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CCD39_HUMAN
ID   CCD39_HUMAN             Reviewed;         941 AA.
AC   Q9UFE4; B4E2H1;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Coiled-coil domain-containing protein 39 {ECO:0000305};
GN   Name=CCDC39 {ECO:0000312|HGNC:HGNC:25244};
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] (ISOFORM 1).
RC   TISSUE=Trachea;
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 MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
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   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN CILD14, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=21131972; DOI=10.1038/ng.726;
RA   Merveille A.C., Davis E.E., Becker-Heck A., Legendre M., Amirav I.,
RA   Bataille G., Belmont J., Beydon N., Billen F., Clement A., Clercx C.,
RA   Coste A., Crosbie R., de Blic J., Deleuze S., Duquesnoy P., Escalier D.,
RA   Escudier E., Fliegauf M., Horvath J., Hill K., Jorissen M., Just J.,
RA   Kispert A., Lathrop M., Loges N.T., Marthin J.K., Momozawa Y.,
RA   Montantin G., Nielsen K.G., Olbrich H., Papon J.F., Rayet I., Roger G.,
RA   Schmidts M., Tenreiro H., Towbin J.A., Zelenika D., Zentgraf H.,
RA   Georges M., Lequarre A.S., Katsanis N., Omran H., Amselem S.;
RT   "CCDC39 is required for assembly of inner dynein arms and the dynein
RT   regulatory complex and for normal ciliary motility in humans and dogs.";
RL   Nat. Genet. 43:72-78(2011).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21131974; DOI=10.1038/ng.727;
RA   Becker-Heck A., Zohn I.E., Okabe N., Pollock A., Lenhart K.B.,
RA   Sullivan-Brown J., McSheene J., Loges N.T., Olbrich H., Haeffner K.,
RA   Fliegauf M., Horvath J., Reinhardt R., Nielsen K.G., Marthin J.K.,
RA   Baktai G., Anderson K.V., Geisler R., Niswander L., Omran H., Burdine R.D.;
RT   "The coiled-coil domain containing protein CCDC40 is essential for motile
RT   cilia function and left-right axis formation.";
RL   Nat. Genet. 43:79-84(2011).
RN   [6]
RP   INVOLVEMENT IN CILD14, AND VARIANT CILD14 ILE-594.
RX   PubMed=22693285; DOI=10.1136/jmedgenet-2012-100867;
RA   Blanchon S., Legendre M., Copin B., Duquesnoy P., Montantin G., Kott E.,
RA   Dastot F., Jeanson L., Cachanado M., Rousseau A., Papon J.F., Beydon N.,
RA   Brouard J., Crestani B., Deschildre A., Desir J., Dollfus H., Leheup B.,
RA   Tamalet A., Thumerelle C., Vojtek A.M., Escalier D., Coste A., de Blic J.,
RA   Clement A., Escudier E., Amselem S.;
RT   "Delineation of CCDC39/CCDC40 mutation spectrum and associated phenotypes
RT   in primary ciliary dyskinesia.";
RL   J. Med. Genet. 49:410-416(2012).
RN   [7]
RP   INVOLVEMENT IN CILD14.
RX   PubMed=23255504; DOI=10.1002/humu.22261;
RA   Antony D., Becker-Heck A., Zariwala M.A., Schmidts M., Onoufriadis A.,
RA   Forouhan M., Wilson R., Taylor-Cox T., Dewar A., Jackson C., Goggin P.,
RA   Loges N.T., Olbrich H., Jaspers M., Jorissen M., Leigh M.W., Wolf W.E.,
RA   Daniels M.L., Noone P.G., Ferkol T.W., Sagel S.D., Rosenfeld M., Rutman A.,
RA   Dixit A., O'Callaghan C., Lucas J.S., Hogg C., Scambler P.J., Emes R.D.,
RA   Chung E.M., Shoemark A., Knowles M.R., Omran H., Mitchison H.M.,
RA   Al-Turki S., Anderson C., Antony D., Barroso I., Beales P., Bentham J.,
RA   Bertolini S., Bhattacharya S., Calandra S., Carss K., Chatterjee K.,
RA   Cirak S., Cosgrove C., Daly A., Danecek P., Durbin R., Fitzpatrick D.,
RA   Floyd J., Foley R., Franklin C., Futema M., Graham C., Humphries S.,
RA   Hurles M., Joyce C., Leitersdorf E., McCarthy S., Mitchison H.M.,
RA   Muddyman D., Muntoni F., Neil A., O'Rahilly S., Onoufriadis A., Parker V.,
RA   Payne F., Plagnol V., Raymond L., Savage D.B., Scambler P., Schmidts M.,
RA   Schoenmakers N., Seed M., Semple R., Serra E., Stalker J.,
RA   Van Bockxmeer F., van Kogelenberg M., Vijayarangakannan P., Walter K.,
RA   Whittall R., Williamson K.;
RT   "Mutations in CCDC39 and CCDC40 are the major cause of primary ciliary
RT   dyskinesia with axonemal disorganization and absent inner dynein arms.";
RL   Hum. Mutat. 34:462-472(2013).
