ZN292_MOUSE
ID ZN292_MOUSE Reviewed; 2698 AA.
AC Q9Z2U2; B1B0E1; B1B0E2; Q8BQX3; Q8BS87; Q8CGI6; Q922D3;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Zinc finger protein 292 {ECO:0000312|EMBL:CAM27828.1, ECO:0000312|MGI:MGI:1353423};
DE AltName: Full=Zinc finger protein 15;
DE Short=Zfp-15 {ECO:0000312|EMBL:AAD01625.1};
GN Name=Zfp292 {ECO:0000312|EMBL:AAH08537.1, ECO:0000312|MGI:MGI:1353423};
GN Synonyms=Zfp15 {ECO:0000312|EMBL:AAD01625.1};
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] {ECO:0000312|EMBL:CAM27815.1}
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:AAH36997.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-520 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1296-2698 (ISOFORMS 1/2).
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH36997.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH36997.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAD01625.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 502-2698 (ISOFORMS 1/2), AND TISSUE
RP SPECIFICITY.
RX PubMed=10687855; DOI=10.1016/s0303-7207(99)00200-2;
RA VanderHeyden T.C., Wojtkiewicz P.W., Voss T.C., Mangin T.M., Harrelson Z.,
RA Ahlers K.M., Phelps C.J., Hurley D.L.;
RT "Mouse growth hormone transcription factor Zn-16: unique bipartite
RT structure containing tandemly repeated zinc finger domains not reported in
RT rat Zn-15.";
RL Mol. Cell. Endocrinol. 159:89-98(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAC28892.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1999-2698 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC28892.1};
RC TISSUE=Corpora quadrigemina {ECO:0000312|EMBL:BAC32648.1}, and
RC Embryo {ECO:0000312|EMBL:BAC28892.1};
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1104 AND LYS-2020, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:19468303};
CC IsoId=Q9Z2U2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:19468303};
CC IsoId=Q9Z2U2-2; Sequence=VSP_053207;
CC -!- TISSUE SPECIFICITY: Expressed in postnatal day 1 (P1) pituitary. Also
CC detected in presomatotrophic cell line GHFT1-5.
CC {ECO:0000269|PubMed:10687855}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD01625.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH36997.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC28892.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC32648.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX465850; CAM27828.1; -; Genomic_DNA.
DR EMBL; BX649603; CAM27828.1; JOINED; Genomic_DNA.
DR EMBL; BX465850; CAM27829.1; -; Genomic_DNA.
DR EMBL; BX649603; CAM27829.1; JOINED; Genomic_DNA.
DR EMBL; BX649603; CAM27815.1; -; Genomic_DNA.
DR EMBL; BX465850; CAM27815.1; JOINED; Genomic_DNA.
DR EMBL; BX649603; CAM27816.1; -; Genomic_DNA.
DR EMBL; BX465850; CAM27816.1; JOINED; Genomic_DNA.
DR EMBL; BC008537; AAH08537.1; -; mRNA.
DR EMBL; BC036997; AAH36997.1; ALT_SEQ; mRNA.
DR EMBL; AF017806; AAD01625.1; ALT_INIT; mRNA.
DR EMBL; AK034951; BAC28892.1; ALT_INIT; mRNA.
DR EMBL; AK046236; BAC32648.1; ALT_INIT; mRNA.
DR CCDS; CCDS51138.1; -. [Q9Z2U2-1]
DR RefSeq; NP_038917.2; NM_013889.2. [Q9Z2U2-1]
DR AlphaFoldDB; Q9Z2U2; -.
DR BioGRID; 205950; 17.
DR IntAct; Q9Z2U2; 15.
DR MINT; Q9Z2U2; -.
DR STRING; 10090.ENSMUSP00000037233; -.
DR iPTMnet; Q9Z2U2; -.
DR PhosphoSitePlus; Q9Z2U2; -.
DR EPD; Q9Z2U2; -.
DR jPOST; Q9Z2U2; -.
DR MaxQB; Q9Z2U2; -.
DR PaxDb; Q9Z2U2; -.
DR PeptideAtlas; Q9Z2U2; -.
DR PRIDE; Q9Z2U2; -.
DR ProteomicsDB; 302077; -. [Q9Z2U2-1]
DR ProteomicsDB; 302078; -. [Q9Z2U2-2]
DR Antibodypedia; 31770; 58 antibodies from 17 providers.
DR DNASU; 30046; -.
DR Ensembl; ENSMUST00000047950; ENSMUSP00000037233; ENSMUSG00000039967. [Q9Z2U2-1]
DR Ensembl; ENSMUST00000098163; ENSMUSP00000095766; ENSMUSG00000039967. [Q9Z2U2-2]
DR GeneID; 30046; -.
DR KEGG; mmu:30046; -.
DR UCSC; uc008sgn.2; mouse. [Q9Z2U2-1]
DR UCSC; uc012dbp.1; mouse. [Q9Z2U2-2]
DR CTD; 30046; -.
DR MGI; MGI:1353423; Zfp292.
DR VEuPathDB; HostDB:ENSMUSG00000039967; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00950000183034; -.
