SPG17_MOUSE
ID SPG17_MOUSE Reviewed; 2320 AA.
AC Q5S003; G3UYF7; Q3UWG8; Q6Q758; Q8CDR5; Q9CUE5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Sperm-associated antigen 17;
DE AltName: Full=Projection protein PF6 homolog;
GN Name=Spag17;
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], FUNCTION, INTERACTION WITH SPAG6, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15827353; DOI=10.1074/mcp.m400177-mcp200;
RA Zhang Z., Jones B.H., Tang W., Moss S.B., Wei Z., Ho C., Pollack M.,
RA Horowitz E., Bennett J., Baker M.E., Strauss J.F. III;
RT "Dissecting the axoneme interactome: the mammalian orthologue of
RT Chlamydomonas PF6 interacts with sperm-associated antigen 6, the mammalian
RT orthologue of Chlamydomonas PF16.";
RL Mol. Cell. Proteomics 4:914-923(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-939 AND 1808-2320.
RC STRAIN=C57BL/6J; TISSUE=Lung, and Testis;
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 [4]
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 [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=23418344; DOI=10.1165/rcmb.2012-0362oc;
RA Teves M.E., Zhang Z., Costanzo R.M., Henderson S.C., Corwin F.D., Zweit J.,
RA Sundaresan G., Subler M., Salloum F.N., Rubin B.K., Strauss J.F. III;
RT "Sperm-associated antigen-17 gene is essential for motile cilia function
RT and neonatal survival.";
RL Am. J. Respir. Cell Mol. Biol. 48:765-772(2013).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=26017218; DOI=10.1371/journal.pone.0125936;
RA Teves M.E., Sundaresan G., Cohen D.J., Hyzy S.L., Kajan I., Maczis M.,
RA Zhang Z., Costanzo R.M., Zweit J., Schwartz Z., Boyan B.D.,
RA Strauss J.F. III;
RT "Spag17 deficiency results in skeletal malformations and bone
RT abnormalities.";
RL PLoS ONE 10:E0125936-E0125936(2015).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29690537; DOI=10.3390/ijms19041252;
RA Kazarian E., Son H., Sapao P., Li W., Zhang Z., Strauss J.F., Teves M.E.;
RT "SPAG17 Is Required for Male Germ Cell Differentiation and Fertility.";
RL Int. J. Mol. Sci. 19:0-0(2018).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DISEASE, VARIANT PCDO 1746-LYS--HIS-2320 DEL,
RP AND CHARACTERIZATION OF VARIANT PCDO 1746-LYS--HIS-2320 DEL.
RX PubMed=32988999; DOI=10.1242/dmm.045344;
RA Abdelhamed Z., Lukacs M., Cindric S., Ali S., Omran H., Stottmann R.W.;
RT "A novel hypomorphic allele of Spag17 causes primary ciliary dyskinesia
RT phenotypes in mice.";
RL Dis. Model. Mech. 13:0-0(2020).
CC -!- FUNCTION: Component of the central pair apparatus of ciliary axonemes.
CC Plays a critical role in the function and structure of motile cilia
CC (PubMed:23418344, PubMed:15827353). May play a role in endochondral
CC bone formation, most likely because of a function in primary cilia of
CC chondrocytes and osteoblasts (PubMed:26017218). Essential for normal
CC spermatogenesis and male fertility (PubMed:29690537). Required for
CC normal manchette structure, transport of proteins along the manchette
CC microtubules and formation of the sperm head and flagellum
CC (PubMed:29690537). Essential for sperm flagellum development and proper
CC assembly of the respiratory motile cilia central pair apparatus, but
CC not the brain ependymal cilia (PubMed:32988999).
CC {ECO:0000269|PubMed:15827353, ECO:0000269|PubMed:23418344,
CC ECO:0000269|PubMed:26017218, ECO:0000269|PubMed:29690537,
CC ECO:0000269|PubMed:32988999}.
CC -!- SUBUNIT: Interacts (via the C-terminus) with SPAG6; the interaction
CC probably occurs on polymerized microtubules.
CC {ECO:0000269|PubMed:15827353}.
