C2CD3_MOUSE
ID C2CD3_MOUSE Reviewed; 2323 AA.
AC Q52KB6; E9QL99; Q3UFQ3; Q80V48; Q8BXE5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=C2 domain-containing protein 3;
DE AltName: Full=Protein hearty;
GN Name=C2cd3; Synonyms=Hty;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-402 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 379-2323 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 71-2323 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1232-2323 (ISOFORM 3).
RC STRAIN=129, and C57BL/6J; TISSUE=Head, and Mammary tumor;
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 FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=19004860; DOI=10.1242/dev.029835;
RA Hoover A.N., Wynkoop A., Zeng H., Jia J., Niswander L.A., Liu A.;
RT "C2cd3 is required for cilia formation and Hedgehog signaling in mouse.";
RL Development 135:4049-4058(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, 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).
RN [6]
RP FUNCTION.
RX PubMed=24997988; DOI=10.1038/ng.3031;
RA Thauvin-Robinet C., Lee J.S., Lopez E., Herranz-Perez V., Shida T.,
RA Franco B., Jego L., Ye F., Pasquier L., Loget P., Gigot N., Aral B.,
RA Lopes C.A., St-Onge J., Bruel A.L., Thevenon J., Gonzalez-Granero S.,
RA Alby C., Munnich A., Vekemans M., Huet F., Fry A.M., Saunier S.,
RA Riviere J.B., Attie-Bitach T., Garcia-Verdugo J.M., Faivre L.,
RA Megarbane A., Nachury M.V.;
RT "The oral-facial-digital syndrome gene C2CD3 encodes a positive regulator
RT of centriole elongation.";
RL Nat. Genet. 46:905-911(2014).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IFT88; BBS4 AND PCM1.
RX PubMed=24469809; DOI=10.1073/pnas.1318737111;
RA Ye X., Zeng H., Ning G., Reiter J.F., Liu A.;
RT "C2cd3 is critical for centriolar distal appendage assembly and ciliary
RT vesicle docking in mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2164-2169(2014).
CC -!- FUNCTION: Component of the centrioles that acts as a positive regulator
CC of centriole elongation (PubMed:24997988). Promotes assembly of
CC centriolar distal appendage, a structure at the distal end of the
CC mother centriole that acts as an anchor of the cilium, and is required
CC for recruitment of centriolar distal appendages proteins CEP83, SCLT1,
CC CEP89, FBF1 and CEP164. Not required for centriolar satellite integrity
CC or RAB8 activation (PubMed:24469809). Required for primary cilium
CC formation. Required for sonic hedgehog/SHH signaling and for
CC proteolytic processing of GLI3 (PubMed:19004860).
CC {ECO:0000269|PubMed:19004860, ECO:0000269|PubMed:24469809,
CC ECO:0000269|PubMed:24997988}.
CC -!- SUBUNIT: Interacts with OFD1; OFD1 may act as a negative regulator of
CC C2CD3. Associates with the BBSome complex (By similarity). Interacts
CC with IFT88, BBS4 and PCM1. {ECO:0000250, ECO:0000269|PubMed:24469809}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole. Note=Localizes to centrioles and procentrioles both in
CC interphase and mitosis. Localizes to centriolar satellites,
CC localization is dependent on PCM1 and dynein-mediated retrograde
CC transport. Also localizes to the distal ends of the mother and daughter
CC centrioles (PubMed:24469809). {ECO:0000269|PubMed:24469809}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q52KB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q52KB6-2; Sequence=VSP_029449, VSP_029450;
CC Name=3;
CC IsoId=Q52KB6-3; Sequence=VSP_029451, VSP_029452;
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in embryos between 8.5 dpc
CC and 10.5 dpc. {ECO:0000269|PubMed:19004860}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality between 11 dpc and 13 dpc.
CC Embryos show multiple defects including neural tube defects, abnormal
CC dorsal-ventral patterning of the spinal cord, a defect in left-right
CC axis determination and severe polydactyly (extra digits).
CC {ECO:0000269|PubMed:19004860}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94430.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK047412; BAC33048.1; -; mRNA.
DR EMBL; AK148365; BAE28507.1; -; mRNA.
DR EMBL; AC117215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC151839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046408; AAH46408.1; -; mRNA.
DR EMBL; BC094430; AAH94430.1; ALT_INIT; mRNA.
DR CCDS; CCDS57568.1; -. [Q52KB6-1]
DR RefSeq; NP_001017985.2; NM_001017985.2. [Q52KB6-1]
DR AlphaFoldDB; Q52KB6; -.
DR BioGRID; 234966; 1.
