CNTRL_MOUSE
ID CNTRL_MOUSE Reviewed; 2334 AA.
AC A2AL36; A0A4W6; A0A4X1; A2AL37; A2AL40; Q6KAR8; Q8CHX3; Q9CRM3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Centriolin;
DE AltName: Full=Centrosomal protein 1;
DE AltName: Full=Centrosomal protein of 110 kDa;
DE Short=Cep110;
GN Name=Cntrl; Synonyms=Cep1, Cep110;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis, Thymus, and Wolffian duct;
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 MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1160-2334 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=10688839;
RA Guasch G., Mack G.J., Popovici C., Dastugue N., Birnbaum D., Rattner J.B.,
RA Pebusque M.-J.;
RT "FGFR1 is fused to the centrosome-associated protein CEP110 in the 8p12
RT stem cell myeloproliferative disorder with t(8;9)(p12;q33).";
RL Blood 95:1788-1796(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, 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).
CC -!- FUNCTION: Involved in cell cycle progression and cytokinesis. During
CC the late steps of cytokinesis, anchors exocyst and SNARE complexes at
CC the midbody, thereby allowing secretory vesicle-mediated abscission (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HOOK2. Interacts with EXOC6 and SNAPIN.
CC Associates with the exocyst complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q7Z7A1}. Midbody, Midbody
CC ring {ECO:0000250|UniProtKB:Q7Z7A1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AL36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AL36-2; Sequence=VSP_032051, VSP_032052;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver.
CC {ECO:0000269|PubMed:10688839}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM17906.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM17908.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK020148; BAB32012.3; -; mRNA.
DR EMBL; AK031338; BAC27353.1; -; mRNA.
DR EMBL; AK041715; BAC31039.1; -; mRNA.
DR EMBL; BC038386; AAH38386.1; -; mRNA.
DR EMBL; AL773523; CAM16866.1; -; Genomic_DNA.
DR EMBL; AL845534; CAM16866.1; JOINED; Genomic_DNA.
DR EMBL; AL773523; CAM16867.1; -; Genomic_DNA.
DR EMBL; AL845534; CAM16867.1; JOINED; Genomic_DNA.
DR EMBL; AL773523; CAM16870.1; -; Genomic_DNA.
DR EMBL; AL845534; CAM16870.1; JOINED; Genomic_DNA.
DR EMBL; AL845534; CAM17903.1; -; Genomic_DNA.
DR EMBL; AL773523; CAM17903.1; JOINED; Genomic_DNA.
DR EMBL; AL845534; CAM17904.1; -; Genomic_DNA.
DR EMBL; AL845534; CAM17906.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL773523; CAM17906.1; JOINED; Genomic_DNA.
DR EMBL; AL845534; CAM17908.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL773523; CAM17908.1; JOINED; Genomic_DNA.
DR EMBL; AK131139; BAD21389.1; -; mRNA.
DR RefSeq; XP_006498131.1; XM_006498068.2.
DR AlphaFoldDB; A2AL36; -.
DR SMR; A2AL36; -.
DR BioGRID; 205064; 4.
DR IntAct; A2AL36; 4.
DR STRING; 10090.ENSMUSP00000028237; -.
DR iPTMnet; A2AL36; -.
DR PhosphoSitePlus; A2AL36; -.
DR EPD; A2AL36; -.
DR jPOST; A2AL36; -.
DR MaxQB; A2AL36; -.
DR PaxDb; A2AL36; -.
DR PeptideAtlas; A2AL36; -.
DR PRIDE; A2AL36; -.
DR ProteomicsDB; 283589; -. [A2AL36-1]
DR ProteomicsDB; 283590; -. [A2AL36-2]
DR Antibodypedia; 30137; 35 antibodies from 13 providers.
DR Ensembl; ENSMUST00000028235; ENSMUSP00000028235; ENSMUSG00000057110. [A2AL36-2]
DR Ensembl; ENSMUST00000028237; ENSMUSP00000028237; ENSMUSG00000057110. [A2AL36-1]
DR Ensembl; ENSMUST00000156933; ENSMUSP00000118731; ENSMUSG00000057110. [A2AL36-1]
DR GeneID; 26920; -.
