NFIA_MOUSE
ID NFIA_MOUSE Reviewed; 532 AA.
AC Q02780; P70250; P70251; Q3UUZ2; Q61960; Q8VBT5; Q9R1G5;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Nuclear factor 1 A-type;
DE Short=NF1-A;
DE Short=Nuclear factor 1/A;
DE AltName: Full=CCAAT-box-binding transcription factor;
DE Short=CTF;
DE AltName: Full=Nuclear factor I/A;
DE Short=NF-I/A;
DE Short=NFI-A;
DE AltName: Full=TGGCA-binding protein;
GN Name=Nfia;
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 [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND PARTIAL NUCLEOTIDE
RP SEQUENCE (ISOFORM 6).
RC TISSUE=Brain;
RX PubMed=1699939; DOI=10.1016/s0021-9258(17)30625-7;
RA Inoue T., Tamura T.A., Furuichi T., Mikoshiba K.;
RT "Isolation of complementary DNAs encoding a cerebellum-enriched nuclear
RT factor I family that activates transcription from the mouse myelin basic
RT protein promoter.";
RL J. Biol. Chem. 265:19065-19070(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 7).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX PubMed=11978849; DOI=10.1523/jneurosci.22-09-03730.2002;
RA Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.;
RT "Congenic mapping of alcohol and pentobarbital withdrawal liability loci to
RT a <1 centimorgan interval of murine chromosome 4: identification of Mpdz as
RT a candidate gene.";
RL J. Neurosci. 22:3730-3738(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 5).
RC STRAIN=NIH Swiss; TISSUE=Embryo;
RX PubMed=12568726; DOI=10.1016/s0378-1119(02)01204-0;
RA Gruender A., Qian F., Ebel T.T., Mincheva A., Lichter P., Kruse U.,
RA Sippel A.E.;
RT "Genomic organization, splice products and mouse chromosomal localization
RT of genes for transcription factor Nuclear Factor One.";
RL Gene 304:171-181(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC STRAIN=C57BL/6J; TISSUE=Vagina;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 2-509 (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=9056636;
RX DOI=10.1002/(sici)1097-0177(199703)208:3<313::aid-aja3>3.0.co;2-l;
RA Chaudhry A.Z., Lyons G.E., Gronostajski R.M.;
RT "Expression patterns of the four nuclear factor I genes during mouse
RT embryogenesis indicate a potential role in development.";
RL Dev. Dyn. 208:313-325(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-209.
RC STRAIN=129;
RX PubMed=10087299; DOI=10.1007/s003359901008;
RA Fletcher C.F., Jenkins N.A., Copeland N.G., Chaudhry A.Z.,
RA Gronostajski R.M.;
RT "Exon structure of the nuclear factor I DNA-binding domain from C. elegans
RT to mammals.";
RL Mamm. Genome 10:390-396(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; SER-310; SER-323 AND
RP SER-342, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; SER-310; SER-323 AND
RP SER-342, 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).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-412, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Recognizes and binds the palindromic sequence 5'-
CC TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the
CC origin of replication of adenovirus type 2. These proteins are
CC individually capable of activating transcription and replication.
CC -!- SUBUNIT: Binds DNA as a homodimer.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=2;
CC IsoId=Q02780-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q02780-2; Sequence=VSP_003537, VSP_003544;
CC Name=3;
CC IsoId=Q02780-3; Sequence=VSP_003538;
CC Name=4;
CC IsoId=Q02780-4; Sequence=VSP_003539;
CC Name=5;
CC IsoId=Q02780-5; Sequence=VSP_003537, VSP_003541;
CC Name=6;
CC IsoId=Q02780-6; Sequence=VSP_003540, VSP_003542, VSP_003543;
CC Name=7;
CC IsoId=Q02780-7; Sequence=VSP_003537;
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:Q12857}.
CC -!- MISCELLANEOUS: [Isoform 4]: Incomplete sequence. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Incomplete sequence. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CTF/NF-I family. {ECO:0000255|PROSITE-
CC ProRule:PRU00436}.
