EFCB6_MOUSE
ID EFCB6_MOUSE Reviewed; 1516 AA.
AC Q6P1E8; A6PW10; A6PW11; A6PW12; Q5DTV8; Q6PGK8; Q9D2D8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=EF-hand calcium-binding domain-containing protein 6;
DE AltName: Full=DJ-1-binding protein;
DE Short=DJBP;
GN Name=Efcab6; Synonyms=Djbp, Kiaa1672;
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 2).
RC STRAIN=C57BL/6J; TISSUE=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal 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 [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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 THR-906; SER-1265; SER-1311;
RP THR-1315 AND THR-1319, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- FUNCTION: Negatively regulates the androgen receptor by recruiting
CC histone deacetylase complex, and protein DJ-1 antagonizes this
CC inhibition by abrogation of this complex. Microtubule inner protein
CC (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia
CC axoneme, which is required for motile cilia beating.
CC {ECO:0000250|UniProtKB:Q5THR3}.
CC -!- SUBUNIT: Binds PARK7. Part of a ternary complex containing PARK7,
CC EFCAB6/DJBP and AR (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5THR3}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q5THR3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P1E8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1E8-3; Sequence=VSP_019814;
CC Name=3;
CC IsoId=Q6P1E8-4; Sequence=VSP_029427, VSP_029428;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH56955.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH65111.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK019850; BAB31880.1; -; mRNA.
DR EMBL; AK220412; BAD90458.1; -; mRNA.
DR EMBL; AL513354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL603867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056955; AAH56955.1; ALT_INIT; mRNA.
DR EMBL; BC065111; AAH65111.1; ALT_INIT; mRNA.
DR CCDS; CCDS27707.2; -. [Q6P1E8-1]
DR RefSeq; NP_001155100.1; NM_001161628.1. [Q6P1E8-3]
DR RefSeq; NP_001155101.1; NM_001161629.1. [Q6P1E8-4]
DR RefSeq; NP_084222.4; NM_029946.4. [Q6P1E8-1]
DR RefSeq; XP_006521596.1; XM_006521533.2. [Q6P1E8-1]
DR RefSeq; XP_017172280.1; XM_017316791.1. [Q6P1E8-1]
DR AlphaFoldDB; Q6P1E8; -.
DR SMR; Q6P1E8; -.
DR BioGRID; 218809; 2.
DR STRING; 10090.ENSMUSP00000114909; -.
DR iPTMnet; Q6P1E8; -.
DR PhosphoSitePlus; Q6P1E8; -.
DR MaxQB; Q6P1E8; -.
DR PaxDb; Q6P1E8; -.
DR PRIDE; Q6P1E8; -.
DR ProteomicsDB; 277445; -. [Q6P1E8-1]
DR ProteomicsDB; 277446; -. [Q6P1E8-3]
DR ProteomicsDB; 277447; -. [Q6P1E8-4]
DR Antibodypedia; 320; 28 antibodies from 10 providers.
DR Ensembl; ENSMUST00000156187; ENSMUSP00000114909; ENSMUSG00000022441. [Q6P1E8-1]
DR GeneID; 77627; -.
DR KEGG; mmu:77627; -.
DR UCSC; uc007xbo.1; mouse. [Q6P1E8-4]
DR UCSC; uc007xbq.1; mouse. [Q6P1E8-1]
DR CTD; 64800; -.
DR MGI; MGI:1924877; Efcab6.
DR VEuPathDB; HostDB:ENSMUSG00000022441; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00390000013629; -.
DR HOGENOM; CLU_004260_0_0_1; -.
DR InParanoid; Q6P1E8; -.
DR OMA; IHWKYFL; -.
DR OrthoDB; 193070at2759; -.
DR PhylomeDB; Q6P1E8; -.
DR TreeFam; TF329179; -.
DR BioGRID-ORCS; 77627; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Efcab6; mouse.
DR PRO; PR:Q6P1E8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6P1E8; protein.
DR Bgee; ENSMUSG00000022441; Expressed in spermatid and 55 other tissues.
DR ExpressionAtlas; Q6P1E8; baseline and differential.
DR Genevisible; Q6P1E8; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR015070; EF_hand_DJBP.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF08976; EF-hand_11; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 11.