DR IntAct; Q52KB6; 1.
DR STRING; 10090.ENSMUSP00000062637; -.
DR iPTMnet; Q52KB6; -.
DR PhosphoSitePlus; Q52KB6; -.
DR MaxQB; Q52KB6; -.
DR PaxDb; Q52KB6; -.
DR PRIDE; Q52KB6; -.
DR ProteomicsDB; 281712; -. [Q52KB6-1]
DR ProteomicsDB; 281713; -. [Q52KB6-2]
DR ProteomicsDB; 281714; -. [Q52KB6-3]
DR Antibodypedia; 48039; 147 antibodies from 19 providers.
DR Ensembl; ENSMUST00000051777; ENSMUSP00000062637; ENSMUSG00000047248. [Q52KB6-1]
DR GeneID; 277939; -.
DR KEGG; mmu:277939; -.
DR UCSC; uc029wni.1; mouse. [Q52KB6-1]
DR CTD; 26005; -.
DR MGI; MGI:2142166; C2cd3.
DR VEuPathDB; HostDB:ENSMUSG00000047248; -.
DR eggNOG; ENOG502QRQ8; Eukaryota.
DR GeneTree; ENSGT00510000048072; -.
DR InParanoid; Q52KB6; -.
DR OMA; XLSKELL; -.
DR OrthoDB; 88005at2759; -.
DR PhylomeDB; Q52KB6; -.
DR TreeFam; TF323591; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 277939; 6 hits in 58 CRISPR screens.
DR ChiTaRS; C2cd3; mouse.
DR PRO; PR:Q52KB6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q52KB6; protein.
DR Bgee; ENSMUSG00000047248; Expressed in ventricular zone and 221 other tissues.
DR ExpressionAtlas; Q52KB6; baseline and differential.
DR Genevisible; Q52KB6; MM.
DR GO; GO:0034451; C:centriolar satellite; IDA:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0061511; P:centriole elongation; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0021997; P:neural plate axis specification; IMP:MGI.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; ISS:UniProtKB.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
DR GO; GO:0030162; P:regulation of proteolysis; IDA:MGI.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:MGI.
DR CDD; cd08683; C2_C2cd3; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR037775; C2_C2CD3.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR Pfam; PF00168; C2; 3.
DR SMART; SM00239; C2; 5.
DR SUPFAM; SSF49562; SSF49562; 4.
DR PROSITE; PS50004; C2; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..2323
FT /note="C2 domain-containing protein 3"
FT /id="PRO_0000311240"
FT DOMAIN 504..663
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 771..903
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 969..1131
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1155..1323
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1383..1517
FT /note="C2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1598..1726
FT /note="C2 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1798..1824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1891..1918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1952..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2074..2163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2182..2231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2261..2323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1552..1572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1952..1969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2107..2124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2145..2163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2185..2202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4AC94"
FT MOD_RES 1871
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4AC94"
