ZZEF1_MOUSE
ID ZZEF1_MOUSE Reviewed; 2924 AA.
AC Q5SSH7; Q499C8; Q6ZQC5; Q8C710; Q8CI54;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Zinc finger ZZ-type and EF-hand domain-containing protein 1;
GN Name=Zzef1; Synonyms=Kiaa0399;
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).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
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 2202-2924 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver, and Pancreas;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2642-2924 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1538, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1488; SER-1515; THR-1519 AND
RP SER-2407, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Histone H3 reader which may act as a transcriptional
CC coactivator for KLF6 and KLF9 transcription factors.
CC {ECO:0000250|UniProtKB:O43149}.
CC -!- SUBUNIT: Interacts with KLF6 and KLF9 (By similarity). Interacts via
CC (ZZ-type 2 zinc finger) with histone H3 trimethylated at 'Lys-4'
CC (H3K4me3) and histone H3 acetylated at 'Lys-4' (H3K4ac) (By
CC similarity). {ECO:0000250|UniProtKB:O43149}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5SSH7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SSH7-2; Sequence=VSP_025876;
CC Name=3;
CC IsoId=Q5SSH7-3; Sequence=VSP_025877;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37463.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH99976.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC97941.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129131; BAC97941.1; ALT_INIT; mRNA.
DR EMBL; AL663082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037463; AAH37463.1; ALT_INIT; mRNA.
DR EMBL; BC099976; AAH99976.1; ALT_INIT; mRNA.
DR EMBL; AK052734; BAC35122.1; -; mRNA.
DR CCDS; CCDS36218.1; -. [Q5SSH7-2]
DR RefSeq; NP_001039001.1; NM_001045536.2. [Q5SSH7-2]
DR SMR; Q5SSH7; -.
DR IntAct; Q5SSH7; 3.
DR STRING; 10090.ENSMUSP00000068790; -.
DR iPTMnet; Q5SSH7; -.
DR PhosphoSitePlus; Q5SSH7; -.
DR SwissPalm; Q5SSH7; -.
DR EPD; Q5SSH7; -.
DR jPOST; Q5SSH7; -.
DR MaxQB; Q5SSH7; -.
DR PaxDb; Q5SSH7; -.
DR PeptideAtlas; Q5SSH7; -.
DR PRIDE; Q5SSH7; -.
DR ProteomicsDB; 275324; -. [Q5SSH7-1]
DR ProteomicsDB; 275325; -. [Q5SSH7-2]
DR ProteomicsDB; 275326; -. [Q5SSH7-3]
DR Antibodypedia; 23205; 33 antibodies from 9 providers.
DR Ensembl; ENSMUST00000069395; ENSMUSP00000068790; ENSMUSG00000055670. [Q5SSH7-2]
DR GeneID; 195018; -.
DR KEGG; mmu:195018; -.
DR UCSC; uc007jzl.2; mouse. [Q5SSH7-2]
DR CTD; 23140; -.
DR MGI; MGI:2444286; Zzef1.
DR VEuPathDB; HostDB:ENSMUSG00000055670; -.
DR eggNOG; KOG1426; Eukaryota.
DR GeneTree; ENSGT00940000155045; -.
DR InParanoid; Q5SSH7; -.
DR OMA; MMNVTEQ; -.
DR OrthoDB; 256080at2759; -.
DR PhylomeDB; Q5SSH7; -.
DR TreeFam; TF331572; -.
DR BioGRID-ORCS; 195018; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Zzef1; mouse.
DR PRO; PR:Q5SSH7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SSH7; protein.
DR Bgee; ENSMUSG00000055670; Expressed in rostral migratory stream and 223 other tissues.
DR ExpressionAtlas; Q5SSH7; baseline and differential.
DR Genevisible; Q5SSH7; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:MGI.
DR GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0140566; F:histone reader activity; ISS:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0061659; F:ubiquitin-like protein ligase activity; IMP:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IMP:MGI.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR CDD; cd00051; EFh; 1.
DR CDD; cd02343; ZZ_EF; 1.
DR Gene3D; 3.30.60.90; -; 2.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR InterPro; IPR040099; ZZEF1.
DR InterPro; IPR041986; ZZEF1_ZZ.
