CTTB2_MOUSE
ID CTTB2_MOUSE Reviewed; 1648 AA.
AC B9EJA2; G3X9L7; Q69ZB2; Q8BVG1; Q8C044;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=Cttnbp2; Synonyms=Kiaa1758;
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), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 470-1648 (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Skin;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1648 (ISOFORM 4).
RC TISSUE=Pancreas islet cell;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1510, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
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 [7]
RP INTERACTION WITH CTTN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF PRO-540; PRO-543; PRO-599 AND PRO-602.
RX PubMed=22262902; DOI=10.1523/jneurosci.4405-11.2012;
RA Chen Y.K., Hsueh Y.P.;
RT "Cortactin-binding protein 2 modulates the mobility of cortactin and
RT regulates dendritic spine formation and maintenance.";
RL J. Neurosci. 32:1043-1055(2012).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23015759; DOI=10.1091/mbc.e12-05-0365;
RA Chen Y.K., Chen C.Y., Hu H.T., Hsueh Y.P.;
RT "CTTNBP2, but not CTTNBP2NL, regulates dendritic spinogenesis and synaptic
RT distribution of the striatin-PP2A complex.";
RL Mol. Biol. Cell 23:4383-4392(2012).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-495, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and 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: Regulates the dendritic spine distribution of CTTN/cortactin
CC in hippocampal neurons, and thus controls dendritic spinogenesis and
CC dendritic spine maintenance. {ECO:0000269|PubMed:23015759}.
CC -!- SUBUNIT: Interacts with CTTN/cortactin SH3 domain. Interacts with STRN,
CC STRN4/zinedin and MOB4/phocein; this interaction may regulate dendritic
CC spine distribution of STRN and STRN4 in hippocampal neurons (By
CC similarity). Activation of glutamate receptors weakens the interaction
CC with STRN and STRN4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cell projection,
CC dendritic spine. Note=Remains associated with dendritic spines even
CC after glutamate stimulation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=CTTNBP2-L;
CC IsoId=B9EJA2-1; Sequence=Displayed;
CC Name=2; Synonyms=CTTNBP2-S;
CC IsoId=B9EJA2-2; Sequence=VSP_046474, VSP_046475;
CC Name=3; Synonyms=CTTNBP2-intron;
CC IsoId=B9EJA2-3; Sequence=VSP_046476, VSP_046477;
CC Name=4;
CC IsoId=B9EJA2-4; Sequence=VSP_046478;
CC Name=5;
CC IsoId=B9EJA2-5; Sequence=VSP_046473;
CC -!- TISSUE SPECIFICITY: Isoform 2 is predominantly expressed in brain (at
CC protein level). In the brain, expressed at high levels in hypothalamus
CC and striatum and at lower levels in cerebellum and cortex.
CC {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32532.1; Type=Miscellaneous discrepancy; Note=Erroneous CDS prediction and frameshift.; Evidence={ECO:0000305};
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DR EMBL; AK028980; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK032356; BAC27832.1; -; mRNA.
DR EMBL; AK078315; BAC37216.1; -; mRNA.
DR EMBL; AC027654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466533; EDL13863.1; -; Genomic_DNA.
DR EMBL; BC068156; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BQ769661; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC141407; AAI41408.1; -; mRNA.
DR EMBL; CB526439; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK173254; BAD32532.1; ALT_SEQ; mRNA.
DR CCDS; CCDS39432.1; -. [B9EJA2-1]
DR RefSeq; NP_525024.1; NM_080285.1. [B9EJA2-1]
DR RefSeq; XP_006505167.1; XM_006505104.2. [B9EJA2-5]
DR AlphaFoldDB; B9EJA2; -.
DR SMR; B9EJA2; -.
DR BioGRID; 205963; 27.
DR IntAct; B9EJA2; 4.
DR MINT; B9EJA2; -.
DR STRING; 10090.ENSMUSP00000088089; -.
DR iPTMnet; B9EJA2; -.
DR PhosphoSitePlus; B9EJA2; -.
DR PaxDb; B9EJA2; -.
DR PeptideAtlas; B9EJA2; -.
DR PRIDE; B9EJA2; -.