FT VAR_SEQ 1941..1943
FT /note="DLQ -> GDY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029449"
FT VAR_SEQ 1944..2323
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029450"
FT VAR_SEQ 2114..2130
FT /note="QPAQGSPSQSGVCEGGA -> CPEALSPQTLLHPSQPS (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029451"
FT VAR_SEQ 2131..2323
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029452"
FT CONFLICT 483
FT /note="Q -> K (in Ref. 1; BAC33048)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="E -> G (in Ref. 3; AAH94430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2323 AA; 255346 MW; 5C0A87CC728245E0 CRC64;
MKQRKGQGPG GGRGRKKRGL SDISPSTSLP PLVEGQLRCF LKLTINKVVW KIAKPPTSVL
VRVRWWGETS DGTLFCPRDA LQTEPKAVRT TTRYGIRCGP KQFTSYLTDM AVLVLEVITK
FDHLPVGRVQ ISGLAQLSPT HQINGFFTIV SPASKKLGEL QVSLALEPLS ETYDSYKPLP
ATEVTKNVLL SERELRENTE SSNTQSMIPS RSCRGPAIKI DGKELAGHSS RSTTPRGKDH
LYFAENSDAV KGSLCGLQQH LNQGTNVETI TLRGKAPQKQ LSLLNSSEFQ PQISTVAKSH
SDSCILSSNT PPAKDLLSAL LEQGNKLRNA MLISAMNSNP DTSMLLDKVP PPMTEAIPRS
SALNSSENHF KGHSADHLLP LADTGAIQLL LGSAELSQGH FWNGLGSPPD SPTPGSDEYC
SSDLNDPQYD QSLLENLFYT VPKSDVGTSE LPSEDDGVEP SRTMNQSKAS GRSKVVESKE
QKQKRAAVKK SRNPIDQQEL SRTPGHTPAM SLSVDRLALL GRVHSVRIIV ETMGVPPDSP
HMTPSRKNFA GKPPKPTAAK KRTFFVEYHF PVGFSKSGLG KTALITEVVR LASSKITDGV
VKFQQRFVCP VEFGGPMIEH WWDSNLIFQI YAKKTPQKKP EVIGSASLPL RAVIQSELLS
FSSQLPVQQE NGLSSLGPLK VTMELVLGHK DFTGISAKLS SSTQPAPVSA ATSSDTILPE
TGQDTACTRN PQSSNKIHEE TTKKTQNLVL PDQESANSVA SNSSIFMAVP SCNLVHQING
SNKESGLLLH VLLMVPDGKD FVFGEREKQP SCNVYLNCKL FSTEEVTRSV VSWGTAQPVF
NFSQVIPVSL TSKCLERLKN NVMIIETWNK VRSPGQDKLL GLVKLPLHQF YMSFKDPKIS
RLLLDARYPV VAVDSYMPVI DVFSGHQNGS LRVFLAMGSS AQIMMLQRLK NEEGTLPPFS
PRPAHFLDQP PVASVAMPEK QGTRLMEHHF EFCVAMVKGL MPLQATVWGE ADCYVQYYFP
FQDSQPSVLQ GPDFLENGIT LKPFRTSTTL CVPDPVFNSE HHHSLLLPTD VPVQRLLLSA
FSSQGLVPGG GVQFEVWCRY YYPNVRDQMV AKGTLPLSRV CAMVTMQYRE DVGMQSFNLP
LTSRLEHSKE LKNQSSGFLD VGLRYRRSPR TAEGILAARA VSISVHIIRA CGLQAAAKAL
AEQEPALQFS ATVGVNASVT AHLSFLPKGE QRQTRPVACS FCPEFSHHIE FPCNLVTQHC
SGEACFLAEL LEFAEIIFAI YHENTKSVSD ITSIQSCKDY LLGIVKVPTK DLLVKRSGIT
GWYPVILPED KGLPQDLDLM QKIVGGLELS VSFAHPGDRE RVLEAAELLG WSFESIPKDL
VKKEEEVPAT VTISTPRLWL PIHCVLLAGH MNIHKNTYCY LRYKLYNQEA FWTPLRKPKE
STNKNQVLIT FKASKRAEVT RSQSLLWYFR EEKLEIQVWR AYGNDNLERP HQTDSWIGSA
YVDLSRLGEK SPRTLTISGV YPLFGRNASD LSGAALRIHV LLSPLSPHTE PARELDSMDC
SSHSESEQHP RKSDALQLSP PHVLQTSPTS TQVHGNSAAA QVCPAQEGPP ELAGTFAVSI
LVERAMHLSL KGSPLTDRKV SVPSCCVSFA TATELSPVYT HVVENTDSPI WGFHQQARLS
KELLLDPHQT LVFKVWHKGD EERVVGFASV DLSPLLSGFQ FICGWYNITD FSGECQGQIK
VAISPMESLM HLKEERQARR GIDTPGALIP LFSALSFPAS AGCDAFPRPI ARHVEGQLAH
TSPKEDGLSS PARNGAIRSQ AARHEEHVQN IRRFHESLQH GEAVLTSDEK LTTAPSSSHT
SILTSLRKNL SELDEIQKYF SQKLSKPFLP FSSQSSPAVS QSQESQRDPV AAGTGRQDPE
NQCILEKSNH LVSQVSSLIS DLQTLTRGSQ AALTSQQARS RSRAVTTIPD AQGTEAAGEG
STTLEEPLAG AIEASTDSLP PPVEEPSKGG GMLHESLEQT MPITRVQSID DTEVGPDYSD
EDYEEDIIEP RTLNEITTVT DRTSPWSSFM SDMSEVLSPQ PTEVQREGPS CPPEPFPREE
LKVKSSPQKA VSPQPAQGSP SQSGVCEGGA YKIEVEDLAS AKPQPVPSLT FSEAQEGSDS
VGWRASQINQ VRKPMPEMLA ESEAFSSEFS DSSESFETFP LHLPSQSKRE DYKDSPAVRQ
KQVPTGSEVS TRQTLLLPEP VVVPNFFLPP QQLEASLRMI SHSPGLPPAA TTDQDKSEAT
RGALAQRPCR PRPYSIPPNL PEEETRRIAR IFSSQYSKKT EET
