CCD61_HUMAN
ID CCD61_HUMAN Reviewed; 512 AA.
AC Q9Y6R9; C8CAP4; Q9HDB6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Centrosomal protein CCDC61 {ECO:0000303|PubMed:30354798};
DE AltName: Full=Coiled-coil domain-containing protein 61;
DE AltName: Full=VFL3 homolog {ECO:0000303|PubMed:31789463, ECO:0000303|PubMed:32375023};
GN Name=CCDC61 {ECO:0000312|HGNC:HGNC:33629};
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 [MRNA] (ISOFORM 2).
RA Iyadurai K.B., Piasecki B.P., LaVoie M., Sislo R., Silflow C.D.;
RT "The Chlamydomonas VFL3 gene is essential for probasal body positioning and
RT segregation.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373 AND SER-376, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373 AND SER-376, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373 AND SER-376, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373 AND SER-376, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-336; SER-373;
RP SER-376; SER-447 AND SER-473, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-285; SER-373 AND SER-376, AND
RP IDENTIFICATION BY 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 [11]
RP FUNCTION, INTERACTION WITH CEP170, AND SUBCELLULAR LOCATION.
RX PubMed=30354798; DOI=10.1091/mbc.e18-02-0115;
RA Baerenz F., Kschonsak Y.T., Meyer A., Jafarpour A., Lorenz H., Hoffmann I.;
RT "Ccdc61 controls centrosomal localization of Cep170 and is required for
RT spindle assembly and symmetry.";
RL Mol. Biol. Cell 29:3105-3118(2018).
RN [12]
RP FUNCTION, INTERACTION WITH CEP131; CEP170 AND PCM1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=31789463; DOI=10.1111/boc.201900038;
RA Pizon V., Gaudin N., Poteau M., Cifuentes-Diaz C., Demdou R., Heyer V.,
RA Reina San Martin B., Azimzadeh J.;
RT "hVFL3/CCDC61 is a component of mother centriole subdistal appendages
RT required for centrosome cohesion and positioning.";
RL Biol. Cell 112:22-37(2020).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-143, FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 128-PHE-ASP-129; LYS-259;
RP ARG-263; ARG-266; ARG-268 AND LYS-270.
RX PubMed=32375023; DOI=10.1016/j.str.2020.04.010;
RA Ochi T., Quarantotti V., Lin H., Jullien J., Rosa e Silva I., Boselli F.,
RA Barnabas D.D., Johnson C.M., McLaughlin S.H., Freund S.M.V.,
RA Blackford A.N., Kimata Y., Goldstein R.E., Jackson S.P., Blundell T.L.,
RA Dutcher S.K., Gergely F., van Breugel M.;
RT "CCDC61/VFL3 Is a Paralog of SAS6 and Promotes Ciliary Functions.";
RL Structure 28:674-689(2020).
CC -!- FUNCTION: Microtubule-binding centrosomal protein required for
CC centriole cohesion, independently of the centrosome-associated
CC protein/CEP250 and rootletin/CROCC linker (PubMed:31789463). In
CC interphase, required for anchoring microtubule at the mother centriole
CC subdistal appendages and for centrosome positioning (PubMed:31789463).
CC During mitosis, may be involved in spindle assembly and chromatin
CC alignment by regulating the organization of spindle microtubules into a
CC symmetrical structure (PubMed:30354798). Has been proposed to play a
CC role in CEP170 recruitment to centrosomes (PubMed:30354798). However,
CC this function could not be confirmed (PubMed:31789463). Plays a non-
CC essential role in ciliogenesis (PubMed:31789463, PubMed:32375023).
CC {ECO:0000269|PubMed:30354798, ECO:0000269|PubMed:31789463,
CC ECO:0000269|PubMed:32375023}.
CC -!- SUBUNIT: Forms homodimers (via head domain) (PubMed:32375023).
CC Interacts with CEP170 (PubMed:30354798, PubMed:31789463). Interacts
CC with PCM1 and CEP131 (PubMed:31789463). Binds tubulin
CC (PubMed:31789463). {ECO:0000269|PubMed:30354798,
CC ECO:0000269|PubMed:31789463, ECO:0000269|PubMed:32375023}.
