ID   CE164_MOUSE             Reviewed;        1446 AA.
AC   Q5DU05; Q3TYF9; Q6NZG6; Q8BQD2; Q8BSI0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   08-NOV-2023, entry version 111.
DE   RecName: Full=Centrosomal protein of 164 kDa {ECO:0000250|UniProtKB:Q9UPV0};
DE            Short=Cep164 {ECO:0000312|EMBL:AAH66145.1};
GN   Name=Cep164 {ECO:0000312|MGI:MGI:2384878};
GN   Synonyms=Kiaa1052 {ECO:0000312|EMBL:BAD90247.1};
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 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   [2] {ECO:0000305, ECO:0000312|EMBL:BAC28073.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-114 (ISOFORMS 1/2/3),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 223-862 (ISOFORM 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1028-1446 (ISOFORM 2).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC28073.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:BAC34489.1}, Visual cortex
RC   {ECO:0000312|EMBL:BAE34604.1}, and Wolffian duct
RC   {ECO:0000312|EMBL:BAC28073.1};
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   [3] {ECO:0000305, ECO:0000312|EMBL:BAD90247.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-1446 (ISOFORM 2).
RC   TISSUE=Fetal brain {ECO:0000312|EMBL:BAD90247.1};
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAH66145.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 909-1446 (ISOFORM 2).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH66145.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH66145.1};
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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, AND SUBCELLULAR LOCATION.
RX   PubMed=22863007; DOI=10.1016/j.cell.2012.06.028;
RA   Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H.,
RA   Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J.,
RA   Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H.,
RA   van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H.,
RA   Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A.,
RA   Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S.,
RA   Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S.,
RA   Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C.,
RA   Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G.,
RA   Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A.,
RA   Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R.,
RA   Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J.,
RA   Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A.,
RA   Hildebrandt F.;
RT   "Exome capture reveals ZNF423 and CEP164 mutations, linking renal
RT   ciliopathies to DNA damage response signaling.";
RL   Cell 150:533-548(2012).
RN   [7]
RP   INTERACTION WITH DZIP1.
RX   PubMed=23955340; DOI=10.1074/jbc.m113.492066;
RA   Wang C., Low W.C., Liu A., Wang B.;
RT   "Centrosomal protein DZIP1 regulates Hedgehog signaling by promoting
RT   cytoplasmic retention of transcription factor GLI3 and affecting
RT   ciliogenesis.";
RL   J. Biol. Chem. 288:29518-29529(2013).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=26337392; DOI=10.1091/mbc.e15-04-0235;
RA   Van de Mark D., Kong D., Loncarek J., Stearns T.;
RT   "MDM1 is a microtubule-binding protein that negatively regulates centriole
RT   duplication.";
RL   Mol. Biol. Cell 26:3788-3802(2015).
CC   -!- FUNCTION: Plays a role in microtubule organization and/or maintenance
CC       for the formation of primary cilia (PC), a microtubule-based structure
CC       that protrudes from the surface of epithelial cells. Plays a critical
CC       role in G2/M checkpoint and nuclear divisions. A key player in the DNA
CC       damage-activated ATR/ATM signaling cascade since it is required for the
CC       proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical
CC       role in chromosome segregation, acting as a mediator required for the
CC       maintenance of genomic stability through modulation of MDC1, RPA and
CC       CHEK1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:22863007}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with ATRIP. Interacts with ATM, ATR
CC       and MDC1. Interacts with XPA (via N-terminus) upon UV irradiation (By
CC       similarity). Interacts with CEP83, CCDC92, TTBK2, DVL3, NPHP3 and
CC       weakly with NPHP4 (By similarity). Interacts with DZIP1
CC       (PubMed:23955340). {ECO:0000250, ECO:0000269|PubMed:23955340}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000269|PubMed:22863007,
CC       ECO:0000269|PubMed:26337392}. Nucleus {ECO:0000250|UniProtKB:Q9UPV0}.
CC       Note=Localizes specifically to very distally located appendage
CC       structures on the mature centriole from which initiate PC formation
CC       (PubMed:26337392). Persisted at centrioles throughout mitosis (By
CC       similarity). In response to DNA damage, it translocates to nuclear foci
CC       that contain the DNA damage response proteins KAT5/TIP60 and CHEK1 (By
CC       similarity). {ECO:0000250|UniProtKB:Q9UPV0,
CC       ECO:0000269|PubMed:26337392}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:16141072};
CC         IsoId=Q5DU05-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072,
CC       ECO:0000269|Ref.3};
CC         IsoId=Q5DU05-2; Sequence=VSP_053075, VSP_053077;
CC       Name=3 {ECO:0000269|PubMed:16141072};
CC         IsoId=Q5DU05-3; Sequence=VSP_053078, VSP_053079;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH66145.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC34489.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC126804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK032890; BAC28073.1; -; mRNA.
DR   EMBL; AK050991; BAC34489.1; ALT_INIT; mRNA.
DR   EMBL; AK158671; BAE34604.1; -; mRNA.
DR   EMBL; AK220365; BAD90247.1; -; mRNA.
DR   EMBL; BC066145; AAH66145.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q5DU05; -.
DR   SMR; Q5DU05; -.
DR   STRING; 10090.ENSMUSP00000114053; -.
DR   iPTMnet; Q5DU05; -.
DR   PhosphoSitePlus; Q5DU05; -.
DR   jPOST; Q5DU05; -.
DR   MaxQB; Q5DU05; -.
DR   PaxDb; 10090-ENSMUSP00000114053; -.
DR   ProteomicsDB; 281445; -. [Q5DU05-1]
DR   ProteomicsDB; 281446; -. [Q5DU05-2]
DR   ProteomicsDB; 281447; -. [Q5DU05-3]
DR   UCSC; uc009pgb.2; mouse. [Q5DU05-2]
DR   AGR; MGI:2384878; -.