DR UCSC; uc008jjr.2; mouse. [A2AL36-1]
DR UCSC; uc008jjs.2; mouse. [A2AL36-2]
DR CTD; 11064; -.
DR MGI; MGI:1889576; Cntrl.
DR VEuPathDB; HostDB:ENSMUSG00000057110; -.
DR eggNOG; KOG0531; Eukaryota.
DR GeneTree; ENSGT00940000155434; -.
DR HOGENOM; CLU_595226_0_0_1; -.
DR InParanoid; A2AL36; -.
DR OrthoDB; 79816at2759; -.
DR PhylomeDB; A2AL36; -.
DR TreeFam; TF101135; -.
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 BioGRID-ORCS; 26920; 0 hits in 59 CRISPR screens.
DR ChiTaRS; Cntrl; mouse.
DR PRO; PR:A2AL36; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AL36; protein.
DR Bgee; ENSMUSG00000057110; Expressed in undifferentiated genital tubercle and 191 other tissues.
DR ExpressionAtlas; A2AL36; baseline and differential.
DR Genevisible; A2AL36; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0120103; C:centriolar subdistal appendage; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0072687; C:meiotic spindle; IDA:MGI.
DR GO; GO:0090619; C:meiotic spindle pole; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:InterPro.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR028640; CEP110.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR34491:SF2; PTHR34491:SF2; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Leucine-rich repeat; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..2334
FT /note="Centriolin"
FT /id="PRO_0000323676"
FT REPEAT 126..147
FT /note="LRR 1"
FT REPEAT 148..169
FT /note="LRR 2"
FT REPEAT 170..191
FT /note="LRR 3"
FT REPEAT 194..215
FT /note="LRR 4"
FT DOMAIN 228..266
FT /note="LRRCT"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1951..2121
FT /note="Required for centrosome localization"
FT /evidence="ECO:0000250"
FT REGION 1988..2334
FT /note="Sufficient for interaction with HOOK2"
FT /evidence="ECO:0000250"
FT REGION 2291..2334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 265..343
FT /evidence="ECO:0000255"
FT COILED 437..800
FT /evidence="ECO:0000255"
FT COILED 858..1102
FT /evidence="ECO:0000255"
FT COILED 1320..2169
FT /evidence="ECO:0000255"
FT COMPBIAS 21..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2291..2325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7A1"
FT VAR_SEQ 552..559
FT /note="SHMKAQKR -> VSKMGNLD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032051"
FT VAR_SEQ 560..2334
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032052"
FT CONFLICT 8
FT /note="R -> K (in Ref. 2; AAH38386)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="C -> G (in Ref. 1; BAB32012)"
FT /evidence="ECO:0000305"
FT CONFLICT 1219
FT /note="Missing (in Ref. 4; BAD21389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2334 AA; 268880 MW; 43C2CDA65A295857 CRC64;
