CEP83_HUMAN
ID CEP83_HUMAN Reviewed; 701 AA.
AC Q9Y592; A4FVB1; Q08AP1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Centrosomal protein of 83 kDa;
DE Short=Cep83;
DE AltName: Full=Coiled-coil domain-containing protein 41;
DE AltName: Full=Renal carcinoma antigen NY-REN-58;
GN Name=CEP83; Synonyms=CCDC41;
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 1), AND IDENTIFICATION AS A RENAL
RP CANCER ANTIGEN.
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-642 (ISOFORM 1).
RC TISSUE=Retinoblastoma;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-567 (ISOFORM 1).
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23348840; DOI=10.1101/gad.207043.112;
RA Tanos B.E., Yang H.J., Soni R., Wang W.J., Macaluso F.P., Asara J.M.,
RA Tsou M.F.;
RT "Centriole distal appendages promote membrane docking, leading to cilia
RT initiation.";
RL Genes Dev. 27:163-168(2013).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP164 AND IFT20.
RX PubMed=23530209; DOI=10.1073/pnas.1220927110;
RA Joo K., Kim C.G., Lee M.S., Moon H.Y., Lee S.H., Kim M.J., Kweon H.S.,
RA Park W.Y., Kim C.H., Gleeson J.G., Kim J.;
RT "CCDC41 is required for ciliary vesicle docking to the mother centriole.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5987-5992(2013).
RN [7]
RP INTERACTION WITH CEP164 AND IFT20, VARIANTS NPHP18 PRO-87; 112-PRO--LEU-117
RP DEL; PRO-511; GLU-684 DEL AND GLN-692 DEL, AND CHARACTERIZATION OF VARIANTS
RP NPHP18 PRO-87; 112-PRO--LEU-117 DEL; PRO-511; GLU-684 DEL AND GLN-692 DEL.
RX PubMed=24882706; DOI=10.1016/j.ajhg.2014.05.002;
RA Failler M., Gee H.Y., Krug P., Joo K., Halbritter J., Belkacem L.,
RA Filhol E., Porath J.D., Braun D.A., Schueler M., Frigo A., Alibeu O.,
RA Masson C., Brochard K., Hurault de Ligny B., Novo R., Pietrement C.,
RA Kayserili H., Salomon R., Gubler M.C., Otto E.A., Antignac C., Kim J.,
RA Benmerah A., Hildebrandt F., Saunier S.;
RT "Mutations of CEP83 cause infantile nephronophthisis and intellectual
RT disability.";
RL Am. J. Hum. Genet. 94:905-914(2014).
CC -!- FUNCTION: Component of the distal appendage region of the centriole
CC involved in the initiation of primary cilium assembly. May collaborate
CC with IFT20 in the trafficking of ciliary membrane proteins from the
CC Golgi complex to the cilium during the initiation of primary cilium
CC assembly. {ECO:0000269|PubMed:23348840, ECO:0000269|PubMed:23530209}.
CC -!- SUBUNIT: Interacts with CEP164 and IFT20. {ECO:0000269|PubMed:23530209,
CC ECO:0000269|PubMed:24882706}.
CC -!- INTERACTION:
CC Q9Y592-2; P18848: ATF4; NbExp=3; IntAct=EBI-11123098, EBI-492498;
CC Q9Y592-2; O43439-4: CBFA2T2; NbExp=3; IntAct=EBI-11123098, EBI-11954144;
CC Q9Y592-2; Q9Y592-2: CEP83; NbExp=3; IntAct=EBI-11123098, EBI-11123098;
CC Q9Y592-2; Q96DZ5: CLIP3; NbExp=3; IntAct=EBI-11123098, EBI-12823145;
CC Q9Y592-2; Q08426: EHHADH; NbExp=3; IntAct=EBI-11123098, EBI-2339219;
CC Q9Y592-2; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-11123098, EBI-1216080;
CC Q9Y592-2; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-11123098, EBI-11984663;
CC Q9Y592-2; P07947: YES1; NbExp=3; IntAct=EBI-11123098, EBI-515331;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:23348840,
CC ECO:0000269|PubMed:23530209}. Note=Localizes specifically to the distal
CC appendage region of the centriole, which anchors the mother centriole
CC to the plasma membrane. Localizes to centrioles at all stages of the
CC cell cycle, including mitosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y592-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y592-2; Sequence=VSP_037760, VSP_037761, VSP_037762;
CC -!- DISEASE: Nephronophthisis 18 (NPHP18) [MIM:615862]: An autosomal
CC recessive disorder characterized by chronic tubulointerstitial
CC nephritis resulting in end-stage renal disease in early childhood.
