FRY_MOUSE
ID FRY_MOUSE Reviewed; 3020 AA.
AC E9Q8I9; Q4VA57; Q5DTL4; Q8BIW6; Q8BUA0; Q8CG91;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein furry homolog;
GN Name=Fry; Synonyms=Kiaa4143;
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 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2397-3020 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Embryonic head;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2014-3020 (ISOFORM 2).
RC TISSUE=Brain;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2176-3020 (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryonic brain, and 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1382; SER-1383; SER-1936;
RP SER-1940; SER-2427; SER-2428; SER-2495 AND SER-2815, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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).
RN [6]
RP FUNCTION, INTERACTION WITH AURKA AND PLK1, PHOSPHORYLATION AT THR-2516 BY
RP CDK1, AND MUTAGENESIS OF THR-2516.
RX PubMed=22753416; DOI=10.1074/jbc.m112.378968;
RA Ikeda M., Chiba S., Ohashi K., Mizuno K.;
RT "Furry protein promotes Aurora A-mediated polo-like kinase 1 activation.";
RL J. Biol. Chem. 287:27670-27681(2012).
CC -!- FUNCTION: Plays a crucial role in the structural integrity of mitotic
CC centrosomes and in the maintenance of spindle bipolarity by promoting
CC PLK1 activity at the spindle poles in early mitosis. May function as a
CC scaffold promoting the interaction between AURKA and PLK1, thereby
CC enhancing AURKA-mediated PLK1 phosphorylation.
CC {ECO:0000269|PubMed:22753416}.
CC -!- SUBUNIT: When phosphorylated by CDK1, interacts with PLK1; this
CC interaction occurs in mitotic cells, but not in interphase cells, and
CC leads to further FRY phosphorylation by PLK1.
CC {ECO:0000269|PubMed:22753416}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250}. Note=Distributed diffusely
CC throughout the cytoplasm in interphase. Localizes to the separating
CC centrosomes in prophase, to the spindle poles and spindle microtubules
CC in prometaphase to metaphase, to spindle microtubules in anaphase and
CC to the distal sections of the midbody in cytokinesis. Colocalizes with
CC PLK1 to separating centrosomes and spindle poles from prophase to
CC metaphase in mitosis, but not in other stages of the cell cycle (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=E9Q8I9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9Q8I9-2; Sequence=VSP_044444, VSP_044445;
CC Name=3;
CC IsoId=E9Q8I9-3; Sequence=VSP_044441, VSP_044442, VSP_044443;
CC -!- PTM: Phosphorylated by AURKA, CDK1 and PLK1.
CC {ECO:0000269|PubMed:22753416}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the furry protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37538.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK079097; BAC37538.1; ALT_INIT; mRNA.
DR EMBL; AK086708; BAC39723.1; -; mRNA.
DR EMBL; AC084217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK220506; BAD90515.1; -; mRNA.
DR EMBL; BC042756; AAH42756.1; -; mRNA.
DR EMBL; BC096532; AAH96532.1; -; mRNA.
DR CCDS; CCDS51708.1; -. [E9Q8I9-1]
DR RefSeq; NP_766475.2; NM_172887.2. [E9Q8I9-1]
DR RefSeq; XP_006504993.1; XM_006504930.3. [E9Q8I9-2]
DR BioGRID; 235965; 5.
DR IntAct; E9Q8I9; 4.
DR MINT; E9Q8I9; -.
DR STRING; 10090.ENSMUSP00000084454; -.
DR iPTMnet; E9Q8I9; -.
DR PhosphoSitePlus; E9Q8I9; -.
DR SwissPalm; E9Q8I9; -.
DR EPD; E9Q8I9; -.
DR jPOST; E9Q8I9; -.
DR MaxQB; E9Q8I9; -.
DR PaxDb; E9Q8I9; -.
DR PeptideAtlas; E9Q8I9; -.