DR PANTHER; PTHR22772:SF4; PTHR22772:SF4; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF00569; ZZ; 2.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM00291; ZnF_ZZ; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Lipoprotein; Metal-binding;
KW Myristate; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43149"
FT CHAIN 2..2924
FT /note="Zinc finger ZZ-type and EF-hand domain-containing
FT protein 1"
FT /id="PRO_0000289001"
FT DOMAIN 111..146
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 226..405
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT ZN_FING 1776..1831
FT /note="ZZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1825..1880
FT /note="ZZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2388..2418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2398..2418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1781
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1784
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1795
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1798
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1804
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1807
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1817
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1821
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1830
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1833
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1844
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1847
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1853
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1856
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1866
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1870
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43149"
FT MOD_RES 1475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43149"
FT MOD_RES 1488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43149"
FT MOD_RES 1510
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43149"
FT MOD_RES 1515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1519
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1521
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43149"
FT MOD_RES 1535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43149"
FT MOD_RES 1538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 2407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2630
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43149"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:O43149"
FT VAR_SEQ 1..2840
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_025877"
FT VAR_SEQ 2664..2697
FT /note="VRESKHSYNNNTSFEDKVHIPGAIYLSIKFDPQR -> C (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_025876"
FT CONFLICT 2670
FT /note="S -> P (in Ref. 4; BAC35122)"
FT /evidence="ECO:0000305"
FT CONFLICT 2697
FT /note="R -> C (in Ref. 4; BAC35122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2924 AA; 328312 MW; 35E1B0C9981C4B78 CRC64;
MGNAPSNSSE DEAAAAGGEG WSPHQDWAAD SGTTPGPGPA AAVLPSAAAL LEPARLREAA
AALRPAPPCE SLVSRHHGAL LRWLEERLGR GEESVTLEQF RELLEARGAG CSGEQFEEAF
