ANS1B_MOUSE
ID ANS1B_MOUSE Reviewed; 1259 AA.
AC Q8BIZ1; E9Q644; Q4KMR9; Q8BJ47; Q8BJ49;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ankyrin repeat and sterile alpha motif domain-containing protein 1B;
DE AltName: Full=Amyloid-beta protein intracellular domain-associated protein 1;
DE Short=AIDA-1;
DE AltName: Full=E2A-PBX1-associated protein;
DE Short=EB-1;
GN Name=Anks1b;
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] (ISOFORMS 2; 4 AND 5).
RC STRAIN=C57BL/6J;
RC TISSUE=Corpus striatum, Hippocampus, Medulla oblongata, and Olfactory bulb;
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] (ISOFORM 3).
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 4), AND SUBCELLULAR LOCATION.
RX PubMed=15169875; DOI=10.1074/mcp.m400045-mcp200;
RA Jordan B.A., Fernholz B.D., Boussac M., Xu C., Grigorean G., Ziff E.B.,
RA Neubert T.A.;
RT "Identification and verification of novel rodent postsynaptic density
RT proteins.";
RL Mol. Cell. Proteomics 3:857-871(2004).
RN [5]
RP INTERACTION WITH EPHA8.
RX PubMed=17875921; DOI=10.1128/mcb.00794-07;
RA Shin J., Gu C., Park E., Park S.;
RT "Identification of phosphotyrosine binding domain-containing proteins as
RT novel downstream targets of the EphA8 signaling function.";
RL Mol. Cell. Biol. 27:8113-8126(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-900 AND TYR-1006, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; SER-311; SER-315;
RP SER-353; THR-503; SER-507; SER-510; SER-738 AND SER-973, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Isoform 2 may participate in the regulation of nucleoplasmic
CC coilin protein interactions in neuronal and transformed cells.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EPHA8. Isoform 2 interacts with COIL (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Postsynaptic density. Cell
CC projection, dendritic spine. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8BIZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BIZ1-2; Sequence=VSP_032715, VSP_032716, VSP_032717;
CC Name=3;
CC IsoId=Q8BIZ1-3; Sequence=VSP_032714, VSP_032719;
CC Name=4;
CC IsoId=Q8BIZ1-4; Sequence=VSP_032715, VSP_032716, VSP_032718;
CC Name=5;
CC IsoId=Q8BIZ1-5; Sequence=VSP_032713;
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DR EMBL; AK032061; BAC27677.1; -; mRNA.
DR EMBL; AK032211; BAC27761.1; -; mRNA.
DR EMBL; AK049899; BAC33978.1; -; mRNA.
DR EMBL; AK163750; BAE37478.1; -; mRNA.
DR EMBL; AC107661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC151984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC098373; AAH98373.1; -; mRNA.
DR CCDS; CCDS59552.1; -. [Q8BIZ1-4]
DR CCDS; CCDS59553.1; -. [Q8BIZ1-2]
DR CCDS; CCDS59554.1; -. [Q8BIZ1-3]
DR CCDS; CCDS83746.1; -. [Q8BIZ1-5]
DR RefSeq; NP_001170868.1; NM_001177397.1.
DR RefSeq; NP_001170869.1; NM_001177398.1.
DR RefSeq; NP_001333982.1; NM_001347053.1.
DR RefSeq; NP_001333983.1; NM_001347054.1.
DR RefSeq; NP_852063.1; NM_181398.3.
DR AlphaFoldDB; Q8BIZ1; -.
DR SMR; Q8BIZ1; -.
DR BioGRID; 218749; 7.
DR IntAct; Q8BIZ1; 153.
DR MINT; Q8BIZ1; -.
DR STRING; 10090.ENSMUSP00000138539; -.
DR iPTMnet; Q8BIZ1; -.
DR PhosphoSitePlus; Q8BIZ1; -.
DR MaxQB; Q8BIZ1; -.
DR PaxDb; Q8BIZ1; -.
DR PeptideAtlas; Q8BIZ1; -.
DR PRIDE; Q8BIZ1; -.
DR ProteomicsDB; 281886; -. [Q8BIZ1-1]
DR ProteomicsDB; 281887; -. [Q8BIZ1-2]
DR ProteomicsDB; 281888; -. [Q8BIZ1-3]
DR ProteomicsDB; 281889; -. [Q8BIZ1-4]
DR ProteomicsDB; 281890; -. [Q8BIZ1-5]
DR GeneID; 77531; -.
DR KEGG; mmu:77531; -.
DR UCSC; uc033fry.1; mouse. [Q8BIZ1-4]
DR UCSC; uc033frz.1; mouse. [Q8BIZ1-2]
DR CTD; 56899; -.
DR MGI; MGI:1924781; Anks1b.
DR eggNOG; KOG0507; Eukaryota.
DR InParanoid; Q8BIZ1; -.
DR OrthoDB; 549581at2759; -.
DR BioGRID-ORCS; 77531; 1 hit in 69 CRISPR screens.
DR ChiTaRS; Anks1b; mouse.
DR PRO; PR:Q8BIZ1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BIZ1; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:MGI.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; ISO:MGI.
DR GO; GO:0097120; P:receptor localization to synapse; ISO:MGI.
DR GO; GO:1900383; P:regulation of synaptic plasticity by receptor localization to synapse; IMP:MGI.
DR CDD; cd09499; SAM_AIDA1AB-like_repeat1; 1.