DR PRIDE; E9Q8I9; -.
DR ProteomicsDB; 271637; -. [E9Q8I9-1]
DR ProteomicsDB; 271638; -. [E9Q8I9-2]
DR ProteomicsDB; 271639; -. [E9Q8I9-3]
DR Antibodypedia; 63056; 40 antibodies from 8 providers.
DR Ensembl; ENSMUST00000087204; ENSMUSP00000084454; ENSMUSG00000056602. [E9Q8I9-1]
DR GeneID; 320365; -.
DR KEGG; mmu:320365; -.
DR UCSC; uc009att.1; mouse. [E9Q8I9-3]
DR UCSC; uc009atv.2; mouse. [E9Q8I9-1]
DR CTD; 10129; -.
DR MGI; MGI:2443895; Fry.
DR VEuPathDB; HostDB:ENSMUSG00000056602; -.
DR eggNOG; KOG1825; Eukaryota.
DR GeneTree; ENSGT00610000086058; -.
DR HOGENOM; CLU_000483_0_0_1; -.
DR InParanoid; E9Q8I9; -.
DR OMA; GPTQFCQ; -.
DR OrthoDB; 11874at2759; -.
DR PhylomeDB; E9Q8I9; -.
DR TreeFam; TF313568; -.
DR BioGRID-ORCS; 320365; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Fry; mouse.
DR PRO; PR:E9Q8I9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; E9Q8I9; protein.
DR Bgee; ENSMUSG00000056602; Expressed in ascending aorta and 259 other tissues.
DR ExpressionAtlas; E9Q8I9; baseline and differential.
DR Genevisible; E9Q8I9; MM.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:HGNC.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:1904428; P:negative regulation of tubulin deacetylation; IDA:HGNC.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR025614; Cell_morpho_N.
DR InterPro; IPR025481; Cell_Morphogen_C.
DR InterPro; IPR045842; Fry_C.
DR InterPro; IPR039867; Furry/Tao3/Mor2.
DR InterPro; IPR029473; MOR2-PAG1_mid.
DR PANTHER; PTHR12295; PTHR12295; 1.
DR Pfam; PF19421; Fry_C; 1.
DR Pfam; PF14225; MOR2-PAG1_C; 1.
DR Pfam; PF14228; MOR2-PAG1_mid; 3.
DR Pfam; PF14222; MOR2-PAG1_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..3020
FT /note="Protein furry homolog"
FT /id="PRO_0000420369"
FT REGION 1378..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1529..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1937..2042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2355..2384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2439..2458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2508..2535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1748..1773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1937..1986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2008..2042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2370..2384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 213
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5TBA9"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1940
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2516
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:22753416"
FT MOD_RES 2815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..23
FT /note="MASQQDSGFFEISIKYLLKSWSN -> MEITTACWRRSCVISLIKGL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_044441"
FT VAR_SEQ 808..817
FT /note="ATLPPTHNVD -> VSRRVVPNAI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_044442"
FT VAR_SEQ 818..3020
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_044443"
FT VAR_SEQ 2480
FT /note="E -> EELQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_044444"
FT VAR_SEQ 2831
FT /note="Q -> QMESLAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_044445"
FT MUTAGEN 2516
FT /note="T->A: Loss of phosphorylation by CDK1. Loss of PLK1-
FT binding."
FT /evidence="ECO:0000269|PubMed:22753416"
FT MUTAGEN 2516
FT /note="T->E: Loss of PLK1-binding."