DR HOGENOM; CLU_000520_0_0_1; -.
DR InParanoid; Q9Z2U2; -.
DR OMA; LIVFKQC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Z2U2; -.
DR TreeFam; TF350813; -.
DR BioGRID-ORCS; 30046; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Zfp292; mouse.
DR PRO; PR:Q9Z2U2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9Z2U2; protein.
DR Bgee; ENSMUSG00000039967; Expressed in rostral migratory stream and 267 other tissues.
DR Genevisible; Q9Z2U2; MM.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..2698
FT /note="Zinc finger protein 292"
FT /id="PRO_0000392944"
FT ZN_FING 567..589
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 681..705
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 722..744
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 750..774
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 779..803
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 807..831
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1085..1110
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1361..1383
FT /note="C2H2-type 8; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1879..1904
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1924..1949
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2091..2116
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2149..2174
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2193..2218
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2233..2258
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2362..2386
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 822..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1964..1997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2021..2075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2262..2323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2411..2454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2467..2553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2580..2608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1574..1607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1968..1994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2283..2304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2411..2433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2467..2490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2491..2527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2580..2594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60281"
FT MOD_RES 2020
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 178..182
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19468303"
FT /id="VSP_053207"
FT CONFLICT 1224
FT /note="N -> Y (in Ref. 3; AAD01625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1296..1298
FT /note="LKG -> HAS (in Ref. 2; AAH08537)"
FT /evidence="ECO:0000305"
FT CONFLICT 1527
FT /note="V -> L (in Ref. 2; AAH08537)"
FT /evidence="ECO:0000305"
FT CONFLICT 1643
FT /note="A -> S (in Ref. 3; AAD01625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1647
FT /note="P -> T (in Ref. 3; AAD01625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1664
FT /note="R -> Q (in Ref. 2; AAH08537)"
FT /evidence="ECO:0000305"
FT CONFLICT 1690
FT /note="C -> R (in Ref. 2; AAH08537)"
FT /evidence="ECO:0000305"
FT CONFLICT 1787
FT /note="N -> S (in Ref. 3; AAD01625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2128
FT /note="E -> Q (in Ref. 3; AAD01625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2227
FT /note="A -> T (in Ref. 2; AAH08537)"
FT /evidence="ECO:0000305"
FT CONFLICT 2412
FT /note="K -> R (in Ref. 3; AAD01625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2426
FT /note="D -> G (in Ref. 3; AAD01625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2513