RN   [8]
RP   INVOLVEMENT IN CILD14.
RX   PubMed=25186273; DOI=10.1183/09031936.00052014;
RA   Raidt J., Wallmeier J., Hjeij R., Onnebrink J.G., Pennekamp P., Loges N.T.,
RA   Olbrich H., Haeffner K., Dougherty G.W., Omran H., Werner C.;
RT   "Ciliary beat pattern and frequency in genetic variants of primary ciliary
RT   dyskinesia.";
RL   Eur. Respir. J. 44:1579-1588(2014).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=27120127; DOI=10.1002/humu.23005;
RA   Jeanson L., Thomas L., Copin B., Coste A., Sermet-Gaudelus I.,
RA   Dastot-Le Moal F., Duquesnoy P., Montantin G., Collot N., Tissier S.,
RA   Papon J.F., Clement A., Louis B., Escudier E., Amselem S., Legendre M.;
RT   "Mutations in GAS8, a gene encoding a nexin-dynein regulatory complex
RT   subunit, cause primary ciliary dyskinesia with axonemal disorganization.";
RL   Hum. Mutat. 37:776-785(2016).
CC   -!- FUNCTION: Required for assembly of dynein regulatory complex (DRC) and
CC       inner dynein arm (IDA) complexes, which are responsible for ciliary
CC       beat regulation, thereby playing a central role in motility in cilia
CC       and flagella (PubMed:21131972). Probably acts together with CCDC40 to
CC       form a molecular ruler that determines the 96 nanometer (nm) repeat
CC       length and arrangements of components in cilia and flagella (By
CC       similarity). Not required for outer dynein arm complexes assembly
CC       (PubMed:21131972). {ECO:0000250|UniProtKB:A8IQT2,
CC       ECO:0000269|PubMed:21131972}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000269|PubMed:21131972, ECO:0000269|PubMed:21131974,
CC       ECO:0000269|PubMed:27120127}. Note=CCDC40 is required for localization
CC       to axonemes. {ECO:0000269|PubMed:21131974}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UFE4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UFE4-2; Sequence=VSP_037014, VSP_037015, VSP_037016;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in nasal brushings and, to a
CC       lesser extent, in lungs and testis. {ECO:0000269|PubMed:21131972}.
CC   -!- DISEASE: Ciliary dyskinesia, primary, 14 (CILD14) [MIM:613807]: A
CC       disorder characterized by abnormalities of motile cilia. Respiratory
CC       infections leading to chronic inflammation and bronchiectasis are
CC       recurrent, due to defects in the respiratory cilia; reduced fertility
CC       is often observed in male patients due to abnormalities of sperm tails.
CC       Half of the patients exhibit randomization of left-right body asymmetry
CC       and situs inversus, due to dysfunction of monocilia at the embryonic
CC       node. Primary ciliary dyskinesia associated with situs inversus is
CC       referred to as Kartagener syndrome. {ECO:0000269|PubMed:21131972,
CC       ECO:0000269|PubMed:22693285, ECO:0000269|PubMed:23255504,
CC       ECO:0000269|PubMed:25186273}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry. The disease is
CC       characterized by primary ciliary dyskinesia with inner dynein arm (IDA)
CC       defects and axonemal dizorganisation: defects in CCDC39 and CCDC40
CC       constitute the major cause of this phenotype.
CC       {ECO:0000269|PubMed:22693285, ECO:0000269|PubMed:23255504}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CCDC39 family. {ECO:0000305}.
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DR   EMBL; AK304270; BAG65133.1; -; mRNA.
DR   EMBL; AL122120; CAB59277.1; -; mRNA.
DR   EMBL; AC068298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS46964.1; -. [Q9UFE4-1]
DR   PIR; T34567; T34567.