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DR EMBL; D90172; BAA20909.1; -; mRNA.
DR EMBL; D90173; BAA14203.1; -; mRNA.
DR EMBL; D90174; BAA14204.1; -; mRNA.
DR EMBL; D90175; BAA14205.1; -; mRNA.
DR EMBL; D90176; BAA14206.1; -; mRNA.
DR EMBL; AF326554; AAL37400.1; -; mRNA.
DR EMBL; AF326553; AAL37399.1; -; mRNA.
DR EMBL; Y07690; CAA68954.1; -; mRNA.
DR EMBL; Y07691; CAA68955.1; -; mRNA.
DR EMBL; AK137731; BAE23481.1; -; mRNA.
DR EMBL; AK052204; BAC34883.1; -; mRNA.
DR EMBL; U57633; AAB49928.1; -; mRNA.
DR EMBL; AF111263; AAD39098.1; -; Genomic_DNA.
DR CCDS; CCDS18373.1; -. [Q02780-7]
DR CCDS; CCDS51234.1; -. [Q02780-5]
DR PIR; B36596; B36596.
DR RefSeq; NP_001116424.1; NM_001122952.1. [Q02780-1]
DR RefSeq; NP_001116425.1; NM_001122953.1. [Q02780-5]
DR RefSeq; NP_035035.1; NM_010905.3. [Q02780-7]
DR RefSeq; XP_006502905.1; XM_006502842.3. [Q02780-3]
DR AlphaFoldDB; Q02780; -.
DR IntAct; Q02780; 1.
DR STRING; 10090.ENSMUSP00000074899; -.
DR CarbonylDB; Q02780; -.
DR iPTMnet; Q02780; -.
DR PhosphoSitePlus; Q02780; -.
DR EPD; Q02780; -.
DR jPOST; Q02780; -.
DR MaxQB; Q02780; -.
DR PaxDb; Q02780; -.
DR PeptideAtlas; Q02780; -.
DR PRIDE; Q02780; -.
DR ProteomicsDB; 287490; -. [Q02780-1]
DR ProteomicsDB; 287491; -. [Q02780-2]
DR ProteomicsDB; 287492; -. [Q02780-3]
DR ProteomicsDB; 287493; -. [Q02780-4]
DR ProteomicsDB; 287494; -. [Q02780-5]
DR ProteomicsDB; 287495; -. [Q02780-6]
DR ProteomicsDB; 287496; -. [Q02780-7]
DR Antibodypedia; 1812; 290 antibodies from 31 providers.
DR DNASU; 18027; -.
DR Ensembl; ENSMUST00000075448; ENSMUSP00000074899; ENSMUSG00000028565. [Q02780-7]
DR Ensembl; ENSMUST00000092532; ENSMUSP00000130032; ENSMUSG00000028565. [Q02780-5]
DR GeneID; 18027; -.
DR KEGG; mmu:18027; -.
DR UCSC; uc008tts.2; mouse. [Q02780-1]
DR UCSC; uc008ttt.2; mouse. [Q02780-6]
DR UCSC; uc008ttu.2; mouse. [Q02780-7]
DR UCSC; uc008ttv.2; mouse. [Q02780-5]
DR CTD; 4774; -.
DR MGI; MGI:108056; Nfia.
DR VEuPathDB; HostDB:ENSMUSG00000028565; -.
DR eggNOG; KOG3663; Eukaryota.
DR GeneTree; ENSGT00950000182916; -.
DR InParanoid; Q02780; -.
DR OMA; XSPHATP; -.
DR OrthoDB; 967862at2759; -.
DR PhylomeDB; Q02780; -.
DR TreeFam; TF313889; -.
DR BioGRID-ORCS; 18027; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Nfia; mouse.
DR PRO; PR:Q02780; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q02780; protein.
DR Bgee; ENSMUSG00000028565; Expressed in ureter smooth muscle and 262 other tissues.
DR ExpressionAtlas; Q02780; baseline and differential.
