ALMS1_MOUSE
ID ALMS1_MOUSE Reviewed; 3251 AA.
AC Q8K4E0; E9QKT8; Q6A084; Q8C9N9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Centrosome-associated protein ALMS1 {ECO:0000305};
DE AltName: Full=Alstrom syndrome protein 1 homolog;
GN Name=Alms1; Synonyms=Kiaa0328;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11941369; DOI=10.1038/ng867;
RA Collin G.B., Marshall J.D., Ikeda A., So W.V., Russell-Eggitt I.,
RA Maffei P., Beck S., Boerkoel C., Sicolo N., Martin M., Nishina P.M.,
RA Naggert J.K.;
RT "Mutations in ALMS1 cause obesity, type 2 diabetes and neurosensory
RT degeneration in Alstrom syndrome.";
RL Nat. Genet. 31:74-78(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(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 2941-3251 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [5]
RP POSSIBLE FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16000322; DOI=10.1093/hmg/ddi235;
RA Collin G.B., Cyr E., Bronson R., Marshall J.D., Gifford E.J., Hicks W.,
RA Murray S.A., Zheng Q.Y., Smith R.S., Nishina P.M., Naggert J.K.;
RT "Alms1-disrupted mice recapitulate human Alstrom syndrome.";
RL Hum. Mol. Genet. 14:2323-2333(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1916, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 PCM1-dependent intracellular transport. Required,
CC directly or indirectly, for the localization of NCAPD2 to the proximal
CC ends of centrioles. Required for proper formation and/or maintenance of
CC primary cilia (PC), microtubule-based structures that protrude from the
CC surface of epithelial cells (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8K4E0; Q7TPR4: Actn1; NbExp=4; IntAct=EBI-6272972, EBI-774010;
CC Q8K4E0; P57780: Actn4; NbExp=4; IntAct=EBI-6272972, EBI-445071;
CC Q8K4E0; Q9D753: Exosc8; NbExp=3; IntAct=EBI-6272972, EBI-8387079;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle pole {ECO:0000250}. Note=Associated with centrosomes and basal
CC bodies at the base of primary cilia. Specifically locates to the
CC proximal ends of centrioles and basal bodies. Colocalizes partially
CC with NCAPD2 at these sites. During mitosis localizes to both spindle
CC poles (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K4E0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K4E0-2; Sequence=VSP_017350;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11941369}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 7.5 dpc. At 8.0 dpc expression is
CC found in mesodermal- and ectodermal-derived layers. At 10.5 dpc mainly
CC detected in midbrain, hindbrain, forelimb and hindlimb. Also expressed
CC at 15.5 dpc and 18.5 dpc. {ECO:0000269|PubMed:16000322}.
CC -!- DISRUPTION PHENOTYPE: Mice display obesity, hypogonadism,
CC hyperinsulinemia, retinal dysfunction and hearing loss.
CC {ECO:0000269|PubMed:16000322}.
CC -!- SIMILARITY: Belongs to the ALMS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32212.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF425257; AAM62320.1; -; mRNA.
DR EMBL; AK172934; BAD32212.1; ALT_INIT; mRNA.
DR EMBL; AC104743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK041679; BAC31030.1; -; mRNA.
DR CCDS; CCDS20298.1; -. [Q8K4E0-1]
DR RefSeq; NP_660258.2; NM_145223.2. [Q8K4E0-1]
DR BioGRID; 231749; 6.
DR CORUM; Q8K4E0; -.
DR IntAct; Q8K4E0; 11.
DR MINT; Q8K4E0; -.
DR STRING; 10090.ENSMUSP00000071904; -.
DR iPTMnet; Q8K4E0; -.
DR PhosphoSitePlus; Q8K4E0; -.
DR jPOST; Q8K4E0; -.
DR MaxQB; Q8K4E0; -.
DR PaxDb; Q8K4E0; -.
DR PeptideAtlas; Q8K4E0; -.
DR PRIDE; Q8K4E0; -.
DR ProteomicsDB; 296174; -. [Q8K4E0-1]
DR ProteomicsDB; 296175; -. [Q8K4E0-2]
DR Antibodypedia; 8144; 130 antibodies from 26 providers.