DR   MGI; MGI:2384878; Cep164.
DR   eggNOG; ENOG502QR4A; Eukaryota.
DR   InParanoid; Q5DU05; -.
DR   PhylomeDB; Q5DU05; -.
DR   Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR   ChiTaRS; Cep164; mouse.
DR   PRO; PR:Q5DU05; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q5DU05; Protein.
DR   GO; GO:0097729; C:9+2 motile cilium; IDA:MGI.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0097539; C:ciliary transition fiber; IDA:MGI.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 3.30.1470.10; Photosystem I PsaD, reaction center subunit II; 1.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR18902:SF27; CENTROSOMAL PROTEIN OF 164 KDA; 1.
DR   PANTHER; PTHR18902; NUCLEAR MITOTIC APPARATUS PROTEIN 1-RELATED; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division;
KW   Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   DNA damage; DNA repair; Mitosis; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1446
FT                   /note="Centrosomal protein of 164 kDa"
FT                   /id="PRO_0000370737"
FT   DOMAIN          56..89
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   REGION          1..195
FT                   /note="Interaction with ATRIP"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPV0"
FT   REGION          106..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1261..1287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1143..1197
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        109..123
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..550
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPV0"
FT   MOD_RES         1369
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPV0"
FT   MOD_RES         1371
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPV0"
FT   VAR_SEQ         186..188
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT                   /id="VSP_053075"
FT   VAR_SEQ         514..626
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT                   /id="VSP_053077"
FT   VAR_SEQ         515..563
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_053078"
FT   VAR_SEQ         604..608
FT                   /note="EERLW -> EDEEEEGEEEEEEEEKEEEEE (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_053079"
FT   CONFLICT        1021
FT                   /note="Missing (in Ref. 3; BAD90247)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1025
FT                   /note="A -> V (in Ref. 4; AAH66145)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1192
FT                   /note="S -> P (in Ref. 4; AAH66145)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1446 AA;  162601 MW;  14EB2ED0166C0FDE CRC64;
     MARRPILLGD QLVLEEDSDE TYVPSEQEIL DFARVIGIDP IKEPELMWLA REGIEAPLPK
     GWKPCQNITG DLYYFNFDTG QSIWDHPCDE HYRKLVIQER ERWSAPGAIK KKDKKKKKEK
     KNKKDKETSK SPLVLGSPLA LVQAPLWGLA PLRGLGDAPP SALRGSQSVS LGSSADSGHL
     GEPTLPPQGL KAAACAKGLL ASVHEGKNAL SLLTLGEETN EEDEEESDNQ SVRSSSELLK
     NLHLDLGALG GNFEYEESPR TSQPDKKDVS LDSDADRPPT PGKLFSQGAD SSVASANGSK
     SQGRGASPWN PQKENENSDP KASSSQMAPE LDPGGDQPSR ASKKQQAEDP VQAGKEGECR
     RESAAKEPKE ASALENTSDV SEESEIHGHL KDARHSGSEA SGPKSFLGLD LGFRSRISEH
     LLDGDTLSPV LGGGHWEAQG LDQEEQDDSK SSIAEPQSKH TQGSEREHLQ SSLHSQATEE
     GPLQTLEGQP EWKEAEGPGK DSVASPAPLS LLQREQVLSP PASPERAEEK HSQAEELGLE
     QPEAEETEEK VAVCPSSPVS PEVQTAEPAA PQKLFSEAIL KGMELEEDQR LLLEFQKEKP
     QQLEERLWEE EEEEVCQLYQ QKEKSLSLLK AQLQKATAEE KEKEEETKIR EEESRRLVCL
     RAQVQSRTEA FENQIRTEQQ AALQRLREEA ETLQKAERAS LEQKSRRALE QLREQLEAEE
     RSAQAALRAE KEAEKEAALL QLREQLEGER KEAVAGLEKK HSAELEQLCS SLEAKHQEVI
     SSLQKKIEGA QQKEEAQLQE SLGWAEQRAH QKVHQVTEYE QELSSLLRDK RQEVEREHER
     KMDKMKEEHW QEMADARERY EAEERKQRAD LLGHLTGELE RLRRAHEREL ESMRQEQDQQ
     LEDLRRRHRD HERKLQDLEV ELSSRTKDVK ARLAQLNVQE ENIRKEKQLL LDAQRQAALE
     REEATATHQH LEEAKKEHTH LLETKQQLRR TIDDLRVRRV ELESQVDLLQ AQSQRLQKHL
     SSLEAEVQRK QDVLKEMAAE MNASPHPEPG LHIEDLRKSL DTNKNQEVSS SLSLSKEEID
     LSMESVRQFL SAEGVAVRNA KEFLVRQTRS MRRRQTALKA AQQHWRHELA SAQEVDEDLP
     GTEVLGNMRK NLNEETRHLD EMKSAMRKGH DLLKKKEEKL IQLESSLQEE VSDEDTLKGS
     SIKKVTFDLS DMDDLSSESL ESSPVLHITP TPTSADPNKI HYLSSSLQRI SSELNGVLNV
     LGSLNSQPPP QGLGSQPPPP LFTSSLRSSK NVLDPAYSSQ AKLSSLSSIT PMSTQWAWDP
     GQGTKLTSSS SSQTVDDFLL EKWRKYFPSG IPLLSGSPPP PENKLGYVSV SEQLHFLQRS
     HPRVPRTDGV SIQSLIDSNR KWLEHFRNDP KVQLFSSAPK ATTTSNLSNL LQLGLDENNR
     LNVFHY
//