AQFDAEGDGT VDAENMLEAL KNSSGANLQG ELSHVIRQLQ ACSLVPGFID IFSESKEGLG
IHSSMILRFL HRNRISSMVI PYPMLDHCNN MCTMRSSVLK ESLDQLVQKE KESPGDLARS
PEMDKLKSVT KCYAYIETSS NPADIYRMTN GETSSYWQSD GSARSHWIRL KMKPDVVLRH
LSIAVAATDQ SYMPQQVTVA VGRSASDLQE VRDVHIPSNV TGYVTLLENA NISQLYVQIN
IKRCLSDGCD TRIHGLRAVG FQRVKKSGVS VSDASAIWYW SLLTSLVTAS METNPAFVQT
VLHNTQKALQ HMPPLSLSPG STDFSTFLSP NVLEEVDSFL IRITSCCSTP EVELTLLAFA
LARGSIAKVM SSLCTITDHL DTQYDASSLI SSMASVRQNL LLKYGKPLQL TLQACDVKGK
EDKSGPENLL VEPWTRDGFL TETGKTRAST IFSTGSDSAF QVTQIRIMVR RGGIGAQCGL
VFAYNSPSNK FHAEEHFKRF EKYDKWKLQE LRQFVKSRIG CSSDDLGEDD PIGWFELEEE
WDEADVKLQQ CRVAKFLMVK FLCTRQESAE RLGVQGLSIS GYLRPARAEA EQSILYAHCR
RDTENIHGAT LLLRTLQFIQ QLSHDLMQQK ESGLKHKSFL DFAGLDLQIF WKFYSKLKQN
RREECICAQT LLLKLLQSCF SVLQGDPQAA SEEEKPTAQR SEGIQAAKEL YTHLCNVVDK
PNGNSMPMEI LKQEVRNTLL NGAAIFFPDR QTRRSQLFTM MKSVTEHERK QSLQLTFHSL
CTYFSDKDPG GLLLLPEKSD LATMNTSEVL AVMNTLLSVA ARECELLMLN RSHGAVGSVL
FSLFWSVQGS LLSWCFLQLK STDAAAKELA MDLIEKYVGQ FLASMRVILE SLLSQYSGKT
IVEKLCNSVF SMAARQLVIF LLDFCTLDVS HCTLLREFST LTELLKKLCS DPEGGLSKLD
VETWQQEQPV VLHTWTKEST HNYENNCHEV SVFISPGATY FEVEFDERCE TEKRYDYLEF
TDSRGGKTRY DTKVGTYKWP KKVTFKDGPR LQFLFHSDSS NNEWGYKFTV TAYGLPDVAV
SWGLDLQLLV SRLMGRLASQ CMALKSVHQL GSNMAVSQAK LTSVLNSPLW KPVFRHQICP
ELELEASWPT HPHKDGKEVK NIPDDPCRHF LLDFAQSEPA QNFCGPYSEL FKGFIQACRK
QAPKTDIVAG STIDQAVNAT FAALVYRTPD LYEKLQKYVN SGGKIALTEE FSQVYSLADG
IRIWMLEMKQ KSLLSLGNDS EEKRGLEAAE VNPESLAKEC IQKSLLLLKF LPMSKSSKEN
CDKLETVDET DHLQPLDRRQ RTSSVVEEHF QGSASPTEAA TPAAGDRSPA LEIQPKLLPS
SGPCVAEVST AEEPSPPSTP TRRPPFTRGR LRLLSFRSME ETRPVPTVKE KYPVLKDVMD
FIKDQSLSHE SVVKVLSLRK AQGQSILEVL RIIQYCTESL GQPHCFHPPY ILFLLELLTC
QKDFTNYFGH LEGCGADLHR EIRDTYYQLV LFLVKAIKRF SSINDRSLLP ALSCVQTALL
HLLDMGWEPS DLAFFVDIQL PDLLMNMSQE NISVHDSVIS QWSEEDELAD AKQNSEWMDE
CQDGMFEAWY EKIAQEDPEK QRKMHMFIAR YCDLLNVDIS CDGCDEIAPW HRYRCLQCSD
MDLCKTCFLG GVKPEGHGDD HEMVNMEFTC DHCQGLIIGR RMNCNVCDDF DLCYGCYTAK
KYSYGHLPTH SITAHPMVTI RISDRQRLIQ PYIHNYSWLL FAALALYSAH LTSTEQVDGE
QLDPQARTNA ATLRSQCMQL VGDCLMKAHQ GKGLKALALL GVLPDGDSTS ENQALPVTVS
FQASEEQADA GLLVPCNGKR AADTEVRPLD YKQKKKAGED LSIVKDPSCQ TQVSDAPASA
HVPPGLPDAE HPEVSAQVLV EEKAITPNPE QVFAECSQKR ILGLLAAMLP PIKSGPTVPL
IDLEHVLPLM FQVVISNAGH LNETYHLTLG LLGQLIIRLQ PAEVDAAVMK VLSAKHNLRV
GLDWACSMAE ILRSLNNAPL WRDVIATFTD HCIKQLPFQL KHTNIFTLLV LVGFPQVLCV
GTRCVYMDNA NEPHNVIILK HFTEKNRAVI VDVKTRKRKT VKDYQLVQKG GGQECGTSQS
QLSQYSQHFA FIASHLLQTS MDSHCPEAVE ATWVLSLALK GLYKTLKAHG FEETHATFLQ
TDLLKLLVKK CSKGTGFSKT WLLRDLEILS IMLYSSKKEI NTLAEHGDLE LDERGDQEEE
LDRPVSSPGE AEQKKLDPLE NLDEPTRICF LMAHDALNAP LHILRAIYEL QMKKTDSFFL
EVQKRFDGDE LTTDERIRSL AQRWQPSRSL RLEEQSAKAV DTDMIILPCL SRPARSDQAT
PESNPVTQKL ISSTESELQQ SYAKQRRSKS AALLHKELNC KSKRAIRDYL FRVNEATSVL
YARHVLASLL AEWPGHVPVS EDILELSGPA HMTYILDMFM QLEEKHQWEK ILQKVLQGCR
ENMLGTMALA ACQFMEEPGM EVQVRESKHS YNNNTSFEDK VHIPGAIYLS IKFDPQRNTE
EGCDELAMSS SSDFQQDRHN FSGSQQKWKD FELPGDTLYY RFTSDMSNTE WGYRFTVTAG
HLGRFQTGFE ILKQMLSEER VVPHLALGKI WEWLVGVACR QTGHQRLKAI HLLLRIVQCC
SHSDLCDLGL LKPLWQLFTH MEYGLFEDVT QPGILLPLHR ALTELFFVTE NRAQELGLLQ
EYLLALTTED HLLRCAAQAL QNIAAISLAI NYPNKATRLW NVEC