DR ProteomicsDB; 279291; -. [B9EJA2-1]
DR ProteomicsDB; 279292; -. [B9EJA2-2]
DR ProteomicsDB; 279293; -. [B9EJA2-3]
DR ProteomicsDB; 279294; -. [B9EJA2-4]
DR ProteomicsDB; 279295; -. [B9EJA2-5]
DR Antibodypedia; 3970; 95 antibodies from 19 providers.
DR Ensembl; ENSMUST00000090601; ENSMUSP00000088089; ENSMUSG00000000416. [B9EJA2-1]
DR Ensembl; ENSMUST00000148602; ENSMUSP00000118432; ENSMUSG00000000416. [B9EJA2-2]
DR GeneID; 30785; -.
DR KEGG; mmu:30785; -.
DR UCSC; uc009bak.1; mouse. [B9EJA2-1]
DR UCSC; uc009ban.1; mouse. [B9EJA2-3]
DR CTD; 83992; -.
DR MGI; MGI:1353467; Cttnbp2.
DR VEuPathDB; HostDB:ENSMUSG00000000416; -.
DR eggNOG; ENOG502QWG2; Eukaryota.
DR GeneTree; ENSGT00940000158293; -.
DR HOGENOM; CLU_028813_1_0_1; -.
DR InParanoid; B9EJA2; -.
DR OMA; MCPVEAL; -.
DR OrthoDB; 264951at2759; -.
DR PhylomeDB; B9EJA2; -.
DR TreeFam; TF325130; -.
DR BioGRID-ORCS; 30785; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cttnbp2; mouse.
DR PRO; PR:B9EJA2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; B9EJA2; protein.
DR Bgee; ENSMUSG00000000416; Expressed in caudate-putamen and 190 other tissues.
DR ExpressionAtlas; B9EJA2; baseline and differential.
DR Genevisible; B9EJA2; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR019131; Cortactin-binding_p2_N.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF09727; CortBP2; 2.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell projection; Coiled coil; Cytoplasm;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1648
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000422172"
FT REPEAT 699..729
FT /note="ANK 1"
FT REPEAT 733..762
FT /note="ANK 2"
FT REPEAT 766..795
FT /note="ANK 3"
FT REPEAT 799..828
FT /note="ANK 4"
FT REPEAT 832..861
FT /note="ANK 5"
FT REPEAT 901..931
FT /note="ANK 6"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1522..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..274
FT /evidence="ECO:0000255"
FT COMPBIAS 200..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 495
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 626..680
FT /note="VGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVA
FT ASG -> KIQKVKCTREEPSC (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_046473"
FT VAR_SEQ 626..630
FT /note="VGAWP -> AGHPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046474"
FT VAR_SEQ 631..1648
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046475"
FT VAR_SEQ 681..710
FT /note="WSPSLTPLLMSGGPAPLAGRPTLLQQAAAQ -> KGIEVFYPFVKNVPYSLT
FT SLNFFYVVLKRF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_046476"
FT VAR_SEQ 711..1648
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_046477"
FT VAR_SEQ 1568..1648
FT /note="EASPPSSRQTAECSNSKSKTEMGVSSVKSFLPVPRSKVAQCSQNTKRNSSSS
FT NTRQLEINNNSKEENWTLDKHEQVEKPNK -> KQSRSVFPEHQKKQQQQQYKATRNQQ
FT QLQRRELDLRQTRTSRKTKQIGLPTPPTTT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_046478"
FT MUTAGEN 540
FT /note="P->A: Almost complete loss of CTTN-binding and loss
FT of regulation of spine density; when associated with A-
FT 543."
FT /evidence="ECO:0000269|PubMed:22262902"
FT MUTAGEN 543
FT /note="P->A: Almost complete loss of CTTN-binding and loss
FT of regulation of spine density; when associated with A-
FT 540."
FT /evidence="ECO:0000269|PubMed:22262902"
FT MUTAGEN 599
FT /note="P->A: Reduced CTTN-binding; when associated with A-
FT 602."
FT /evidence="ECO:0000269|PubMed:22262902"
FT MUTAGEN 602
FT /note="P->A: Reduced CTTN-binding; when associated with A-
FT 599."