DR DNASU; 236266; -.
DR Ensembl; ENSMUST00000072018; ENSMUSP00000071904; ENSMUSG00000063810. [Q8K4E0-1]
DR GeneID; 236266; -.
DR KEGG; mmu:236266; -.
DR UCSC; uc009cpz.1; mouse. [Q8K4E0-1]
DR UCSC; uc009cqe.1; mouse. [Q8K4E0-2]
DR CTD; 7840; -.
DR MGI; MGI:1934606; Alms1.
DR VEuPathDB; HostDB:ENSMUSG00000063810; -.
DR eggNOG; KOG4613; Eukaryota.
DR GeneTree; ENSGT00940000153123; -.
DR HOGENOM; CLU_000177_0_0_1; -.
DR InParanoid; Q8K4E0; -.
DR OrthoDB; 9342at2759; -.
DR TreeFam; TF335596; -.
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; 236266; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Alms1; mouse.
DR PRO; PR:Q8K4E0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8K4E0; protein.
DR Bgee; ENSMUSG00000063810; Expressed in spermatid and 80 other tissues.
DR ExpressionAtlas; Q8K4E0; baseline and differential.
DR Genevisible; Q8K4E0; MM.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0051393; F:alpha-actinin binding; IPI:MGI.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:MGI.
DR GO; GO:0001678; P:cellular glucose homeostasis; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0016197; P:endosomal transport; ISO:MGI.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0030728; P:ovulation; IMP:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0046599; P:regulation of centriole replication; IBA:GO_Central.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0046548; P:retinal rod cell development; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR InterPro; IPR028781; ALMS1.
DR InterPro; IPR029299; ALMS_motif.
DR InterPro; IPR040972; ALMS_repeat.
DR PANTHER; PTHR21553:SF22; PTHR21553:SF22; 10.
DR Pfam; PF15309; ALMS_motif; 1.
DR Pfam; PF18727; ALMS_repeat; 11.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..3251
FT /note="Centrosome-associated protein ALMS1"
FT /id="PRO_0000225593"
FT REPEAT 440..485
FT /note="1"
FT REPEAT 486..534
FT /note="2"
FT REPEAT 540..587
FT /note="3"
FT REPEAT 588..638
FT /note="4"
FT REPEAT 639..684
FT /note="5"
FT REPEAT 685..731
FT /note="6"
FT REPEAT 732..777
FT /note="7"
FT REPEAT 778..824
FT /note="8"
FT REPEAT 825..871
FT /note="9"
FT REPEAT 872..917
FT /note="10"
FT REPEAT 918..959
FT /note="11"
FT REPEAT 960..1005
FT /note="12"
FT REPEAT 1006..1048
FT /note="13"
FT REPEAT 1115..1163
FT /note="14"
FT REPEAT 1164..1208
FT /note="15"
FT REPEAT 1269..1314
FT /note="16"
FT REPEAT 1315..1362
FT /note="17"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..1362
FT /note="17 X 47 AA approximate tandem repeat"