CC Extrarenal manifestations, including intellectual disability or liver
CC changes, may occur in some patients. {ECO:0000269|PubMed:24882706}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the CEP83 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD42881.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAI25087.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF155115; AAD42881.1; ALT_FRAME; mRNA.
DR EMBL; AC073655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053614; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC125086; AAI25087.1; ALT_INIT; mRNA.
DR EMBL; BC125087; AAI25088.1; -; mRNA.
DR EMBL; AK056316; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS41820.1; -. [Q9Y592-1]
DR RefSeq; NP_001035858.1; NM_001042399.1. [Q9Y592-1]
DR RefSeq; NP_001333386.1; NM_001346457.1. [Q9Y592-1]
DR RefSeq; NP_057206.2; NM_016122.2. [Q9Y592-1]
DR RefSeq; XP_011536726.1; XM_011538424.1. [Q9Y592-1]
DR RefSeq; XP_016874874.1; XM_017019385.1. [Q9Y592-1]
DR RefSeq; XP_016874875.1; XM_017019386.1. [Q9Y592-1]
DR AlphaFoldDB; Q9Y592; -.
DR SMR; Q9Y592; -.
DR BioGRID; 119321; 41.
DR IntAct; Q9Y592; 35.
DR MINT; Q9Y592; -.
DR STRING; 9606.ENSP00000380911; -.
DR iPTMnet; Q9Y592; -.
DR PhosphoSitePlus; Q9Y592; -.
DR BioMuta; CEP83; -.
DR DMDM; 97045295; -.
DR EPD; Q9Y592; -.
DR jPOST; Q9Y592; -.
DR MassIVE; Q9Y592; -.
DR MaxQB; Q9Y592; -.
DR PaxDb; Q9Y592; -.
DR PeptideAtlas; Q9Y592; -.
DR PRIDE; Q9Y592; -.
DR ProteomicsDB; 86318; -. [Q9Y592-1]
DR ProteomicsDB; 86319; -. [Q9Y592-2]
DR Antibodypedia; 52583; 92 antibodies from 18 providers.
DR DNASU; 51134; -.
DR Ensembl; ENST00000339839.9; ENSP00000344655.5; ENSG00000173588.16. [Q9Y592-1]
DR Ensembl; ENST00000397809.10; ENSP00000380911.4; ENSG00000173588.16. [Q9Y592-1]
DR GeneID; 51134; -.
DR KEGG; hsa:51134; -.
DR MANE-Select; ENST00000397809.10; ENSP00000380911.4; NM_016122.3; NP_057206.2.
DR UCSC; uc058ruu.1; human. [Q9Y592-1]
DR CTD; 51134; -.
DR DisGeNET; 51134; -.
DR GeneCards; CEP83; -.
DR GeneReviews; CEP83; -.
DR HGNC; HGNC:17966; CEP83.
DR HPA; ENSG00000173588; Low tissue specificity.
DR MalaCards; CEP83; -.
DR MIM; 615847; gene.
DR MIM; 615862; phenotype.
DR neXtProt; NX_Q9Y592; -.
DR OpenTargets; ENSG00000173588; -.
DR Orphanet; 93591; Infantile nephronophthisis.
DR PharmGKB; PA142672158; -.
DR VEuPathDB; HostDB:ENSG00000173588; -.
DR eggNOG; ENOG502QWE2; Eukaryota.
DR GeneTree; ENSGT00940000154003; -.
DR InParanoid; Q9Y592; -.
DR OMA; KHQTENR; -.
DR PhylomeDB; Q9Y592; -.
DR PathwayCommons; Q9Y592; -.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR SignaLink; Q9Y592; -.
DR BioGRID-ORCS; 51134; 10 hits in 1077 CRISPR screens.
DR ChiTaRS; CEP83; human.
DR GenomeRNAi; 51134; -.
DR Pharos; Q9Y592; Tdark.
DR PRO; PR:Q9Y592; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y592; protein.