FT /note="N -> T (in Ref. 2; AAH08537)"
FT /evidence="ECO:0000305"
FT CONFLICT 2589
FT /note="H -> D (in Ref. 4; BAC32648)"
FT /evidence="ECO:0000305"
FT CONFLICT 2600
FT /note="S -> C (in Ref. 2; AAH08537)"
FT /evidence="ECO:0000305"
FT CONFLICT 2607
FT /note="D -> A (in Ref. 2; AAH08537)"
FT /evidence="ECO:0000305"
FT CONFLICT 2610
FT /note="A -> V (in Ref. 2; AAH08537)"
FT /evidence="ECO:0000305"
FT CONFLICT 2625..2626
FT /note="IF -> TL (in Ref. 2; AAH08537)"
FT /evidence="ECO:0000305"
FT CONFLICT 2646
FT /note="D -> H (in Ref. 2; AAH08537)"
FT /evidence="ECO:0000305"
FT CONFLICT 2678
FT /note="N -> S (in Ref. 3; AAD01625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2698 AA; 301048 MW; E38581486D7ACDB9 CRC64;
MADDEAEQER LSGGGCAAEL RRLGERLQEL ERRLCESREP AVEAAAAYCR QLCQTLLEYA
EKWKTSEDPL PLLEVYTVAI QSYVKARPYL TSECESVALV LERLALSCVE LLLCLPVELS
DKQWEQFQTL VQVAHETLME SGSCELQFLA TLAQETGVWK NAVLSTILSQ EPLDKEKVNE
FLAFEGPILL DMRIKHLIKT NQLSQATALA KLCSDHPEIG TKGSFKQTYL VCLCTSSPSE
KLIEEISEVD CKDALEMICN LESEGDEKSA LVLCTAFLSR QLQQGDMYCA WELTLFWSKL
QQRVEPSVQV YLERCRQLSL LTKTVYHIFF LIKVINSETE GAGLATCIEL CVKALRLEST
ENTEVKISIC KTISCLLPED LEVKRACQLS EFLIEPTVDA YYAVEMLYNQ PDQKYDEENL
PIPNSLRCEL LLVLKTQWPF DPEFWDWKTL KRQCLALMGE EASIVSSIDE LNDSEVYEKV
DYQGERGDTS VNGLSAAGLG TDSGLLMDTG DEKQKKKEIK ELKDRGFISA RFRNWQAYMQ
YCLLCDKEFL GHRIVRHAQK HYKDGIYSCP ICAKNFNSKD SFVPHVTLHV KQSSKERLAA
MKPLRRLGRP PKITATHENQ KTNINTVAKQ EQRPIKKNSL YSTDFIVFND NDGSDDENDD
KDKSYEPEVI PVQKPVPVNE FNCPVTFCKK GFKYFKNLIA HVKGHKDSED AKRFLEMQSK
KVICQYCRRH FVSVTHLNDH LQMHCGSKPY ICIQMKCKAG FNSYAELLAH RKEHQVFRAK
CLFPKCGRIF SQAYLLYDHE AQHYNTYTCK FTGCGKVYRS QSEMEKHQDG HSHPETGLPP
EDQLQPSGND VNPDSGATAA GGRSENSIDK NLGSNRSADW EKNRAEPAVT KHGQISAAEL
RQANIPLSNG LETRDNTTVL RTNEVAVSIK VSVNHGVEGD FGKQENLTME GTGEPLITDV
HKPGIGAGVQ LCHPGFQEKK GHECLNEAQN SLSNSESLKM DDLNPQSLER QVNTLMTFSV
QNEAGLEDNS QICKFECGGD VKTSSSLYDL PLKTLESITF VQSQPDLSSP LGSPSVPPKA
PGQKFSCQVE GCTRTYNSSQ SIGKHMKTAH PDQYAAFKLQ RKTKKGQKSN NLNTPNHGKC
VYFLPSQVSS SNHAFFTPQT KANGNPACSA QVQHVSPSIF PAHLASVSAP LLPSVESVLS
PNIPSQDKHG QDGILCSQME NLSNAPLPAQ MEDLTKTVLP LNIDSGSDPF LPLPTENSSL
FSSPADSENN SVFSQLENST NHYPSQTDGN INSSFLKGGS SENGVFPSQV SSADDFSSTS
AQPSTPKKVK KDRGRGPNGK ERKPKHNKRA KWPAIIRDGK FICSRCYRAF TNPRSLGGHL
SKRSYCKPLD GAEIAQELLQ TNRQPSLLAS MILSTSAVNM QQPQQSNFNP ETCFKDPSFL
QLLNVENRPT FLPSTFPRCD VSNFNASVSQ EGSEIIKQAL ETAGIPSTFE SAEMLSQVVP
IGSVSDAAQV SAAGMPGPPV TPLLQTVCHP NTSPSNQNQT PNSKTLKECN SLPLFTTNDL
LLKTIENGLC SNSFSSSTEP PQNFTNNSAH VSVISGPQNT RSSHLNKKGN SASKKRKKVA
PAVSVSNTSQ NVLPTDLPVG LPAKNLPVPD TNTRSDMTPD CEPRALVENL TQKLNNIDNH
LFITDVKENC KASLEPHTML TPLTLKTENG DSRMMPLSSC TPVNSDLQIS EDNVIQNFEK
TLEIIKTAMN SQILEVKSGS QGTGETTQNA QINYSMQLPS VNSIPDNKLP DASQCSSFLT
VMPTKSEALH KEDQIQDILE GLQNLKLEND TSAPASQSML MNKSVALSPT PTKSTPNIVV
QPVPEVIHVQ LNDRVNKPFV CQNQGCNYSA MTKDALFKHY GKIHQYTPEM ILEIKKNQLK
FAPFKCVVPS CTKTFTRNSN LRAHCQLVHH FTIEEMVKLK IKRPYGRKSQ SENLSSPQNN
QVKKQPSMAE ETKTESQPAF KVPAATGDAA LANATVIPEK QLAEKKSPEK PESSSQPVTS
SAEQYNANLA NLKTKGRKNK RHRKEKEEKR EKNPVSQAFE LPTKYSSYRP YCCVHQGCFA
AFTIQQNLIL HYQAVHKSNL PTFSAEVEEE SEAVKESEET EPKQSMKEFR CQVSDCSRIF
QAITGLIQHY MKLHEMTPEE IESMTAAVDV GKFPCDQLEC KLSFTTYLSY VVHLEVDHGI
GTRTSKAEED GIYKCDCEGC DRIYATRSNL LRHIFNKHND KHKAHLIRPR KLTGQENISS
KANQEKSKSK HRTTKPNRSG KDGMKMPKTK RKKKSNLENK SAKVVQIEEN KPYSLKRGKH
VYSIKARNDA LAECTSKFVT QYPCMIKGCT SVVTSESNII RHYKCHKLSR AFTSQHRNIL
IVFKRYGNPQ GKEISEQEDE KNDKKDPDSS VLEKNDNSEP AAAPQEEGRK GEKDEMDELT
ELFITKLINE DSTNAENQGN TTLKGNNEFQ EHDSCTSERQ KPGNLKRVYK EKNTVQSKKR
KIDKTEPEVS LVVNNTRKEE EPAVAVQTTE EHPASFDWSS FKPMGFEASF LKFLEESAVK
QKKNSDRDHS NSGSKRGSHS SSRRHVDKAA VAGSSHVCSC KDSEIFVQFA NPSKLQCSEN
VKIVLDKTLK DRSELVLKQL QEMKPTVSLK KLEVLSNNPD RTVLKEISIG KATGRGQY