DR SUPFAM; SSF47473; SSF47473; 7.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 15.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell projection; Cytoplasm; Cytoskeleton;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1516
FT /note="EF-hand calcium-binding domain-containing protein 6"
FT /id="PRO_0000246026"
FT DOMAIN 96..131
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 197..232
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 321..356
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 444..462
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 528..563
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 674..690
FT /note="EF-hand 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 763..798
FT /note="EF-hand 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 905..940
FT /note="EF-hand 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1086..1121
FT /note="EF-hand 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1193..1228
FT /note="EF-hand 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1229..1264
FT /note="EF-hand 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1348..1373
FT /note="EF-hand 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1374..1409
FT /note="EF-hand 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1454..1484
FT /note="EF-hand 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1485..1516
FT /note="EF-hand 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1516
FT /note="Interaction with PARK7"
FT /evidence="ECO:0000250"
FT REGION 1422..1516
FT /note="Interaction with AR"
FT /evidence="ECO:0000250"
FT COMPBIAS 8..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 776
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 778
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 780
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 787
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 906
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1315
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1319
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..838
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_029427"
FT VAR_SEQ 1..688
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_019814"
FT VAR_SEQ 839..844
FT /note="PQRLIR -> MSKKHG (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_029428"
FT CONFLICT 632
FT /note="E -> K (in Ref. 4; AAH65111)"
FT /evidence="ECO:0000305"
FT CONFLICT 1101
FT /note="E -> V (in Ref. 2; BAD90458)"
FT /evidence="ECO:0000305"
FT CONFLICT 1181
FT /note="R -> K (in Ref. 2; BAD90458)"
FT /evidence="ECO:0000305"
FT CONFLICT 1391
FT /note="Missing (in Ref. 4; AAH56955)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1516 AA; 175771 MW; 786C634E6CFA5CFD CRC64;
MKRNGTRLNF AKANSTKSGS TRARDLMNKM SIIPEWHSLY SNTRKLPCSR PHSSPCKMQR
TIFQDLCRPS SSTTAIANPV LSYLDIERIL AQKISSRRDD IKKVFQILDR NHNQMVTKGD
LKRVITAFLI PLTKDQFQDL LAQIPISSLG NVPYLEFLSR FGGGIDININ GIKRVNENEV
DNRRTVKEVQ LTEKIFRNMR SIRKVFQVMD VNNTGLVQPQ ELRRVLETFC LRMQDGDYEK
FLEQYNIDKT TAVDYNAFLK NLSVKNDASF KYLLSNAAEL SRETQQGKNG KRLLDTGSSE
DVWKNYSLDD LEKTFCQEFS KSYEKIEKAL SAGDPSKGGY ISLNYLKVVL DTFIYRLPRR
IFIQLIRRFG LKTSTKINWK QFLTAIYERQ KLEVSKTLPL KKRSSTEARN RSRKENIIKK
LFKYSEDRYT ALKKTLLIIS STPSGHITWE ELRHILNCMV AKLNDSEFSE LKQTFDPEGT
GAVRVNSLLD VLDDSTKVRK MSPSTDTKTP LPVAWDSVEE LVLDSITRNL QAFYSMLQSY
DLRDTGTIGK NNFRKVMRVF CPYLSNEHLV RFSSKFQEAG SGRILYKKFL LSIGVGIPPP
TPPLSSPKVQ LSDQFQIEEP GQQDERTQPS GEKTSEINNM TKEEVIDGLK HRIQQKDPVF
RKQFLSISKE PDVKINQEEF RKVLERSGMP MNDCQYAMLA SKLGFKNEEG MSYQDFTMGF
EDCMLSGLET VPLQSRTASR TNMDEHFISA EECLRIFPKK LKESFRDVYS AFFRIDLDRD
GIISMHDFHR LLQYLQLNMV DLEFERFLSL LGLRLSVTLN FREFQNLCEK RPWKSDEAPQ
RLIRCKQKVA DSELACEQAH QYLIMKAKTR WADLSKNFIE TDNEGNGILR RRDIKNSLYG
FDIPLTPREF EKLWQNYDTE GRGYITYQEF LHRLGIRYSP KVHRPYKEDY FNFLGHFTKP
KQVQEEIQEL QQISEREKLM NHYEEISKAF NAMEKSKPVA LCRVQKVLQE CGCPLKEEEL
ISLLKSLDVS VHNNHIDPVE FLRALEISWA SKARPKEKEE SSPPPISFSK VTPDEVIKTM
QEVVESSQPA LVEAFSALDK EDTGFVKAME FGDVLRSVCQ KLTDNQYHYF LRRLRLHLTP
NIHWKYFLEN FSTFQDETAD DWAENMPKAP PPMSPKETAH RDIVARVQKA VASHYHTIVQ
EFENFDTLKS NTVSRDEFRS ICTRHIQILT DEQFDRLWSE LPVNAKGRLK YQDFLSKLSI
ERVPSPPMAA GDSGESTMAQ RGSSAPEFSQ GTRSNLYSPP RDSRVGLKSR SHPCTPVGTP
PLQNCEPIES RLRKQIQGCW RELLRECKEK DTDKQGTISA AEFLALVEKF KLDISREESQ
QLIVKYDLKN NGKFAYCDFI QSCVLLLKAK ETSLMRRMRI QNADKMKEAG METPSFYSAL
LRIQPKIVHC WRPMRRSFKT YDKNGTGLLS VADFRKVLRQ YSINLSEEEF FHVLEYYDKS
LSSKISYNDF LRAFLQ