DR   RefSeq; NP_852091.1; NM_181426.1. [Q9UFE4-1]
DR   AlphaFoldDB; Q9UFE4; -.
DR   SMR; Q9UFE4; -.
DR   BioGRID; 130945; 4.
DR   IntAct; Q9UFE4; 3.
DR   STRING; 9606.ENSP00000405708; -.
DR   iPTMnet; Q9UFE4; -.
DR   PhosphoSitePlus; Q9UFE4; -.
DR   BioMuta; CCDC39; -.
DR   DMDM; 296439421; -.
DR   EPD; Q9UFE4; -.
DR   MassIVE; Q9UFE4; -.
DR   PaxDb; Q9UFE4; -.
DR   PeptideAtlas; Q9UFE4; -.
DR   PRIDE; Q9UFE4; -.
DR   ProteomicsDB; 84179; -. [Q9UFE4-1]
DR   ProteomicsDB; 84180; -. [Q9UFE4-2]
DR   Antibodypedia; 79042; 110 antibodies from 16 providers.
DR   DNASU; 339829; -.
DR   Ensembl; ENST00000476379.6; ENSP00000417960.2; ENSG00000284862.3. [Q9UFE4-1]
DR   GeneID; 339829; -.
DR   KEGG; hsa:339829; -.
DR   MANE-Select; ENST00000476379.6; ENSP00000417960.2; NM_181426.2; NP_852091.1.
DR   UCSC; uc010hxe.4; human. [Q9UFE4-1]
DR   CTD; 339829; -.
DR   DisGeNET; 339829; -.
DR   GeneCards; CCDC39; -.
DR   GeneReviews; CCDC39; -.
DR   HGNC; HGNC:25244; CCDC39.
DR   HPA; ENSG00000284862; Tissue enhanced (lymphoid tissue, retina).
DR   MalaCards; CCDC39; -.
DR   MIM; 613798; gene.
DR   MIM; 613807; phenotype.
DR   neXtProt; NX_Q9UFE4; -.
DR   Orphanet; 244; Primary ciliary dyskinesia.
DR   PharmGKB; PA142672194; -.
DR   VEuPathDB; HostDB:ENSG00000284862; -.
DR   eggNOG; ENOG502QS0D; Eukaryota.
DR   GeneTree; ENSGT00390000015010; -.
DR   HOGENOM; CLU_009793_2_0_1; -.
DR   InParanoid; Q9UFE4; -.
DR   OMA; LYRTQRQ; -.
DR   OrthoDB; 355514at2759; -.
DR   PhylomeDB; Q9UFE4; -.
DR   TreeFam; TF329312; -.
DR   PathwayCommons; Q9UFE4; -.
DR   SignaLink; Q9UFE4; -.
DR   BioGRID-ORCS; 339829; 10 hits in 1066 CRISPR screens.
DR   ChiTaRS; CCDC39; human.
DR   GenomeRNAi; 339829; -.
DR   Pharos; Q9UFE4; Tbio.
DR   PRO; PR:Q9UFE4; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9UFE4; protein.
DR   Bgee; ENSG00000284862; Expressed in right uterine tube and 93 other tissues.
DR   ExpressionAtlas; Q9UFE4; baseline and differential.
DR   Genevisible; Q9UFE4; HS.
DR   GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:GOC.
DR   GO; GO:0070286; P:axonemal dynein complex assembly; IMP:UniProtKB.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0090660; P:cerebrospinal fluid circulation; IEA:Ensembl.
DR   GO; GO:0003341; P:cilium movement; IMP:SYSCILIA_CCNET.
DR   GO; GO:0060285; P:cilium-dependent cell motility; IMP:UniProtKB.
DR   GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IMP:BHF-UCL.
DR   GO; GO:0071910; P:determination of liver left/right asymmetry; IMP:BHF-UCL.
DR   GO; GO:0035469; P:determination of pancreatic left/right asymmetry; IMP:BHF-UCL.
DR   GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IMP:UniProtKB.
DR   GO; GO:0061966; P:establishment of left/right asymmetry; IEA:Ensembl.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0030317; P:flagellated sperm motility; IMP:SYSCILIA_CCNET.
DR   GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
DR   GO; GO:0036159; P:inner dynein arm assembly; IMP:SYSCILIA_CCNET.
DR   GO; GO:0030324; P:lung development; IMP:BHF-UCL.