CC -!- INTERACTION:
CC Q5S003; Q9JLI7: Spag6; NbExp=3; IntAct=EBI-1783665, EBI-1783654;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15827353,
CC ECO:0000269|PubMed:29690537}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000269|PubMed:15827353}. Cytoplasmic vesicle, secretory
CC vesicle, acrosome {ECO:0000269|PubMed:29690537}. Golgi apparatus
CC {ECO:0000269|PubMed:29690537}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:29690537}. Note=Detected in the cytoplasm of round
CC spermatids and in condensing spermatids. Localized to the central pair
CC of the sperm flagellar axoneme. Colocalizes with SPAG6 on microtubules.
CC Localizes to the manchette in elongating spermatids (PubMed:29690537).
CC {ECO:0000269|PubMed:29690537}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, round spermatids,
CC testicular sperm, epididymal sperm and in condensing spermatids (at
CC protein level) (PubMed:15827353, PubMed:29690537, PubMed:32988999).
CC Expressed in organs that contain cilia-bearing cells including brain,
CC oviduct, lung, and uterus (PubMed:15827353, PubMed:32988999). Expressed
CC in articular cartilage and bone (PubMed:26017218).
CC {ECO:0000269|PubMed:15827353, ECO:0000269|PubMed:26017218,
CC ECO:0000269|PubMed:29690537, ECO:0000269|PubMed:32988999}.
CC -!- DEVELOPMENTAL STAGE: Expressed from day 16 when pachytene spermatocytes
CC are present. {ECO:0000269|PubMed:15827353}.
CC -!- DISEASE: Note=Defects in Spag17 are the cause of primary ciliary
CC dyskinesia only (Pcdo) phenotype. Mice are generally viable to
CC adulthood but have a significantly shortened lifespan, with chronic
CC morbidity. Show neonatal progressive hydrocephalus, accumulation of
CC mucus in the respiratory passages and male infertility.
CC {ECO:0000269|PubMed:32988999}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice die within 12 hours of birth with
CC severe defects in motile cilia (PubMed:23418344). Mice also have
CC skeletal malformations (PubMed:26017218). Male mice are infertile
CC because of a severe defect in spermatogenesis (PubMed:29690537).
CC Spermatids display abnormally long manchette structures and defects in
CC the morphology of the sperm head, acrosome, and tail (PubMed:29690537).
CC Additionally, the transport of proteins along the manchette
CC microtubules is disrupted in the elongating spermatids
CC (PubMed:29690537). {ECO:0000269|PubMed:23418344,
CC ECO:0000269|PubMed:26017218, ECO:0000269|PubMed:29690537}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS66754.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAV66533.1; Type=Miscellaneous discrepancy; Note=Missing sequence in a highly repetitive region between exons 21 and 22.; Evidence={ECO:0000305};
CC Sequence=BAC26566.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE22947.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY555275; AAS66754.1; ALT_FRAME; mRNA.
DR EMBL; AY792594; AAV66533.1; ALT_SEQ; mRNA.
DR EMBL; AC102209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK016477; BAB30259.1; -; mRNA.
DR EMBL; AK029691; BAC26566.1; ALT_FRAME; mRNA.
DR EMBL; AK136364; BAE22947.1; ALT_INIT; mRNA.
DR CCDS; CCDS57248.1; -.
DR RefSeq; NP_083168.3; NM_028892.4.
DR AlphaFoldDB; Q5S003; -.
DR SMR; Q5S003; -.
DR BioGRID; 216691; 5.
DR IntAct; Q5S003; 2.
DR MINT; Q5S003; -.
DR STRING; 10090.ENSMUSP00000134066; -.
DR iPTMnet; Q5S003; -.
DR PhosphoSitePlus; Q5S003; -.
DR MaxQB; Q5S003; -.
DR PaxDb; Q5S003; -.
DR PRIDE; Q5S003; -.
DR ProteomicsDB; 258720; -.
DR Antibodypedia; 33897; 36 antibodies from 8 providers.
DR Ensembl; ENSMUST00000164539; ENSMUSP00000134066; ENSMUSG00000027867.
DR GeneID; 74362; -.
DR KEGG; mmu:74362; -.
DR UCSC; uc012cus.1; mouse.
DR CTD; 200162; -.
