KNDC1_MOUSE
ID KNDC1_MOUSE Reviewed; 1742 AA.
AC Q0KK55; Q0KK50; Q3TF27; Q3UGX9; Q3UGZ3; Q3UHK4; Q7TNH0; Q8BTH5; Q8BXJ3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Kinase non-catalytic C-lobe domain-containing protein 1 {ECO:0000312|MGI:MGI:1923734};
DE Short=KIND domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Protein very KIND {ECO:0000303|PubMed:16099729};
DE Short=v-KIND {ECO:0000303|PubMed:17984326};
DE AltName: Full=Ras-GEF domain-containing family member 2 {ECO:0000305};
GN Name=Kndc1 {ECO:0000312|MGI:MGI:1923734};
GN Synonyms=Kiaa1768, Rasgef2, Vkind {ECO:0000303|PubMed:17984326};
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16099729; DOI=10.1016/j.modgep.2005.04.015;
RA Mees A., Rock R., Ciccarelli F.D., Leberfinger C.B., Borawski J.M.,
RA Bork P., Wiese S., Gessler M., Kerkhoff E.;
RT "Very-KIND is a novel nervous system specific guanine nucleotide exchange
RT factor for Ras GTPases.";
RL Gene Expr. Patterns 6:79-85(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=BALB/cCrSlc; TISSUE=Brain;
RX PubMed=16807365; DOI=10.1096/fj.06-5952fje;
RA Nakayama M., Iida M., Koseki H., Ohara O.;
RT "A gene-targeting approach for functional characterization of KIAA genes
RT encoding extremely large proteins.";
RL FASEB J. 20:1718-1720(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, Cerebellum, Liver, and Medulla oblongata;
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 [4]
RP FUNCTION, INTERACTION WITH MAP2, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND TISSUE SPECIFICITY.
RX PubMed=17984326; DOI=10.1083/jcb.200702036;
RA Huang J., Furuya A., Furuichi T.;
RT "Very-KIND, a KIND domain containing RasGEF, controls dendrite growth by
RT linking Ras small GTPases and MAP2.";
RL J. Cell Biol. 179:539-552(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267 AND SER-951, AND
RP IDENTIFICATION 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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAP2, AND MUTAGENESIS OF
RP LEU-461; LEU-474; LEU-477; LEU-482 AND LEU-485.
RX PubMed=21385318; DOI=10.1111/j.1742-4658.2011.08085.x;
RA Huang J., Furuya A., Hayashi K., Furuichi T.;
RT "Interaction between very-KIND Ras guanine exchange factor and microtubule-
RT associated protein 2, and its role in dendrite growth -- structure and
RT function of the second kinase noncatalytic C-lobe domain.";
RL FEBS J. 278:1651-1661(2011).
CC -!- FUNCTION: RAS-Guanine nucleotide exchange factor (GEF) that controls
CC the negative regulation of neuronal dendrite growth by mediating a
CC signaling pathway linking RAS and MAP2 (PubMed:17984326,
CC PubMed:21385318). May be involved in cellular senescence (By
CC similarity). {ECO:0000250|UniProtKB:Q76NI1,
CC ECO:0000269|PubMed:17984326, ECO:0000269|PubMed:21385318}.
CC -!- SUBUNIT: Interacts (via KIND2) with MAP2; the interaction enhances MAP2
CC phosphorylation and localizes KNDC1 to dendrites.
CC {ECO:0000269|PubMed:17984326}.
CC -!- INTERACTION:
CC Q0KK55; P20357: Map2; NbExp=9; IntAct=EBI-8605532, EBI-397863;
CC -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000269|PubMed:17984326}. Perikaryon
CC {ECO:0000269|PubMed:17984326}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q0KK55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0KK55-2; Sequence=VSP_028600, VSP_028601;
CC Name=3;
CC IsoId=Q0KK55-3; Sequence=VSP_028599;
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and at low levels in
CC the ovary. In the brain it is most prominently expressed in the
CC cerebellum where it is restricted to the granular Purkinje cell layer.
CC {ECO:0000269|PubMed:16099729, ECO:0000269|PubMed:17984326}.
CC -!- DEVELOPMENTAL STAGE: At 14.5 dpc, highly expressed in the mid- and
CC hindbrain and only weakly in the forebrain, but during development the
CC main expression shifts towards the telencephalon as seen at 17.5 dpc
CC (PubMed:16099729). In cerebellum expression is highly up-regulated
CC between postnatal days P7 and P12. At P7, low expression levels
CC throughout the brain, but high in hippocampus, thalamus and the
CC cerebellar white matter (PubMed:17984326).
CC {ECO:0000269|PubMed:16099729, ECO:0000269|PubMed:17984326}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41157.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ580324; CAE30489.2; -; mRNA.
DR EMBL; AB257857; BAF03200.1; -; mRNA.
