ID   CROCC_MOUSE             Reviewed;        2009 AA.
AC   Q8CJ40; A2AA81; Q7TQL2; Q80U01; Q8R0B9;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Rootletin;
DE   AltName: Full=Ciliary rootlet coiled-coil protein;
GN   Name=Crocc {ECO:0000312|MGI:MGI:3529431};
GN   Synonyms=Kiaa0445 {ECO:0000312|EMBL:BAC65567.3};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAN73044.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH KLC3.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAN73044.1};
RX   PubMed=12427867; DOI=10.1083/jcb.200207153;
RA   Yang J., Liu X., Yue G., Adamian M., Bulgakov O., Li T.;
RT   "Rootletin, a novel coiled-coil protein, is a structural component of the
RT   ciliary rootlet.";
RL   J. Cell Biol. 159:431-440(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAH54054.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH27090.1}, and FVB/N
RC   {ECO:0000312|EMBL:AAH54054.1};
RC   TISSUE=Colon {ECO:0000312|EMBL:AAH54054.1}, and Retina
RC   {ECO:0000312|EMBL:AAH27090.1};
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:BAC65567.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 391-2009 (ISOFORM 3).
RC   TISSUE=Brain {ECO:0000312|EMBL:BAC65567.3};
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   PROTEIN SEQUENCE OF 1261-1274, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6] {ECO:0000305}
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15870283; DOI=10.1128/mcb.25.10.4129-4137.2005;
RA   Yang J., Gao J., Adamian M., Wen X.-H., Pawlyk B., Zhang L.,
RA   Sanderson M.J., Zuo J., Makino C.L., Li T.;
RT   "The ciliary rootlet maintains long-term stability of sensory cilia.";
RL   Mol. Cell. Biol. 25:4129-4137(2005).
RN   [7] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH CEP250.
RX   PubMed=16339073; DOI=10.1091/mbc.e05-10-0943;
RA   Yang J., Adamian M., Li T.;
RT   "Rootletin interacts with C-Nap1 and may function as a physical linker
RT   between the pair of centrioles/basal bodies in cells.";
RL   Mol. Biol. Cell 17:1033-1040(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1463; SER-1469; TYR-1475;
RP   SER-1476; SER-1479; SER-1483; SER-1489 AND SER-1568, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 (PubMed:12427867). Furthermore, is required for
CC       the correct positioning of the cilium basal body relative to the cell
CC       nucleus, to allow for ciliogenesis (By similarity). Contributes to
CC       centrosome cohesion before mitosis (By similarity).
CC       {ECO:0000250|UniProtKB:Q5TZA2, ECO:0000269|PubMed:12427867}.
CC   -!- SUBUNIT: Homomer. Interacts with KLC3, NEK2 and the N-terminus of
CC       CEP250 (PubMed:12427867, PubMed:16339073). Interacts with CEP44 (By
CC       similarity). {ECO:0000250|UniProtKB:Q5TZA2,
CC       ECO:0000269|PubMed:12427867, ECO:0000269|PubMed:16339073}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000269|PubMed:12427867,
CC       ECO:0000269|PubMed:16339073}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000250|UniProtKB:Q5TZA2}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:Q5TZA2}. Note=In ciliated cells, associated with
CC       ciliary rootlets. In non-ciliated cells, localized between, around and
CC       at the proximal ends of the centrioles. Dissociates from the centrioles
CC       at the onset of mitosis and reassociates with them at anaphase.
CC       {ECO:0000269|PubMed:12427867, ECO:0000269|PubMed:16339073}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:12427867};
CC         IsoId=Q8CJ40-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:15489334};
CC         IsoId=Q8CJ40-2; Sequence=VSP_052066, VSP_052067;
CC       Name=3 {ECO:0000269|PubMed:12693553};
CC         IsoId=Q8CJ40-3; Sequence=VSP_052068;
CC   -!- TISSUE SPECIFICITY: Highest expression detected in photoreceptor cells
CC       of retina. Expressed at lower levels in brain, trachea and kidney.