DR MGI; MGI:1921612; Spag17.
DR VEuPathDB; HostDB:ENSMUSG00000027867; -.
DR eggNOG; ENOG502QSCB; Eukaryota.
DR GeneTree; ENSGT00390000013693; -.
DR HOGENOM; CLU_001433_0_0_1; -.
DR InParanoid; Q5S003; -.
DR OMA; WDIMVRQ; -.
DR OrthoDB; 32420at2759; -.
DR PhylomeDB; Q5S003; -.
DR TreeFam; TF328540; -.
DR BioGRID-ORCS; 74362; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Spag17; mouse.
DR PRO; PR:Q5S003; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q5S003; protein.
DR Bgee; ENSMUSG00000027867; Expressed in interventricular septum and 26 other tissues.
DR Genevisible; Q5S003; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:1990716; C:axonemal central apparatus; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0002177; C:manchette; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:1904158; P:axonemal central apparatus assembly; IMP:MGI.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:1990953; P:intramanchette transport; IMP:UniProtKB.
DR GO; GO:1905198; P:manchette assembly; IMP:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR026173; SPAG17.
DR PANTHER; PTHR21963; PTHR21963; 1.
PE 1: Evidence at protein level;
KW Cell projection; Ciliopathy; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Differentiation;
KW Flagellum; Golgi apparatus; Microtubule; Primary ciliary dyskinesia;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..2320
FT /note="Sperm-associated antigen 17"
FT /id="PRO_0000331446"
FT REGION 139..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1983..2028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2080..2101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 865..965
FT /evidence="ECO:0000255"
FT COMPBIAS 139..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1983..1999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2013..2028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 1746..2320
FT /note="Missing (in pcdo)"
FT /evidence="ECO:0000269|PubMed:32988999"
FT CONFLICT 193
FT /note="K -> N (in Ref. 3; BAC26566)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="T -> S (in Ref. 3; BAC26566)"
FT CONFLICT 788
FT /note="Y -> C (in Ref. 1; AAV66533/AAS66754 and 3;
FT BAC26566)"
FT /evidence="ECO:0000305"
FT CONFLICT 1629
FT /note="D -> N (in Ref. 1; AAV66533)"
FT /evidence="ECO:0000305"
FT CONFLICT 2029
FT /note="T -> P (in Ref. 3; BAE22947)"
FT /evidence="ECO:0000305"
FT CONFLICT 2082
FT /note="E -> G (in Ref. 3; BAE22947)"
FT /evidence="ECO:0000305"
FT CONFLICT 2212
FT /note="P -> S (in Ref. 1; AAV66533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2320 AA; 263102 MW; 2AC5D4505F7514B5 CRC64;