MKKGSERRLS KAKMPLSSHF PGPSSLRSSM RSRSLSPLIG SETQPLHPGG QWPAQAELTD
ESTVPLEPQQ RKGAESYVGV RYITEALIKK LTKQDNLALV KSLNLSLSKD GGKKFRYIEN
LEKCVKLEVL NLSYNLIVKI EKVDKLLRLR ELNLSYNKIS KIEGLENMCN LQKLNLAGNE
IEHIPVWFAK KLKSLRVLNL KGNKISSLQD VSKLKPLQDL TSLVLIDNPV VALPHYLQFI
IFHLRSLESL EGQPVTTQDR QEAFERFSLE EIERLEKDLE KKTVETEELK NKQTKFLEEI
KNQDKLNKSL KEEAMLQKQS CEELESDLST KKELLKQKTV ELTRACQKQY ELEQELAFYK
IDAKFEPLNY YPSEYAEIDK YPDESPYIGK SRYKRNMFAT ETYIVSDAQA VQIRKMVPEG
GQLRHEHTPP RVQAPPDLQL EDTEKKISAA QTRLSELHHE IETAEQKVLR ATQEFKQLEE
AIQQKKISEA EKDLLLKQLS GRLQHLNRLR QEALDLEIQM EKQRKEIAEK HEEINTVQLA
TDSLDPKDPK HSHMKAQKRG KEQQLDIMNR QYTQLESRLD EILCRIAKET EEIKDLEQQL
TDGQIAANEA LKKDLEGVIS GLQEYLGTIK GQATQAQNEC RKLQDEKETL LQRLTEVQQE
KEELELIAMD AENMRKELAE LESALQEQHE VNASLQQAQG DLSAYETELE TQLKLKDAET
SQLKQELEKL LRRTQLEQSV LQTELEKERE SLRDALGKAQ SSEEKQQENN ELRTQLKQLQ
DDNSLLKKQL KEFQNHLNHV VDGLIHPEEV AARVDELRKR LKLGAGEMRI HSPSDVLGKS
LADLQKQFSE ILARSQWEKE EAQVRERKLH EEMALQQEKL ANGQEEFRQA CERALEARIK
FDKRQHNARI QQLENEIHYL QENLKSMEKI QGLTDLQLQE ADEEKERILA QLQELEKKKK
REDARSQEQF LGLDEELKSL KKAVAASDKL AAAELTIAKD QLKSLHGTVV RINQERAEEL
QEAERFSREA MQAAKDLSRA EAEIELLQHL LREREGQFRD EMENADLGAK GANSQLLEIE
ALNEAMAKQR AEITRLRDVL NLTGAGTKGG IENVLEEIAE LRHAVSAQNE YISSMADPFR
RQGWWYFMPP APSSKVSSHS SQATKDSGLG LKYTASTPLR KPQPGQQEEK DSSGPLPASG
YWVYSPIRST LHKSFSKRED ADSGGDSQEE SGLDDQEEPP FVPPPGYIMY TVLPDGSPVP
QGVALYAPSP PLPNSSHPLT PGTVVYGPPP AGAPIIYGPP PANFAVPLVP AGVQHCNIPE
HHNLENEVSR LEDIMQHLKS KQREERRQKA STQHSEEEVD GLHRDIDDLL QEKKELELEV
EELHRTIERH QQRKDFIDGH VENLMTELEI EKSLKHHEDI VDEIECLEKT LLKRRSELRE
ADRLLAEAEN ELACTKEKTK SAVEKFTDAK RNLLQTESDA EALEKRAQET ALNLVKAEQQ
LRLLQADAED LEQHKIKQEE ILKEINKVVA AKDADFQCLN EKKEKLTEEL QSLQRDIKAA
QHSEDHHLQV LRESETLLQA KRAELETLKS QVTSQQQELA VLDSELGHRR EELLLLQDSL
AQAKADLQEA LTLGETEVAE KCSHIREVKS LLEELSFQKG ELNVHISEKK TQLALIQQEM
EKEEKNLQVV LQQLSRHKTE LKNVADILQL ETSELQGLKL QHDQKVVELE KAQVDVLEEK
LELENLQQAT QQQRRELERQ RQLLERDRRE TERVRAESQA LQSCVECLSK EKEDLQGQCE
SWEKKSSHAQ RVLAATEESN KMEQSNLGKL ELSVRKLRQE LEQLSQDKLA LHSEVAEVQQ
QLQGKQEAIN SLQEELDSTQ DHLDLAKQDL IHTTKCQNEL LNEQTQLQED ISKWMARLES
CQKETETKEQ QVQQLQDEIR ESKLRLDQQE MMFQKLQKER EREEQKFEAG KVTLEQQQRQ
LEKELTDQKS RLKQLLTDVS AAEGRLGTLQ EEERRIEGLE RMLSQAKQQL SEREQQLMAK
SGELLALQKE ADDMRADFSL LRNQFLTERK KAEKQVAGLK EALKIQRSQL EKNLLEQKQE
NSCMQKEMAT IELVAQDNHE RARRLMKELS QMQQEYLELK KQVANQKDLE RRQMEVSDAM
RTLKSEVKDE IRTSLRNLNQ FLPELPADLA SILERNENLR ELESLKENFP FTTKERIFEE
KSNFPQVHIM DEHWRGEALR QRLRRHEDQL KAQLRHCMSK QAEVLIKGKQ QTEGTLHSLR
RQVDALGELV TSTSTDSASS PSLPSLVEDS QHGHSQSSFQ VLQVPLEEPN SYRH