CC       Detected in all major ciliated epithelia. During embryonic development,
CC       enriched along the apical domains of neuroepithelium in brain
CC       ventricular zone, in primordia of retinal pigment epithelia and in
CC       neural retina. {ECO:0000269|PubMed:12427867}.
CC   -!- PTM: Phosphorylated by NEK2 which may regulate its association with
CC       centrosomes.
CC   -!- DISRUPTION PHENOTYPE: Mice have no ciliary rootlets in ciliated cells.
CC       {ECO:0000269|PubMed:15870283}.
CC   -!- SIMILARITY: Belongs to the rootletin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27090.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF527975; AAN73044.1; -; mRNA.
DR   EMBL; AL645625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC027090; AAH27090.1; ALT_INIT; mRNA.
DR   EMBL; BC054054; AAH54054.1; -; mRNA.
DR   EMBL; AK122285; BAC65567.3; -; Transcribed_RNA.
DR   CCDS; CCDS18861.1; -. [Q8CJ40-1]
DR   CCDS; CCDS51346.1; -. [Q8CJ40-2]
DR   RefSeq; NP_001139430.1; NM_001145958.1. [Q8CJ40-2]
DR   RefSeq; NP_742120.2; NM_172122.2. [Q8CJ40-1]
DR   AlphaFoldDB; Q8CJ40; -.
DR   SMR; Q8CJ40; -.
DR   BioGRID; 231046; 14.
DR   IntAct; Q8CJ40; 6.
DR   STRING; 10090.ENSMUSP00000099549; -.
DR   iPTMnet; Q8CJ40; -.
DR   PhosphoSitePlus; Q8CJ40; -.
DR   EPD; Q8CJ40; -.
DR   jPOST; Q8CJ40; -.
DR   MaxQB; Q8CJ40; -.
DR   PaxDb; 10090-ENSMUSP00000099549; -.
DR   PeptideAtlas; Q8CJ40; -.
DR   ProteomicsDB; 277898; -. [Q8CJ40-1]
DR   ProteomicsDB; 277899; -. [Q8CJ40-2]
DR   ProteomicsDB; 277900; -. [Q8CJ40-3]
DR   Pumba; Q8CJ40; -.
DR   Antibodypedia; 14565; 48 antibodies from 15 providers.
DR   Ensembl; ENSMUST00000040222.14; ENSMUSP00000037679.8; ENSMUSG00000040860.17. [Q8CJ40-2]
DR   Ensembl; ENSMUST00000097816.9; ENSMUSP00000095425.3; ENSMUSG00000040860.17. [Q8CJ40-2]
DR   Ensembl; ENSMUST00000102491.10; ENSMUSP00000099549.4; ENSMUSG00000040860.17. [Q8CJ40-1]
DR   Ensembl; ENSMUST00000168157.8; ENSMUSP00000126543.2; ENSMUSG00000040860.17. [Q8CJ40-2]
DR   GeneID; 230872; -.
DR   KEGG; mmu:230872; -.
DR   UCSC; uc008vns.2; mouse. [Q8CJ40-1]
DR   UCSC; uc012dnz.1; mouse. [Q8CJ40-2]
DR   AGR; MGI:3529431; -.
DR   CTD; 9696; -.
DR   MGI; MGI:3529431; Crocc.
DR   VEuPathDB; HostDB:ENSMUSG00000040860; -.
DR   eggNOG; ENOG502QQF0; Eukaryota.
DR   GeneTree; ENSGT00940000155758; -.
DR   HOGENOM; CLU_000920_1_0_1; -.
DR   InParanoid; Q8CJ40; -.
DR   OMA; DPAQDCQ; -.
DR   OrthoDB; 2996539at2759; -.
DR   PhylomeDB; Q8CJ40; -.
DR   TreeFam; TF101138; -.
DR   BioGRID-ORCS; 230872; 6 hits in 78 CRISPR screens.
