT 439
FT /note="A -> V (in dbSNP:rs4463721)"
FT /id="VAR_059628"
FT VARIANT 586
FT /note="D -> H (in dbSNP:rs9435714)"
FT /id="VAR_059629"
FT VARIANT 1097
FT /note="R -> P (in dbSNP:rs6669627)"
FT /id="VAR_059630"
FT VARIANT 1216
FT /note="R -> W (in dbSNP:rs749003874)"
FT /evidence="ECO:0000269|PubMed:29961568"
FT /id="VAR_083473"
FT VARIANT 1866
FT /note="R -> C (in dbSNP:rs374780265)"
FT /evidence="ECO:0000269|PubMed:29961568"
FT /id="VAR_083474"
FT HELIX 1108..1186
FT /evidence="ECO:0007829|PDB:6L5H"
SQ SEQUENCE 2017 AA; 228424 MW; 5A7167A0A906CF03 CRC64;
MSLGLAGAQE VELTLETVIQ TLESSVLCQE KGLGARDLAQ DAQITSLPAL IREIVTRNLS
QPESPVLLPA TEMASLLSLQ EENQLLQQEL SRVEDLLAQS RAERDELAIK YNAVSERLEQ
ALRLEPGELE TQEPRGLVRQ SVELRRQLQE EQASYRRKLQ AYQEGQQRQA QLVQRLQGKI
LQYKKRCSEL EQQLLERSGE LEQQRLRDTE HSQDLESALI RLEEEQQRSA SLAQVNAMLR
EQLDQAGSAN QALSEDIRKV TNDWTRCRKE LEHREAAWRR EEESFNAYFS NEHSRLLLLW
RQVVGFRRLV SEVKMFTERD LLQLGGELAR TSRAVQEAGL GLSTGLRLAE SRAEAALEKQ
ALLQAQLEEQ LRDKVLREKD LAQQQMQSDL DKADLSARVT ELGLAVKRLE KQNLEKDQVN
KDLTEKLEAL ESLRLQEQAA LETEDGEGLQ QTLRDLAQAV LSDSESGVQL SGSERTADAS
NGSLRGLSGQ RTPSPPRRSS PGRGRSPRRG PSPACSDSST LALIHSALHK RQLQVQDMRG
RYEASQDLLG TLRKQLSDSE SERRALEEQL QRLRDKTDGA MQAHEDAQRE VQRLRSANEL
LSREKSNLAH SLQVAQQQAE ELRQEREKLQ AAQEELRRQR DRLEEEQEDA VQDGARVRRE
LERSHRQLEQ LEGKRSVLAK ELVEVREALS RATLQRDMLQ AEKAEVAEAL TKAEAGRVEL
ELSMTKLRAE EASLQDSLSK LSALNESLAQ DKLDLNRLVA QLEEEKSALQ GRQRQAEQEA
TVAREEQERL EELRLEQEVA RQGLEGSLRV AEQAQEALEQ QLPTLRHERS QLQEQLAQLS
RQLSGREQEL EQARREAQRQ VEALERAARE KEALAKEHAG LAVQLVAAER EGRTLSEEAT
RLRLEKEALE GSLFEVQRQL AQLEARREQL EAEGQALLLA KETLTGELAG LRQQIIATQE
KASLDKELMA QKLVQAEREA QASLREQRAA HEEDLQRLQR EKEAAWRELE AERAQLQSQL
QREQEELLAR LEAEKEELSE EIAALQQERD EGLLLAESEK QQALSLKESE KTALSEKLMG
TRHSLATISL EMERQKRDAQ SRQEQDRSTV NALTSELRDL RAQREEAAAA HAQEVRRLQE
QARDLGKQRD SCLREAEELR TQLRLLEDAR DGLRRELLEA QRKLRESQEG REVQRQEAGE
LRRSLGEGAK EREALRRSNE ELRSAVKKAE SERISLKLAN EDKEQKLALL EEARTAVGKE
AGELRTGLQE VERSRLEARR ELQELRRQMK MLDSENTRLG RELAELQGRL ALGERAEKES
RRETLGLRQR LLKGEASLEV MRQELQVAQR KLQEQEGEFR TRERRLLGSL EEARGTEKQQ
LDHARGLELK LEAARAEAAE LGLRLSAAEG RAQGLEAELA RVEVQRRAAE AQLGGLRSAL
RRGLGLGRAP SPAPRPVPGS PARDAPAEGS GEGLNSPSTL ECSPGSQPPS PGPATSPASP
DLDPEAVRGA LREFLQELRS AQRERDELRT QTSALNRQLA EMEAERDSAT SRARQLQKAV
AESEEARRSV DGRLSGVQAE LALQEESVRR SERERRATLD QVATLERSLQ ATESELRASQ
EKISKMKANE TKLEGDKRRL KEVLDASESR TVKLELQRRS LEGELQRSRL GLSDREAQAQ
ALQDRVDSLQ RQVADSEVKA GTLQLTVERL NGALAKVEES EGALRDKVRG LTEALAQSSA
SLNSTRDKNL HLQKALTACE HDRQVLQERL DAARQALSEA RKQSSSLGEQ VQTLRGEVAD
LELQRVEAEG QLQQLREVLR QRQEGEAAAL NTVQKLQDER RLLQERLGSL QRALAQLEAE
KREVERSALR LEKDRVALRR TLDKVEREKL RSHEDTVRLS AEKGRLDRTL TGAELELAEA
QRQIQQLEAQ VVVLEQSHSP AQLEVDAQQQ QLELQQEVER LRSAQAQTER TLEARERAHR
QRVRGLEEQV STLKGQLQQE LRRSSAPFSP PSGPPEK