MAPKKEKPTG SANYKIWEPS LIAAHLNQND WKASIAFVVG NRVEDDLLIH ALDLAVRLPQ
RKLFSIVSWE DILQQMDEIQ SLAESASAKK GKKPTSVNLP LHYEVFLAAK IIMESGEKLT
LPLIGKLLKC QLLHIKSKDQ QRRENEKKMV EERTKSEKDK GKGKSPKEKK VASAKPGKGK
SKDQPEATVT VRKTTQLKRR GEDDEAKSYI DDEPDDGAQY YIIVVGFNNP QLLAIMTELG
IPITSVIKIS SENYEPLQTH LAAVRQQQEA VLQPEDIEAE KLKRKNSIKE LEVFWKYLEP
ILNNEKLEIH LFDVARLQYM VKATYFPSDW SDNEQMLALG TEIFENIACL MYDSLDWKRQ
HHHYLQSMQL INVPQVVSEK TVLEAITIPE PPPSTAPAPT GKKKAQYEES HAPPTVAFII
TTEVDMRYYN DLLNPIPEEF ISVSLILHCM VEQVVATEED LIPPSLVEPA PRADGLDYRI
AAHIVSILPS LCLSEKEKKN LREIFLTEGE SESKALPKGP LLLNYHDAHA HKKYALKDQK
NFDPVQVEQE MQSKLPLWEF LQFPLPPPWN STKRLATIHE LMHFCTNEVL SWNEVERAFK
VFTFESLKLS EVDEEGRLKP TETTSDTDVE NFNIPWDNPA RFAKLIRQRY IHRMSMQKAP
PVVVEIENTE RTLFVNKNFA KAEQDAQGDE NSPNSDEPDA ISVTGSTSNS TKPWNSSNRQ
FSEKETSGSM WPQPESMDQT MDTEIKDDAA TKDDSPEKKP KKMVVEADIE DIKKTQQRSL
MDWSFTEYFQ PKVLLQVLQE AHQQYRCVDS YYHTQDNSLL LVFHNPMNLQ RLQCEHWNIA
LHSNVGFRNY LELVAKSIED WVTQEEAKYQ EAKMAEELNR IRIELELKAT VKTSASKIPG
PKRSKTNKVS SKTELSDQEK DKEKEKDKIP FVLEGSLKAW KEEQERLAEE ERLKEEKKAE
KKGKDTGKKK GKDKADKDDA KALKKKSSSK EKPKEEPAKT LEVIEETAPL PVPEVVYPFR
GYNMGDIPIQ ISGTNYYLYP SDGGQIEVEK TRFERGSTFI KVKVKKDKHN FIIHLKDPKE
IVKKEKEEKN SEEEEEEEEE KEEVEEKKPK EGEEEKVKQK VEMKRAQIEK EAVSKFGSFS
ATLENGICLS ISYYGSNGMA PEVINSELEA MMNIPSAMTA TVVPAVVTVP QGKGKAKPKG
KEKHKDSIKE EELPKEEEKK NHIQEEVEPE IVIQESPPYV PTFQNLNVSC PSGLLLTFIG
QESTDYSIVD EEPTRNLMIR QSYPQRLKHY EFYKAVMPPL EQEASRVVTS QGTVIKYMLD
GSTQILFADG AVSSSPDSGP VYTSPELPTS PHNGDLVDSA SQPKSETGPE IIITKKGKGH
KNQTVANKSE THDIIPEVPP PTPVESHIGT WFTTTPDGRR IGTKGLEKIE DLKPYLFFQA
TDPINGTVMT TREDKVIIVE KKDGTRVVDH ADGTRITTFY QVYEDHITPS NDEETTEGPR
TVTRQVKCMR IESSHYATII TNCEDSSCCA TFGDGTSIIA KPQGSYQVLP PNTGCLYIDK
DCSATYCHES SNNLYHPFQK REQLRASRYI MKHTSEVICE VQDPEGNTFQ VMADGSVSTT
LPKKKLEDDF NVQMEGYESL SSLHLEKNHM QIYGEHVPRF FVVYTDGSGV ELLRDSDIEE
YLSLAYGEST TVVLQEPVQE YPGALSITVL RPFHEASQWI MKKELDTIVP PNLQSRSWER
FPSVEKKTPG PPFGTQIWKG LSIGSKQLTN IPAPILEGPK VLQMRQFIQH EVIKNEVKLK
LQISLKDYIN HILKKEDELQ EMTVKDSRTE EERGNAADLL KLVMSFPKME ETTKSHMTKV
AAHLTVLFKQ SMASAPKCSP DSYSKEFLEK KWRSLSQGTS WKEKLEQQRN NIKKTQSYLM
QIKTKEVTPY FKSELSSLFK SKYDYLEKFS KSLPPFVKKN EAKLMTAVPD LYSDSTLTVD
TEKEASNTHP LLNQEVAENI QESPREKETE YVNKSLQTSS SQNQYENVTI SPKESVYQSQ
TEIETKDTKE SAIQNFTEKF KKYTKKSASQ NEIEDLIKST KESVSQRQTE NVTRPPTEEP
DIYMPIKIPT QSLLQDVTGQ ARKEKVRLPY YMMSSKPKSQ PYAKVEDPVG GRVNTSSIAS
AAMYNPNASP FGFHLLPPSV KFGVLKEGHT YATIVKLKNV GVDFCRFRVK QPPPSTGLKV
TYKPGPVAAG LQAELKVELF AMAVGEDGAK GSAHISHNIE IMTEHDVLFL PVEATVLTSS
NYDNRPKNLP QGKENPMVFR TSTISSSSLG VVMSQKATHH