DR   ChiTaRS; Crocc; mouse.
DR   PRO; PR:Q8CJ40; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8CJ40; Protein.
DR   Bgee; ENSMUSG00000040860; Expressed in retinal neural layer and 175 other cell types or tissues.
DR   ExpressionAtlas; Q8CJ40; baseline and differential.
DR   GO; GO:0097729; C:9+2 motile cilium; IDA:MGI.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0120219; C:subapical part of cell; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0019894; F:kinesin binding; IPI:MGI.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR   GO; GO:0019725; P:cellular homeostasis; IMP:MGI.
DR   GO; GO:0010457; P:centriole-centriole cohesion; ISO:MGI.
DR   GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR   GO; GO:0032053; P:ciliary basal body organization; IMP:MGI.
DR   GO; GO:0010669; P:epithelial structure maintenance; IMP:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0051656; P:establishment of organelle localization; IMP:MGI.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; ISO:MGI.
DR   GO; GO:1903566; P:positive regulation of protein localization to cilium; ISO:MGI.
DR   GO; GO:0008104; P:protein localization; ISO:MGI.
DR   GO; GO:0033365; P:protein localization to organelle; ISO:MGI.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   PANTHER; PTHR23159; CENTROSOMAL PROTEIN 2; 1.
DR   PANTHER; PTHR23159:SF17; ROOTLETIN; 1.
DR   Pfam; PF15035; Rootletin; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 2.
DR   Genevisible; Q8CJ40; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Phosphoprotein; Reference proteome.
FT   CHAIN           1..2009
FT                   /note="Rootletin"
FT                   /id="PRO_0000239944"
FT   REGION          462..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1180..1225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1448..1501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1957..2009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          74..265
FT                   /evidence="ECO:0000255"
FT   COILED          346..438
FT                   /evidence="ECO:0000255"
FT   COILED          550..1058
FT                   /evidence="ECO:0000255"
FT   COILED          1091..1439
FT                   /evidence="ECO:0000255"
FT   COILED          1498..1697
FT                   /evidence="ECO:0000255"
FT   COILED          1744..1998
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        462..497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1475..1491
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1957..1976
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1977..2003
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1453
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5TZA2"
FT   MOD_RES         1463
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1469
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1475
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1476
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1479
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1489
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1568
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..74
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_052066"
FT   VAR_SEQ         120..209