FT REGION 615..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2421..2452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2464..2485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2659..2685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2738..2804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2822..2871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3002..3027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3129..3251
FT /note="ALMS motif"
FT COMPBIAS 1..28
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2421..2435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2659..2683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2743..2764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2787..2804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2822..2858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3010..3027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCU4"
FT MOD_RES 1305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCU4"
FT MOD_RES 1623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCU4"
FT MOD_RES 1788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCU4"
FT MOD_RES 1916
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1958
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCU4"
FT VAR_SEQ 1..2947
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_017350"
FT CONFLICT 26
FT /note="E -> Y (in Ref. 1; AAM62320)"
FT /evidence="ECO:0000305"
FT CONFLICT 2708..2710
FT /note="NPS -> SPC (in Ref. 1; AAM62320)"
FT /evidence="ECO:0000305"
FT CONFLICT 3017
FT /note="D -> G (in Ref. 2; BAD32212)"
FT /evidence="ECO:0000305"
FT CONFLICT 3060
FT /note="S -> N (in Ref. 2; BAD32212)"
FT /evidence="ECO:0000305"
FT CONFLICT 3077
FT /note="V -> G (in Ref. 2; BAD32212)"
FT /evidence="ECO:0000305"
FT CONFLICT 3229
FT /note="W -> R (in Ref. 2; BAD32212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3251 AA; 360215 MW; 560D2B0650DDD0FB CRC64;
MEPEDLPWPD ELEEEEEEEE EEGEEEEGKK EVENASAAAT EEALTSEESG RLEEFEEAGP
DLDFNYESQR QESSDEEEDE LAKAWLQAHP DRPGSAFSLP PPTPPPPPPP LSPRLRYTPV
EHLGKTEVVP LTCRVWQQSS YQDNSRAQFS NSSTMLLETG VRWGSEEDQR TESWHCLPQE
RDSSQTLAMS QTEIGRVEGT EVPDLPSQEG GLPAQSQCPG KKPKLNVLCS PLLVIQDNFA
APDLPLLTCL IQDQEEVEPD SLFQQSELEF APLRGIPDKS EDSEWLARPS EVSEALIQAT
SETSSDLANS CFSISQHPLT EGLQGKAESG VLTRCGDAKY SSLYENLGAQ SERIAVLQRE
VGCSNLGISQ ASPSSLPSFV PQEPTSEPEY HSSNLRMLRV SPDTLLTTHT HSAGSADQKI
GAAVVSSAYS QEIKPGSFHQ EELPDRHLNE EIRKVSPALR TAGQKPEMLP VQSSSYSKGM
KSIFYQHPVS HGHQGKEPLS VSAVCGSAGN KAFHQLSTLS DSLLTEETWP VSVIPGLGNQ
KTPLPSEFSL SYSHRGKNLP EDVVKVSTDS GSAHKKADIL TASSRTYQHK MKPANIYHQE
LPDSRVPIGT RKVAFESGPA GQKSGVSHPY GEMPSVFYQQ GLPDRHSAKS PTKTFIPGPA
DQKTDLSPVP PTSSSHAEKP VSPYQLTLPG SHLPEDVFKA SSVCKSSDEL SGITALTSAS
YSYKGRPNSS YQQKFPDSHL NEEAQKILGT TGTVDQKTVT PTMSSSFLQK EKPSIFYQQT
LPDGGLSEED LQVSAVPWPA DQNIAIPTVT SAAFSQREKP RIFYQQTLSV DRLPGEPLNV