CC -!- INTERACTION:
CC Q9Y6R9; Q5SW79: CEP170; NbExp=3; IntAct=EBI-10961230, EBI-1104799;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:30354798,
CC ECO:0000269|PubMed:31789463}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:30354798, ECO:0000269|PubMed:31789463}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:32375023}.
CC Note=Localization at the centriolar satellite is dependent on intact
CC microtubule network (PubMed:30354798). Localizes at the centriole
CC subdistal appendages and proximal ends (PubMed:31789463). Localized to
CC centrosomal/satellite-like structures with the onset of centrosome
CC separation in early G2 (PubMed:30354798). {ECO:0000269|PubMed:30354798,
CC ECO:0000269|PubMed:31789463}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y6R9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6R9-2; Sequence=VSP_053741;
CC -!- DOMAIN: The coiled-coil domains are involved in microtubule-binding.
CC {ECO:0000269|PubMed:32375023}.
CC -!- MISCELLANEOUS: The N-terminal 3D structure (head domain) resembles that
CC of NHEJ1/XLF, PAXX, SASS6 and XRCC4. {ECO:0000269|PubMed:32375023}.
CC -!- SIMILARITY: Belongs to the CCDC61 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD38244.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAD38244.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF98366.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GQ375050; ACT79331.1; -; mRNA.
DR EMBL; AC007785; AAD38244.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011545; AAF98366.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS46120.2; -. [Q9Y6R9-1]
DR RefSeq; NP_001254652.1; NM_001267723.1. [Q9Y6R9-1]
DR RefSeq; XP_005259249.1; XM_005259192.4. [Q9Y6R9-1]
DR RefSeq; XP_011525559.1; XM_011527257.2. [Q9Y6R9-1]
DR PDB; 6HXT; X-ray; 2.55 A; A/B/C=1-143.
DR PDBsum; 6HXT; -.
DR AlphaFoldDB; Q9Y6R9; -.
DR SMR; Q9Y6R9; -.
DR BioGRID; 609841; 39.
DR IntAct; Q9Y6R9; 58.
DR MINT; Q9Y6R9; -.
DR STRING; 9606.ENSP00000471454; -.
DR iPTMnet; Q9Y6R9; -.
DR PhosphoSitePlus; Q9Y6R9; -.
DR BioMuta; CCDC61; -.
DR DMDM; 160380583; -.
DR EPD; Q9Y6R9; -.
DR jPOST; Q9Y6R9; -.
DR MassIVE; Q9Y6R9; -.
DR MaxQB; Q9Y6R9; -.
DR PeptideAtlas; Q9Y6R9; -.
DR PRIDE; Q9Y6R9; -.
DR ProteomicsDB; 86781; -. [Q9Y6R9-1]
DR Antibodypedia; 49264; 124 antibodies from 18 providers.
DR DNASU; 729440; -.
DR Ensembl; ENST00000536603.5; ENSP00000444279.1; ENSG00000104983.8. [Q9Y6R9-2]
DR Ensembl; ENST00000594087.1; ENSP00000469466.1; ENSG00000104983.8. [Q9Y6R9-2]
DR Ensembl; ENST00000595358.5; ENSP00000471454.1; ENSG00000104983.8. [Q9Y6R9-1]
DR GeneID; 729440; -.
DR KEGG; hsa:729440; -.
DR MANE-Select; ENST00000595358.5; ENSP00000471454.1; NM_001267723.2; NP_001254652.1.
DR UCSC; uc021uwd.3; human. [Q9Y6R9-1]
DR CTD; 729440; -.
DR GeneCards; CCDC61; -.
DR HGNC; HGNC:33629; CCDC61.
DR HPA; ENSG00000104983; Low tissue specificity.
DR neXtProt; NX_Q9Y6R9; -.
DR OpenTargets; ENSG00000104983; -.
DR VEuPathDB; HostDB:ENSG00000104983; -.
DR eggNOG; ENOG502QRAS; Eukaryota.
DR GeneTree; ENSGT00940000154133; -.
DR HOGENOM; CLU_038746_1_0_1; -.
DR InParanoid; Q9Y6R9; -.
DR OMA; THRIKDK; -.