FT /evidence="ECO:0000269|PubMed:22262902"
FT CONFLICT 521
FT /note="V -> F (in Ref. 1; AK028980)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="V -> F (in Ref. 1; AK028980)"
FT /evidence="ECO:0000305"
FT CONFLICT 1619
FT /note="S -> SSS (in Ref. 4; AAI41408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1648 AA; 178774 MW; 7C7016DB9E61D7E0 CRC64;
MATDSASCEP DLSRTPGDTE GATAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGPGDKEK PVCTNPLSIL EAVMAHCRKM
QERMSAQLVA AESRQKKLEM EKLQLQALEQ EHKKLAAHLE EERGKNKHVV LMLVKECKQL
SGKVVEEAQK LEEVMAQLEE EKKKTSELEE QLSAEKQRSS GMEAQLEKQL SEFDTEREQL
RAKLSREEAH TTDLKEEIDK MKKMMEQMKK GSDGKPGLSL PRKTKDKRLA SISVATEGPV
TRSVACQTDV VTESTDPVKK LPLTVPIKPS TGSPLVPTNT KGNVGPSALL IRPGIDRQSS
HSDLGPSPPT ALPSSANRIE ENGPSTGNAP DLSNSTPSTP SSTAPAAAQT PGTAPQNHSQ
APTVHSLHSP CANTHPGLNP RIQAARFRFQ GNANDPDQNG NNTQSPPSRD VSPTSRDNLV
AKQLARNTVT QALSRFTSPQ AGASSRLGVS PGGDAGTCPP VGRTGLKTPG AARVDRGNPP
PIPPKKPGLS QTPSPPHPQL RASNAGAKVD NKIVASPPST LPQGTKVVNE ENVPKSSSPQ
LPPKPSIDLT VAPAGCPVSA LATSQVGAWP AGTPGLNQPA CSDSSLVIPA TVAFCSSINP
VSASSRSPGA SDSLLVAASG WSPSLTPLLM SGGPAPLAGR PTLLQQAAAQ GNVTLLSMLL
NEEGLDINYS CEDGHSALYS AAKNGHTDCV RLLLNAEARV DAADKNGFTP LCVAAAQGHF
ECIELLTAYN ANINHSAAGG QTPLYLACKN GNKECIKLLL EAGTDRSIKT RDGWTPIHAA
VDTGNVDSLK LLMYHRVRAH GNSLSSEEPK SGLFSLNGGE SPTGPSKPVV PADLINHADK
EGWTAAHIAA SKGFKNCLEV LCRHGGLEPE RRDKCNRTVH DVATDDCKHL LENLNALKIP
LRISVGEIQP SNDVSDDFEC EHTICTLNIR KQTSWEDFSK AVSQALTNHF QAISSDGWWS
LEDGTFNNAT DSCIGLGTSS IRSIMLGSMP WSTGQSFSQS PWDFLKKKKV EQVLALLSGP
QEGCLSSVTY ASMIPLQMLQ NYLRLVEQYH NVIFHGPEGS LQDYIANQLA LCMKYRQMAA
GFPCEIVRAE VDSGFSKEQL VDVFIRNACL IPVKQFPVKK KIIVILENLE KSSLSELLGD
FLAPLENRST ESPCTFQKGN GTSECYYFHE NCFLVGTIAK ACLQGSDLLV QQHFRWVQLR
WDCEPIQGLL QRFLRRKVVS KFRGQLPAPC DPVCKIVDWA LSVWRQLNSC LARLGTPEAL
LGPKYFLSCP VVPGHAQATV KWMSKLWNAV IAPRVQEAIL SRASMNKQPG TGQTASKKYP
SQGQQAVVRA ALSILLNKAV LHGCPLPRAE LDQQIADFKG GSFPLSIVSS YSKKKVESGA
WRKVNTSPRK KPGHFSSPTW NKPDPKREGM RNKTIPHLNT NRNSSLSKQQ SLENDLSVTL
TLDHRLSLGS DDEADLVKEL QSMCSSKSES DISKIADSRD DLRKFDSSRT NPGTSAPLNL
RTPVPQKEAS PPSSRQTAEC SNSKSKTEMG VSSVKSFLPV PRSKVAQCSQ NTKRNSSSSN
TRQLEINNNS KEENWTLDKH EQVEKPNK