DR   GO; GO:0044458; P:motile cilium assembly; IMP:SYSCILIA_CCNET.
DR   GO; GO:0061512; P:protein localization to cilium; IEA:Ensembl.
DR   GO; GO:0003356; P:regulation of cilium beat frequency; IMP:SYSCILIA_CCNET.
DR   InterPro; IPR033290; CCDC39.
DR   PANTHER; PTHR18962; PTHR18962; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell projection; Ciliopathy; Cilium; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Kartagener syndrome; Phosphoprotein;
KW   Primary ciliary dyskinesia; Reference proteome.
FT   CHAIN           1..941
FT                   /note="Coiled-coil domain-containing protein 39"
FT                   /id="PRO_0000234493"
FT   REGION          868..941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          16..122
FT                   /evidence="ECO:0000255"
FT   COILED          164..273
FT                   /evidence="ECO:0000255"
FT   COILED          306..605
FT                   /evidence="ECO:0000255"
FT   COILED          665..825
FT                   /evidence="ECO:0000255"
FT   MOD_RES         892
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D5Y1"
FT   MOD_RES         900
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D5Y1"
FT   VAR_SEQ         1
FT                   /note="M -> MEYIFPNTGVLWSWLINILCNRRIVWFTSSQLPRGPPASSGGHSFHT
FT                   LRERSESRLFVESYAAAWQPPGTSGGASCCSSLSAQVM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_037014"
FT   VAR_SEQ         667..671
FT                   /note="AAQEK -> VMSMS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_037015"
FT   VAR_SEQ         672..941
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_037016"
FT   VARIANT         594
FT                   /note="T -> I (in CILD14; unknown pathological
FT                   significance; dbSNP:rs140505857)"
FT                   /evidence="ECO:0000269|PubMed:22693285"
FT                   /id="VAR_072468"
FT   CONFLICT        452
FT                   /note="Y -> H (in Ref. 1; BAG65133)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        811
FT                   /note="R -> H (in Ref. 1; BAG65133)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   941 AA;  109901 MW;  1B7DAFB1B9A30D14 CRC64;
     MSSEFLAELH WEDGFAIPVA NEENKLLEDQ LSKLKDERAS LQDELREYEE RINSMTSHFK
     NVKQELSITQ SLCKARERET ESEEHFKAIA QRELGRVKDE IQRLENEMAS ILEKKSDKEN
     GIFKATQKLD GLKCQMNWDQ QALEAWLEES AHKDSDALTL QKYAQQDDNK IRALTLQLER
     LTLECNQKRK ILDNELTETI SAQLELDKAA QDFRKIHNER QELIKQWENT IEQMQKRDGD
     IDNCALELAR IKQETREKEN LVKEKIKFLE SEIGNNTEFE KRISVADRKL LKCRTAYQDH
     ETSRIQLKGE LDSLKATVNR TSSDLEALRK NISKIKKDIH EETARLQKTK NHNEIIQTKL
     KEITEKTMSV EEKATNLEDM LKEEEKDVKE VDVQLNLIKG VLFKKAQELQ TETMKEKAVL
     SEIEGTRSSL KHLNHQLQKL DFETLKQQEI MYSQDFHIQQ VERRMSRLKG EINSEEKQAL
     EAKIVELRKS LEEKKSTCGL LETQIKKLHN DLYFIKKAHS KNSDEKQSLM TKINELNLFI
     DRSEKELDKA KGFKQDLMIE DNLLKLEVKR TREMLHSKAE EVLSLEKRKQ QLYTAMEERT
     EEIKVHKTML ASQIRYVDQE RENISTEFRE RLSKIEKLKN RYEILTVVML PPEGEEEKTQ
     AYYVIKAAQE KEELQREGDC LDAKINKAEK EIYALENTLQ VLNSCNNNYK QSFKKVTPSS
     DEYELKIQLE EQKRAVDEKY RYKQRQIREL QEDIQSMENT LDVIEHLANN VKEKLSEKQA
     YSFQLSKETE EQKPKLERVT KQCAKLTKEI RLLKDTKDET MEEQDIKLRE MKQFHKVIDE
     MLVDIIEENT EIRIILQTYF QQSGLELPTA STKGSRQSSR SPSHTSLSAR SSRSTSTSTS
     QSSIKVLELK FPASSSLVGS PSRPSSASSS SSNVKSKKSS K
 
 
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