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_052067"
FT   VAR_SEQ         1136..1156
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_052068"
FT   CONFLICT        289
FT                   /note="T -> A (in Ref. 1; AAN73044 and 3; AAH54054)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360
FT                   /note="E -> G (in Ref. 3; AAH54054)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        811
FT                   /note="V -> M (in Ref. 3; AAH54054)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1041
FT                   /note="K -> E (in Ref. 3; AAH54054)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1346
FT                   /note="L -> V (in Ref. 3; BAC65567)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1864
FT                   /note="F -> L (in Ref. 3; AAH54054)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2009 AA;  226945 MW;  62D942401C1085DA CRC64;
     MSLGLAGSLQ AQLALEIVIQ SLENCVLGPN QEKSLSVQNR VQDFQGASLL VCAREVIASN
     LSRPETPAPL QVPEMASLLS LQEENQLLQQ ELSRVEDLLA QSRAERDELA IKYNAVNERL
     EQAVRLETGE LEAQEPRGLV RQSVELRRQL QEEQSSYRRK LQAYQEGQQR QAQLVQRLQA
     KILQYKKQCS ELEKQLMDRS TELEQQRLRD TEHSQDLDSA LLRLEEEQQR SASLAQVNAM
     LREQLDQANL ANQALSEDIR KVTSDWTRSC KELEQREAVW RREEESFNTY FSSEHSRLLR
     LWRQVMGLRR QASEVKMGTE RDLLQLGGEL VRTSRAVQEL GLGLSASLHR AESKAEAALE
     KQKLLQAQLE EQLQAKLLRE KDLAQLQVQS DLDKADLSAR VTELALSVEH LQNQNSEKDQ
     VNRTLSDKLE ALESLRLQEQ TTLDTEDGEG LQQTLRDLAQ AALSDTESGV QLSSSERTAD
     TSDGSLRGFS GQRTPTPPRH SPGRGRSPRR GLSPACSDSS TLTLIHSALH KRQLQVQDMR
     GRYEASQELL GSVRKQLSDS EGERRGLEEQ LQRLRDQTAA SAQAQEDAQR EAQRLRSANE
     LLSREKGNLT HSLQVTQQQA KELRQELEKL QAAQEELKRQ HNQLEDAQED SVQEGARARR
     ELERSHRQLE QLEVKRSGLT KELVEVREAL SCAILQRDVL QTEKAEVAEA LTKAEAGRAQ
     LELSLTKLRA EEASLRDSLS KMSALNESLA QDKLELNRLI AQLEEEKVAL LGRQQQAEHA
     TTMAVEKQEL LEQLRLEQEV ERQGLQGSLC VAEQAREALE QQILVLRSER SHLQEQLAQL
     SRQLSGRDQE LEQALRESQR QVEALERAAR EKEAMAKERA GLAVKLAAAE REGRTLSEEA
     IRLRLEKEAL ESSLFDVQRQ LAQLEARREQ LEADSQALLL AKETLTGELA GLRQQVTSTE
     EKAALDKELM TQKLVQAERE AQASLREQRA AHEEDLQRLQ HEKEAAWREL QAERAQLQGQ
     LQQEREELLA RMEAEKEELS KEIAALQQER DEGLLLAESE KQQALSLKES EKTALSEKLM
     GTRHSLAAIS LEMERQKRDA QSRQEQDRNT LNALTSELRD LRAQLEEATA AHAQTVKELE
     ERTGNLGRQR EACMREAEEL RTQLRVLEDT RDGLRRELLE AQRKGRDSQD SSEAHRQEAS
     ELRRSLSEGA KEREALRRSN EELRSAVKKA ESERISLKLA NEDKEQKLAL LEEARVSVAK
     EAGELRASLQ EVERSRLEAR RELQELRRQM KTLDSDNGRL GRELADLQGR LALGERTEKE
     SRREALGLRQ RLLKGESSLE ALKQELQGSQ RKLQEQEAEF RARERGLLGS LEEARGAEKR
     LLDSARSLEL RLEAVRAETS ELGLRLSAAE GRAQGLEVEL ARVEAQRRVA EAQLGGLRSA
     LRRGLGLGRV SSSPAREAPA GGSGDGLSSP SPLEYSPRSQ PPSPGLIASP APPDLDPEAV
     RDALRDFLQE LRSAQRERDE LKVQTSTLSQ QLVEMEAERD HAASRAKQLQ KAVAESEEAW
     RSADRRLSGA QAELALQEES VRRSKRECRA TLDQMAVLER SLQATESELR ASQEKVSKMK
     ATEAKLESDK RRLKEVLDAS ESRSIKLELQ RRALEGELQR SRLGLGDREA HAQALQDRVD
     SLQRQVADSE VKAGTLQLTV ERLSGALAKV EESEGNLRSK VQSLTDALTQ SSASLSSTQD
     KNLHLQKALS TCEHDRQVLQ ERLDAARQAL SEARRQSSSL GEQVQTLRGE LASLELQRGD
     AEGQLQQLQQ ALRQRQEGEA MALRSVQKLQ EERRLLQERL GSLQRALAQL EAEKRDLERS
     ALQFDKDRVA LRKTLDKVER EKLRSHEDTL RLNAERGRLD RTLTGAELDL AEAQQQIQHL
     EAQVDVALEG NHNPVQPEAG EQQLELQQEV ERLRSAQVQT ERTLEARERA HRQRVSGLEE
     QVSTLKAQLH QELRRSSASV SLPPGTPEK
//