LGTSGPPDQN TGAPTVTPSS YFPGEESIIF YQAGFPGNTL SAMSFKVPRI SGSTEQTNVT
TGSSSSYSVG EKSIIFYHQA LPDGRLPQEA SPAPADLNTG EPPMYLASCS VGVKPIIFYQ
QPMSDSQRTK GHKESDVPGP TDQKTGIATV HSTSQSYIGR RTVSYQKEFP DLSEKALKVL
GDVGSTEQKT QIPVVSSALL HKEGPSAYQE DLPDLTEEPL QILGVSEEVS SSSYQRKLPD
HIEVFLKSVG SGSADRKTGA QIVSSSREKS SGFHQQELPN TGGDAVDAFH PEPVVQEVRK
VQTPGAPAGP SSSHFHKEKL SDYQKASPHR DLTESSLKAS TVPGLSDQKK KPAVSSGFCL
HKEKHEISAS ALLNCQTAEL LTVTQRSCLH REDPAISTVI KPDDQKIPLP TTFHGSSDQK
VKPVIFVQKQ LRDRDQSEDI PKISTVSEPT VVNTVLPVLL PGSYSHREKS DSFYPQELPD
GHLTEVDLKV SSGLGQADQI SGLPTGIPGT YSHSEKHQLI SEHVQELMDN LNSSESSCLS
VDSMPLNSQI DDGVIICKPE SLGFANAGCE EMQNIDRGSK TLKEIQTLLM EAENMALKRC
NFSVPLVPFR DVNDVSFIRS KKVVCFKESS TTDVCTQRES FVEEVPHIEY VQKDIGTQTN
LKYQRGVGNW EFISSATFRS PLQEAEGTAR MAYDETFRQY KAARSVMRSE PEGCSTGIGN
KMIIPMMTII KSDSSSDVSD GCCSWDNNLP ESLESVSDVF LNFFPYTSPK TSITDSREEE
WLSESEDGYG STDSLAAHVK YLLQCETSLN QAKQILKNAE EEEYRVRTQA WNLKFNLGRD
RGYSISELNE DDRRKVEEIK AKLFGHGRAT HMSEGLRSPQ GIGCLPEAVC SRIIIESHEK
GCFRTLTAEQ PRPDSCHCAF RSVEPSDLIR GHRSPSSWRG RHINLSRSIE QSNPCFKVGS
SFQLQSHPPF QKLLPDDIKI SKGVGMPVHA YMDPQPSELV EPTCVPAKEM DFPSSSQILP
PEPKKQFTTA ITFSSHEHSE CISDSSGCKV GVTADSQCSG PSLGVFKPHI PEEQISPRDL
KQKTSFQSSL ERHGSTPVTI LADGSRQRQK LPVDFEHSHQ KEKLLQRLGF KVSHSEPNVS
TNVSNFKGVQ FSGKDTIVSQ DKLTSTVEVK EKNVTVTPDL PSCIFLEQPE LFEESHTPHT
DLQMRKYPSP SCPEIASRIF LEQPKLSEQS KAPHVDREIR EDHSFFPKCQ DYIVADPSPD
FPDQQQCKPP DVVGHTRKQN SLLSEGQDYE LEEVQHIPQS YFSNMVNVEA KVSDAISQSA
PDHCTAASTP PSNRKALSCV RITLCPKTSS KLDSGTLGER FHSLDPASKT RINSEFNSDL
RIISSRSLEP TSKLLTCKPV AQDQESLVFL GPKSPLDLQV AQSSLPDSKT IFQDLKTKPP
QNSQIVTSRQ TQVNISHLEG YSKPEGTPVS ADGSQEQSKV SFTTSFGKLS SDAITQITTE
SPEKTTFSSE IFIHADDRGQ GILDPMAQKP SRFASSSSVQ QIPASHGKDA QPVLLPYKPS
GSSKMYYVPL LKRVPSYLDS KSDTTVESSH SGSNDAIAPD FPPQMLGTRD DDLSNTVNIK
HKEGIYSKRA ATKGKNPSQK GDAAAPVQMP ITWDENVLDE NQEEVISRGV VIKMAGPEEM
SSLEKDLAGP SDITVQDRKT ENLPDTKSIK QKEGSLEIES ECHSAFENTA HSVFRSAKFY
FHHPVHLPHE QDFCHESLGR SVFMQHSWKD FFHHHSGHSC LPPPGPSSDK LDKTKMDYTR
IKSLSINLNL GEHEKIHTIK NQARDPKGKR QANEQKKDQK VTPELTTECP VSLNELWNRY
QERQKQQNPS GACDTKELSL VERLDRLAKL LQNPITHSLR ASESAQDDSR GGHRAREWTG
RRQQKQKGKQ HRKWSKSLER GQSTGDFRKS KVFSPHQGGK SSQFKIEQIK LDKYILRKEP
GFNNVSNTSL DSRPSEESVS LTDSPNIFSS TDSPVDSDVL TPTDRDMPLN ERSSSISTID
TVRLIQAFGQ DRLSLSPRRI KLYSTVTSQR RRYLEQPCKH NRKALNTACP QMTSEHSRRR
HIQVANHMTS SDSVSSPGSL LSLDSALSNE ETVRMVSKGV QAGNLEIVAG VKKYTQDVGV
TFPTPSSSEA RLEEDSDVTS SSEEKAKEKK FLSNYLQTKN LRKNKPNPCA GVSWFVPVES
GQSGSKKENL PKIYRPVISW FEPVTKTKPW REPLREQNWQ AQCMNSRGSL GGPGRDSGQV
SLRPFVRATL QESLQLHRPD FISHSGERIK RLKLLVQERK LQSLFQSERE ALFHSARPLP
RRVLLAVQKN KPIGKKEMIQ RTRRIYEQLP EVKKKREEEK RKSEYKSYWL RAQHYKMKVT
NHLLGRKVPW D