DR EMBL; AB257862; BAF03205.1; -; Genomic_DNA.
DR EMBL; AK046817; BAC32882.1; -; mRNA.
DR EMBL; AK090282; BAC41157.1; ALT_FRAME; mRNA.
DR EMBL; AK147335; BAE27853.1; -; mRNA.
DR EMBL; AK147672; BAE28064.1; -; mRNA.
DR EMBL; AK147693; BAE28078.1; -; mRNA.
DR EMBL; AK169316; BAE41071.1; -; mRNA.
DR RefSeq; NP_796235.4; NM_177261.4. [Q0KK55-1]
DR AlphaFoldDB; Q0KK55; -.
DR SMR; Q0KK55; -.
DR BioGRID; 218148; 3.
DR IntAct; Q0KK55; 1.
DR MINT; Q0KK55; -.
DR STRING; 10090.ENSMUSP00000050586; -.
DR iPTMnet; Q0KK55; -.
DR PhosphoSitePlus; Q0KK55; -.
DR CPTAC; non-CPTAC-4014; -.
DR MaxQB; Q0KK55; -.
DR PaxDb; Q0KK55; -.
DR PeptideAtlas; Q0KK55; -.
DR PRIDE; Q0KK55; -.
DR ProteomicsDB; 297602; -. [Q0KK55-1]
DR ProteomicsDB; 297603; -. [Q0KK55-2]
DR ProteomicsDB; 297604; -. [Q0KK55-3]
DR Antibodypedia; 48672; 62 antibodies from 12 providers.
DR DNASU; 76484; -.
DR Ensembl; ENSMUST00000053445; ENSMUSP00000050586; ENSMUSG00000066129. [Q0KK55-1]
DR GeneID; 76484; -.
DR KEGG; mmu:76484; -.
DR UCSC; uc009kgd.1; mouse. [Q0KK55-1]
DR CTD; 85442; -.
DR MGI; MGI:1923734; Kndc1.
DR VEuPathDB; HostDB:ENSMUSG00000066129; -.
DR eggNOG; ENOG502QSHW; Eukaryota.
DR GeneTree; ENSGT00390000011408; -.
DR HOGENOM; CLU_003380_0_0_1; -.
DR InParanoid; Q0KK55; -.
DR OMA; YWDEQLL; -.
DR OrthoDB; 78094at2759; -.
DR PhylomeDB; Q0KK55; -.
DR TreeFam; TF336009; -.
DR BioGRID-ORCS; 76484; 0 hits in 65 CRISPR screens.
DR PRO; PR:Q0KK55; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q0KK55; protein.
DR Bgee; ENSMUSG00000066129; Expressed in lateral geniculate body and 110 other tissues.
DR ExpressionAtlas; Q0KK55; baseline and differential.
DR Genevisible; Q0KK55; MM.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
DR GO; GO:0050773; P:regulation of dendrite development; IDA:MGI.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IDA:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011019; KIND_dom.
DR InterPro; IPR029899; KNDC1.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR21560; PTHR21560; 1.
DR Pfam; PF16474; KIND; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00750; KIND; 2.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51377; KIND; 2.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1742
FT /note="Kinase non-catalytic C-lobe domain-containing
FT protein 1"
FT /id="PRO_0000307142"
FT DOMAIN 37..217
FT /note="KIND 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 456..620
FT /note="KIND 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 1239..1367
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 1461..1712
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 215..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1112..1177
FT /evidence="ECO:0000255"
FT COMPBIAS 399..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..1126
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028599"
FT VAR_SEQ 538..572
FT /note="ASVYCVAAVLWTAAKFSVPRDHKLALPRRLKTLLL -> VTSHITSLAPSSP
FT SAQWIAGPDGLNVAPILLAGLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028600"
FT VAR_SEQ 573..1742
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028601"
FT MUTAGEN 461
FT /note="L->A: Abolishes interaction with MAP2."
FT /evidence="ECO:0000269|PubMed:21385318"
FT MUTAGEN 474
FT /note="L->A: Abolishes interaction with MAP2."
FT /evidence="ECO:0000269|PubMed:21385318"
FT MUTAGEN 477
FT /note="L->A: Abolishes interaction with MAP2."
FT /evidence="ECO:0000269|PubMed:21385318"
FT MUTAGEN 482
FT /note="L->A: No effect on interaction with MAP2."
FT /evidence="ECO:0000269|PubMed:21385318"
FT MUTAGEN 485
FT /note="L->A: No effect on interaction with MAP2."