DR OrthoDB; 1433381at2759; -.
DR TreeFam; TF329415; -.
DR PathwayCommons; Q9Y6R9; -.
DR SignaLink; Q9Y6R9; -.
DR BioGRID-ORCS; 729440; 16 hits in 1073 CRISPR screens.
DR ChiTaRS; CCDC61; human.
DR GenomeRNAi; 729440; -.
DR Pharos; Q9Y6R9; Tdark.
DR PRO; PR:Q9Y6R9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y6R9; protein.
DR Bgee; ENSG00000104983; Expressed in right uterine tube and 104 other tissues.
DR ExpressionAtlas; Q9Y6R9; baseline and differential.
DR Genevisible; Q9Y6R9; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0120103; C:centriolar subdistal appendage; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IMP:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0098534; P:centriole assembly; IDA:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..512
FT /note="Centrosomal protein CCDC61"
FT /id="PRO_0000311255"
FT REGION 1..143
FT /note="Head domain"
FT /evidence="ECO:0000303|PubMed:32375023"
FT REGION 276..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 178..205
FT /evidence="ECO:0000255"
FT COILED 248..275
FT /evidence="ECO:0000255"
FT COMPBIAS 348..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 285
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 185..364
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_053741"
FT MUTAGEN 128..129
FT /note="FD->EA: Loss of dimerization."
FT /evidence="ECO:0000269|PubMed:32375023"
FT MUTAGEN 259
FT /note="K->E: Loss of microtubule-binding; when associated
FT with E-263, E-266, E-268 and E-270."
FT /evidence="ECO:0000269|PubMed:32375023"
FT MUTAGEN 263
FT /note="R->E: Loss of microtubule-binding; when associated
FT with E-259, E-266, E-268 and E-270."
FT /evidence="ECO:0000269|PubMed:32375023"
FT MUTAGEN 266
FT /note="R->E: Loss of microtubule-binding; when associated
FT with E-259, E-263, E-268 and E-270."
FT /evidence="ECO:0000269|PubMed:32375023"
FT MUTAGEN 268
FT /note="R->E: Loss of microtubule-binding; when associated
FT with E-259, E-263, E-266 and E-270."
FT /evidence="ECO:0000269|PubMed:32375023"
FT MUTAGEN 270
FT /note="K->E: Loss of microtubule-binding; when associated
FT with E-259, E-263, E-266 and E-268."
FT /evidence="ECO:0000269|PubMed:32375023"
FT CONFLICT 389
FT /note="Q -> R (in Ref. 1; ACT79331)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="P -> L (in Ref. 1; ACT79331)"
FT /evidence="ECO:0000305"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:6HXT"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:6HXT"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:6HXT"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:6HXT"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:6HXT"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:6HXT"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:6HXT"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:6HXT"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:6HXT"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:6HXT"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:6HXT"
SQ SEQUENCE 512 AA; 57368 MW; 2DCB8BAFAF5B532E CRC64;
MDQPAGLQVD YVFRGVEHAV RVMVSGQVLE LEVEDRMTAD QWRGEFDAGF IEDLTHKTGN
FKQFNIFCHM LESALTQSSE SVTLDLLTYT DLESLRNRKM GGRPGSLAPR SAQLNSKRYL
ILIYSVEFDR IHYPLPLPYQ GKPDPVVLQG IIRSLKEELG RLQGLDGQNT RDTRENEIWH
LREQVSRLAS EKRELEAQLG RSREEALAGR AARQEAEALR GLVRGLELEL RQERGLGHRV
AGRRGQDCRR LAKELEEAKA SERSLRARLK TLTSELALYK RGRRTPPVQP PPTREDRASS
SRERSASRGR GAARSSSRES GRGSRGRGRP ARPSPSPTGG RALRFDPTAF VKAKERKQRE
IQMKQQQRNR LGSGGSGDGP SVSWSRQTQP PAALTGRGDA PNRSRNRSSS VDSFRSRCSS
ASSCSDLEDF SESLSRGGHR RRGKPPSPTP WSGSNMKSPP VERSHHQKSL ANSGGWVPIK
EYSSEHQAAD MAEIDARLKA LQEYMNRLDM RS