FT /evidence="ECO:0000269|PubMed:22753416"
FT CONFLICT 363
FT /note="P -> Q (in Ref. 1; BAC39723)"
FT /evidence="ECO:0000305"
FT CONFLICT 2366..2368
FT /note="RAM -> TRP (in Ref. 4; AAH42756)"
FT /evidence="ECO:0000305"
FT CONFLICT 2630
FT /note="C -> G (in Ref. 3; BAD90515)"
FT /evidence="ECO:0000305"
FT CONFLICT 2687
FT /note="A -> V (in Ref. 3; BAD90515)"
FT /evidence="ECO:0000305"
FT CONFLICT 2763
FT /note="L -> P (in Ref. 4; AAH96532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3020 AA; 339093 MW; BB72299FB788ED9C CRC64;
MASQQDSGFF EISIKYLLKS WSNASPVGNG YIKPPVPPAS GTHREKGPPA MLPINVDPDS
KPGEYVLKSL FVNFTTQAER KIRIIMAEPL EKPLTKSLQR GEDPQFDQVI SSMSSLSEYC
LPSILRTLFD WYKRQNGIED ESHEYRPRTS NKSKSDEQQR DYLMERRDLA IDFIFSLVLI
EVLKQIPLHP VIDSLIHDII NLAFKHFKYK EGYLGPNTGN MHIVADLYAE VIGVLAQAKF
PAVKKKFMAE LKELRHKEQS PYVVQSIISL IMGMKFFRIK MYPVEDFEAS LQFMQECAHY
FLEVKDKDIK HALAGLFVEI LVPVAAAVKN EVNVPCLRNF VESLYDTTLE LSSRKKHSLA
LYPLVTCLLC VSQKQLFLNR WHVFLNNCLS NLKNKDPKMA RVALESLYRL LWVYMIRIKC
ESNTATQSRL ITITTTLFPK GSRGVVPRDM PLNIFVKIIQ FIAQERLDFA MKEIIFDFLC
VGKPAKAFSL NPERMNIGLR AFLVIADSLQ QKDGEPPMPV TGAVLPSGNT LRVKKTYLSK
TLTEEEAKMI GMSLYYSQVR KAVGNILRHL DKEVGRCMML TNVQMLNKEP EDMITGERKP
KIDLFRTCVA AIPRLLPDGM SKLELIDLLA RLSIHMDDEL RHIAQNSLQG LLVDFSDWRE
DVLFGFTNFL LREVNDMHHT LLDSSLKLLL QLLTQWKLVI QTQGRAYEQA NKIRNSELIP
NGSSHRMQSE RGPHCSVLHA VEGFALVLLC SFQVATRKLS VLILKEIRAL FLALGQPEDD
DRPMIDVMDQ LSSSILESFI HVAVSDSATL PPTHNVDLQW LVEWNAVLVN SHYDVKSPSH
VWIFAQSVKD PWVLCLFSFL RQENLPKHCP TALSYAWPYA FTRLQSVMPL VDPNSPVNAK
KTSTASSGDN YVTLWRNYLI LCFGVAKPSI MSPGHLRAST PEIMATTPDG TVSYDNKAIG
TPSVGVLLKQ LVPLMRLESI EITESLVLGF GRTNSLVFRE LVEELHPLMK EALERRPENK
KRRERRDLLR LQLLRIFELL ADAGVISDST NGALERDTLA LGALFLEYVD LTRMLLEAEN
DKEVEILKDI RAHFSAMVAN LIQCVPVHHR RFLFPQQSLR HHLFILFSQW AGPFSIMFTP
LDRYSDRNHQ ITRYQYCALK AMSAVLCCGP VFDNVGLSPD GYLYKWLDNI LACQDLRVHQ
LGCEVVMLLL ELNPDQINLF NWAIDRCYTG SYQLASGCFK AIATVCGNRN YPFDIVTLLN
