CE164_MOUSE
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 25-MAY-2022, entry version 106.
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},
RC Visual cortex {ECO:0000312|EMBL:BAE34604.1}, and
RC Wolffian duct {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; Q5DU05; -.
DR PRIDE; Q5DU05; -.
DR ProteomicsDB; 281445; -. [Q5DU05-1]
DR ProteomicsDB; 281446; -. [Q5DU05-2]
DR ProteomicsDB; 281447; -. [Q5DU05-3]
DR UCSC; uc009pgb.2; mouse. [Q5DU05-2]
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: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 InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 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