DR Genevisible; Q02780; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA: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:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060074; P:synapse maturation; IMP:MGI.
DR GO; GO:0072189; P:ureter development; IMP:MGI.
DR InterPro; IPR000647; CTF/NFI.
DR InterPro; IPR020604; CTF/NFI_DNA-bd-dom.
DR InterPro; IPR019739; CTF/NFI_DNA-bd_CS.
DR InterPro; IPR019548; CTF/NFI_DNA-bd_N.
DR InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR PANTHER; PTHR11492; PTHR11492; 1.
DR Pfam; PF00859; CTF_NFI; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF10524; NfI_DNAbd_pre-N; 1.
DR SMART; SM00523; DWA; 1.
DR PROSITE; PS00349; CTF_NFI_1; 1.
DR PROSITE; PS51080; CTF_NFI_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA replication; DNA-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..532
FT /note="Nuclear factor 1 A-type"
FT /id="PRO_0000100192"
FT DNA_BIND 24..217
FT /note="CTF/NF-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00436"
FT REGION 212..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 417..425
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:Q12857"
FT COMPBIAS 282..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..480
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12857"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12857"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09414"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12857"
FT MOD_RES 412
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12857"
FT MOD_RES 494
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12857"
FT VAR_SEQ 1..32
FT /note="MKLADSVMAGKASDGSIKWQLCYDISARTWWM -> MYSPLCLTQ (in
FT isoform 1, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:1699939, ECO:0000303|PubMed:9056636"
FT /id="VSP_003537"
FT VAR_SEQ 1..32
FT /note="MKLADSVMAGKASDGSIKWQLCYDISARTWWM -> VWFQQPLPFADLLPGN
FT SIHTASPTCLTQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1699939"
FT /id="VSP_003539"
FT VAR_SEQ 1..32
FT /note="MKLADSVMAGKASDGSIKWQLCYDISARTWWM -> LSPPLSPSRTHTHAHL
FT QPAHRRARTPRRPAVMYSPLCLTQ (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_003540"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1699939"
FT /id="VSP_003538"
FT VAR_SEQ 339..381
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003541"
FT VAR_SEQ 340..370
FT /note="LPSPSTLKKSEKSGFSSPSPSQTSSLGTAFT -> EQSHKREGNGVCVWLCC
FT HGRVVESSRYNGSA (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_003542"
FT VAR_SEQ 371..532
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_003543"
FT VAR_SEQ 476..532
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:1699939,
FT ECO:0000303|PubMed:9056636"
FT /id="VSP_003544"
SQ SEQUENCE 532 AA; 58553 MW; 3AECEEDCD65D28B3 CRC64;
MKLADSVMAG KASDGSIKWQ LCYDISARTW WMDEFHPFIE ALLPHVRAFA YTWFNLQARK
RKYFKKHEKR MSKEEERAVK DELLSEKPEV KQKWASRLLA KLRKDIRPEY REDFVLTVTG
KKPPCCVLSN PDQKGKMRRI DCLRQADKVW RLDLVMVILF KGIPLESTDG ERLVKSPQCS
NPGLCVQPHH IGVSVKELDL YLAYFVHAAD SSQSESPSQP SEADIKDQPE NGHLGFQDSF
VTSGVFSVTE LVRVSQTPIA AGTGPNFSLS DLESSSYYSM SPGAMRRSLP STSSTSSTKR
LKSVEDEMDS PGEEPFYTGQ GRSPGSGSQS SGWHEVEPGL PSPSTLKKSE KSGFSSPSPS
QTSSLGTAFT QHHRPVITGP RASPHATPST LHFPTSPIIQ QPGPYFSHPA IRYHPQETLK
EFVQLVCPDA GQQAGQVGFL NPNGSSQGKV HNPFLPTPML PPPPPPPMAR PVPLPMPDTK
PPTTSTEGGA ASPTSPTYST PSTSPANRFV SVGPRDPSFV NIPQQTQSWY LG