DR Bgee; ENSG00000173588; Expressed in right uterine tube and 148 other tissues.
DR ExpressionAtlas; Q9Y592; baseline and differential.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0097539; C:ciliary transition fiber; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0051660; P:establishment of centrosome localization; IBA:GO_Central.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
DR GO; GO:0048278; P:vesicle docking; IMP:UniProtKB.
DR InterPro; IPR029631; Cep83.
DR PANTHER; PTHR23170:SF2; PTHR23170:SF2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Ciliopathy; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Nephronophthisis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..701
FT /note="Centrosomal protein of 83 kDa"
FT /id="PRO_0000234495"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 40..634
FT /evidence="ECO:0000255"
FT COILED 665..698
FT /evidence="ECO:0000255"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D5R3"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037760"
FT VAR_SEQ 570..601
FT /note="RKSLHENKLKRLQEKVEVLEAKKEELETENQV -> LEQDLELGCPSVTDTY
FT RESVFPPPPLKRDLLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037761"
FT VAR_SEQ 602..693
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037762"
FT VARIANT 78
FT /note="Q -> R (in dbSNP:rs2271979)"
FT /id="VAR_058397"
FT VARIANT 87
FT /note="L -> P (in NPHP18; does not affect interaction with
FT CEP164 and IFT20)"
FT /evidence="ECO:0000269|PubMed:24882706"
FT /id="VAR_071266"
FT VARIANT 112..117
FT /note="Missing (in NPHP18; does not affect interaction with
FT CEP164 and IFT20)"
FT /evidence="ECO:0000269|PubMed:24882706"
FT /id="VAR_071267"
FT VARIANT 511
FT /note="R -> P (in NPHP18; does not interact with CEP164 and
FT IFT20; dbSNP:rs587777487)"
FT /evidence="ECO:0000269|PubMed:24882706"
FT /id="VAR_071268"
FT VARIANT 684
FT /note="Missing (in NPHP18; accumulates in the nucleus)"
FT /evidence="ECO:0000269|PubMed:24882706"
FT /id="VAR_071269"
FT VARIANT 692
FT /note="Missing (in NPHP18; accumulates in the nucleus; does
FT not interact with CEP164 and IFT20)"
FT /evidence="ECO:0000269|PubMed:24882706"
FT /id="VAR_071270"
FT CONFLICT 267
FT /note="E -> G (in Ref. 1; AAD42881)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="I -> L (in Ref. 1; AAD42881)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="E -> D (in Ref. 1; AAD42881)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="R -> C (in Ref. 3; AAI25087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 82940 MW; DF757C84BE784D07 CRC64;
MVVSTFTDMD TFPNNFPPGG DSGLTGSQSE FQKMLIDERL RCEHHKANYQ TLKAEHTRLQ
NEHVKLQNEL KHLFNEKQTQ QEKLQLLLEE LRGELVEKTK DLEEMKLQIL TPQKLELLRA
QIQQELETPM RERFRNLDEE VEKYRAVYNK LRYEHTFLKS EFEHQKEEYA RILDEGKIKY
ESEIARLEED KEELRNQLLN VDLTKDSKRV EQLAREKVYL CQKLKGLEAE VAELKAEKEN
SEAQVENAQR IQVRQLAEMQ ATVRSLEAEK QSANLRAERL EKELQSSSEQ NTFLINKLHK
AEREINTLSS KVKELKHSNK LEITDIKLET ARAKSELERE RNKIQSELDG LQSDNEILKA
AVEHHKVLLV EKDRELIRKV QAAKEEGYQK LVVLQDEKLE LENRLADLEK MKVEHDVWRQ
SEKDQYEEKL RASQMAEEIT RKELQSVRLK LQQQIVTIEN AEKEKNENSD LKQQISSLQI
QVTSLAQSEN DLLNSNQMLK EMVERLKQEC RNFRSQAEKA QLEAEKTLEE KQIQWLEEKH
KLHERITDRE EKYNQAKEKL QRAAIAQKKR KSLHENKLKR LQEKVEVLEA KKEELETENQ
VLNRQNVPFE DYTRLQKRLK DIQRRHNEFR SLILVPNMPP TASINPVSFQ SSAMVPSMEL
PFPPHMQEEQ HQRELSLLRK RLEELETTQR KQLEELGSSG E