LVLFKASDTN REIYEVSMQL MQILEAKLFV HSKKVAEQRP GSILYGTHGP LPPLYSVSLA
LLSCELARMY PELTLPLFSE VSQRFPTTHP NGRQIMLTYL LPWLHNIELV DSRLLLPGSS
PSSPEDEVKD REGEVTASHG LKGNGWGSPE ATSLVLNNLM YMTAKYGDEV PGAEMENAWN
ALANNEKWSN NLRVTLQFLI SLCGVSSDTI LLPYIKKVAT YLCRNNTIQT MEELLFELQQ
TEPVNPIVQH CDNPPFYRFT ASSKASAAAS GTTSSSNTVV AGQDSFPDPE ESKILKESDD
RFSNVIRAHT RLESRYSNSS GGSYDEDKND PISPYTGWLL SITEAKQPQP LPMPCSGGCW
APLVDYLPET ITPRGPLHRC NIAVIFMTEM VVDHSVREDW ALHLPLLLHA VFLGLDHYRP
EVFEHSKKLL LHLLIALSCN SNFHAIASVL LQTREMGEAK TLTMQPAYQP EYLYTGGFDF
LREDQSSPVP DSGLNSSSTS SSISLGGSSG NLPQMTQEVE DVEAATETDE KASKLIEFLT
TRAFGPLWCH EDITPKNQNS KSAEQLSNFL RHVVSVFKDS RSGFHLEQHL SEVALQTALA
SSSRHYAGRS FQIFRALKQP LSAHALSDLL SRLVEVIGEH GDEIQGYVME ALLTLEAAVD
NLSDCLKNSD LFTVLSRSSS PDLSSSSKLT ASRKSTGQLN VNPGTPGSGG GGGGSGNTTT
AERSRHQRSF SVPKKFGVVD RSSDPPRSAT LDRIQACTQQ GLSSKTRSNS SLKESLTDPS
HVSHPTNLLA TIFWVTVALM ESDFEFEYLM ALRLLNRLLA HMPLEKAENR EKLEKLQAQL
KWADFPGLQQ LLLKGFTSLT TTDLTLQLFS LLTSVSKVPM VDSSQAIGFP LNVLCLLPQL
IQHFENPNQF CKDIAERIAQ VCLEEKNPKL SNLAHVMTLY KTHSYTRDCA TWVNVVCRYL
HEAYADITLN MVTYLAELLE KGLPSMQQPL LQVIYSLLSY MDLSVVPVKQ FNMEVLKTIE
KYVQSIHWRE ALNILKLVVS RSASLVLPSY QHSDLSKIEL HRVWTSASKE LPGKTLDFHF
DISETPIIGR RYDELQNSSG RDGKPRAMAV TRSASSTSSG SNSNVLVPVS WKRPQYSQKR
TKEKLVHVLS LCGQEVGLSK NPSVIFSSCG DLDLPEHQTS LVSSEDGPRE QENMDDTNSE
QQFRVFRDFD FLDVELEDGE GESMDNFNWG VRRRSLDSLD KCDMQILEER QLSRSTPSLN
KMSHEDSDES SEEDLTASQI LEHSDLIMNL SPSEEANPME LLTSACDSAP ADPHSFNTRM
ANFEASLPDI NNLQISEGSK AEAVPEEEDT TVHEDDLSSS INELPAAFEC SDSFSLDMTE
AEEKGNRGLD QYTLASFGEG DRGVSPPPSP FFSAILAAFQ PAACDDAEEA WRSHINQLMC
DSDGSCAVYT FHVFSSLFKN IQKRFCFLTC DAASYLGDNL RGIGSKFVSS SQMLTSCSEC
PTLFVDAETL LSCGLLDKLK FSVLELQEYL DTYNNRKEAT LSWLANCKAT FAGGSRDGVI
TCQPGDSEEK QLELCQRLYK LHFQLLLLYQ SYCKLIGQVH EVSSVPELLN MSRELSDLKR
NLKEATAAIA TDPLYIEGAW SEPTFTSTEA AIQSMLECLK NNELGKALRQ IKECRSLWPN
DIFGSSSDDE VQTLLNIYFR HQTLGQTGTY ALVGSNHSLT EICTKLMELN MEIRDMIRRA
QNYRVLTAFL PDSSVSGTSL