DR CDD; cd09500; SAM_AIDA1AB-like_repeat2; 1.
DR Gene3D; 1.10.150.50; -; 2.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR033636; ANKS1B.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR041880; SAM_ANKS1_repeat1.
DR InterPro; IPR041882; SAM_ANKS1_repeat2.
DR PANTHER; PTHR24174:SF3; PTHR24174:SF3; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00536; SAM_1; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00454; SAM; 2.
DR SUPFAM; SSF47769; SSF47769; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell projection; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1259
FT /note="Ankyrin repeat and sterile alpha motif domain-
FT containing protein 1B"
FT /id="PRO_0000327260"
FT REPEAT 2..31
FT /note="ANK 1"
FT REPEAT 58..87
FT /note="ANK 2"
FT REPEAT 91..120
FT /note="ANK 3"
FT REPEAT 127..156
FT /note="ANK 4"
FT REPEAT 160..189
FT /note="ANK 5"
FT REPEAT 193..222
FT /note="ANK 6"
FT REPEAT 225..254
FT /note="ANK 7"
FT DOMAIN 809..875
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 883..948
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1055..1212
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 298..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 934
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 305..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C6S7"
FT MOD_RES 503
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 772
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0C6S7"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C6S7"
FT MOD_RES 900
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1006
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT VAR_SEQ 1..993
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032713"
FT VAR_SEQ 1..830
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032714"
FT VAR_SEQ 1..773
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032715"
FT VAR_SEQ 774..806
FT /note="SFTSEWEEIDKIMNSIDVGINSELEGMNGETTR -> MMWQCHPSAPDYRYY
FT PVDGYSLLKRFPLHPLTG (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032716"
FT VAR_SEQ 962..1021
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032717"
FT VAR_SEQ 962..1021
FT /note="EPSGNHTPPQLSPSLSQSTYTTGGSLDVPHIIMQGDARRRRNENYFDDIPRS
FT KLERQMAQ -> QSSVCEIWTNQNAGFPFSAIHQVHN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032718"
FT VAR_SEQ 1224..1259
FT /note="QIDPSEQKTLANLPWIVEPGQEAKRGINTKYETTIF -> APQTSCPNRLV
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032719"
FT CONFLICT 1092
FT /note="R -> Q (in Ref. 1; BAC27677/BAC27761/BAC33978/
FT BAE37478 and 3; AAH98373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1259 AA; 139047 MW; 90956D38BF970B1C CRC64;
MGKDQELLEA ARTGNVALVE KLLSGRKGGI LGGGSGPLPL SNLLSIWRGP NVNCTDSSGY
TALHHAALNG HKDIVLKLLQ YEASTNVADN KGYFPIHLAA WKGDVEIVKI LIHHGPSHSR
VNEQNNENET ALHCAAQYGH SEVVAVLLEE LTDPTIRNSK LETPLDLAAL YGRLRVVKMI
ISAHPNLMSC NTRKHTPLHL AARNGHKAVV QVLLEAGMDV SCQTEKGSAL HEAALFGKVD
VVRVLLETGI DANIKDSLGR TVLDILKEHP SQKSLQIATL LQDYLEGAGR SAAVLEEHAQ
EDTAQETHLS SPAESPQKTK SETVTGELSK LLDEIKLCQE KDYSFEDLCH TISDHYLDNL
SKISEEELGK NGSQSVRTSS TINLSPGEVE DEEEDPNSCG PTGLWEALTP CNGCRNLGFP
MLAQESYPKK RNFPMEMEPS ASLDTFPSEN ENFLCELVDT AVTKKPCSLE IARAPSPRTD
NASEVAITAP GTSHHRNSST GPTPDCSPPS PDTALKNIVK VIRPQPKQRT SIVSSLDFQR
MNHNQEYFEI STSTGCTSFT SSPAASPPTS SVETTEVKNE GAEHADDLSQ QEDDEPPKEY
DAGQFAGLLH GSSPACESPE NPFHLYGKRN TCEDGPDEAS LANSPLPFKQ TPIENNPEPS
VKKVKPKVVS RTIFHKRNHQ LENHTIVGTR MSRSGSRNGD QWGVNPGGFV ERACTLGRIR
SLPKALIDMH LSKNVSKSDS DLIAYPSKDK ARVNWSKSST AERSSKDNSE RTPSFTSEWE
EIDKIMNSID VGINSELEGM NGETTRPRCP VQTVGQWLES IGLPQYENHL MANGFDSVQF
MGSNVMEDQD LLEIGILNSG HRQRILQAIQ LLPKMRPIGH DGYHPTSVAE WLDSIELGDY
TKAFLINGYT SMDLLKKIWE LELINVLKIS LIGHRKRILA SLGDRLHDDP PQKPPRSITL
REPSGNHTPP QLSPSLSQST YTTGGSLDVP HIIMQGDARR RRNENYFDDI PRSKLERQMA
QTGDWGEPSI TLRPPNEATA STPVQYWQHH PEKLIFQSCD YKAFYLGSML IKELRGTEST
QDACAKMRAN CRKSTEQMKK VPTIILSVSY KGVKFIDAAN KNIIAEHEIR NISCAAQDPE
DLSTFAYITK DLKSNHHYCH VFTAFDVNLA YEIILTLGQA FEVAYQLALQ ARKGGHSSTL
PESFENKPSK PIPKPRVSIR KSVQIDPSEQ KTLANLPWIV EPGQEAKRGI NTKYETTIF