FT /evidence="ECO:0000269|PubMed:21385318"
FT CONFLICT 20
FT /note="D -> G (in Ref. 1; CAE30489)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="L -> V (in Ref. 3; BAC41157)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="R -> E (in Ref. 2; BAF03200)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="D -> G (in Ref. 2; BAF03200)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="R -> Q (in Ref. 2; BAF03205)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="S -> L (in Ref. 2; BAF03200)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="G -> C (in Ref. 3; BAE27853)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="I -> T (in Ref. 3; BAE28078)"
FT /evidence="ECO:0000305"
FT CONFLICT 780
FT /note="A -> V (in Ref. 2; BAF03200)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="G -> D (in Ref. 2; BAF03200)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="K -> R (in Ref. 1; CAE30489)"
FT /evidence="ECO:0000305"
FT CONFLICT 845
FT /note="R -> G (in Ref. 3; BAE28064)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="S -> N (in Ref. 1; CAE30489)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109
FT /note="T -> A (in Ref. 1; CAE30489 and 2; BAF03200)"
FT /evidence="ECO:0000305"
FT CONFLICT 1209
FT /note="C -> F (in Ref. 1; CAE30489)"
FT /evidence="ECO:0000305"
FT CONFLICT 1306
FT /note="T -> A (in Ref. 1; CAE30489)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1742 AA; 191313 MW; 2C54217F515FA984 CRC64;
MQAMDPASRG FYEEDGKDLD FYDFEPLPTL PEDEENVSLA DILSLRDRGL SEQEAWAVCL
ECSLSMRSVA HAAIFQTLCI TPDTLAFNTS GNVCFMEQLS DDPEGAFVPP EFDLTGNTFE
AHIYSLGATL KAALEYVPEP ELEPKLSTDL EGLLSQMQAE DPRERPDLAS IIALCEEKMQ
PVSSCRLCRS LSAIGRRVLS IESFGAFQEL SENTWRGRPA PRNVGPKKMP GDLSTDPEAL
FPSKGLLQPP ASRDAEQEAG QRPRAPSPKP LLSAPVRNGE NPGQEGLADL VLDARCPLGE
LDRDNLRRSR LKKAQTFPRL LQESTETSTL CLSLNGSRNQ LAISEFFPPD PRKLFLEGKN
GLSGFKTQSK SRLWPEQEPG VQLDKTPGAG RNPHRSPGAS GQLEASSPSQ GSVEYKPSPS
PVDAGDSDHE GHIPRSEEKI PEESRQPGST ATEQSLSLKD LLSKLGRPFR EYELWALCLS
CLSTLQTHKE HPAHLCLDNV LVAEDGTVFF GPPPANGAYN SLFLAPEVSE EKLVTEKASV
YCVAAVLWTA AKFSVPRDHK LALPRRLKTL LLDMARRHAS ERPSAAEAIK VCSSYLLQRG
MDSSKILAHL RASTCKVHPE EETIGLQNAF SVVELKSTTA PAPESSPGFL QVSNDTKLVA
VPGPVPGLPP CCKEACELPA AFTSEATHFK PIVLAQDASV TRDQLALPSE SNEKPKEGSG
HLDREGTRKQ AALELVEATD LKMSNQLSPG PELQGATPDP DGDSGSPSSA TECSCPHGPA
LVTQQKGTSG TPSSPASSLP PEHRPDGEGP LGTTVLPGPT SASQGSRHPC KPPRGKAAAS
PSSPRGSDGH PEKPRPADRK LCPSSVDTSS PPKMTACPSL QEAMRLIQEE FAFDGYMDNG
LEALIMGEYI YALKDLTFAT FCGAISEKFC DLYWDEQLLK NLFKVVNGPA SPSESTSEEP
GSQPEHSPSR CSLSSKRPSL HGLGKEKPAT TWGSGGPCSP TALSDIDSDT LSQGNFEVGF
RSQKSIKVTR EQQPEAEVGG QPGPSQDSTS HASDTVARLA RSEDGGPAGS PGASDFQNCS
PGWSSAFYEA DCFGADVYNY VKDLERQKTN GHTELEAQSP ELEQQLMIEK RNYRKTLKFY
QKLLQKEKRN KGSEVRTMLS KLRGQLDEMK SKVQFLSLVK KYLQVMYAER WGLEPCALPV
IVNIAAAPCD TLDFSPLDES SSLIFYNVNK HPGSGRQKKA RILQAGTPLG LMAYLYSSDA
FLEGYVQQFL YTFRYFCTPH DFLHFLLDRI SSTLSRAHQD PTSTFTKIYR RSLCVLQAWV
EDCYTVDFIR NAGLLGQLED FISSKILPLD GTAEHLLALL EVGTERRADS ASRGADLEDP
KEAEEDTRPF NALCKRFSED GITRKSFSWR LPRGNGLVLP HHKERQYTIA SALPKPCFFE
DFYGPYAKAS EKGPYFLTEY STNQLFTQLT LLQQELFQKC HPVHFLNSRA LGVMDKSAAI
PKASSSESLS AKTCSLFLPN YVQDKYLLQL LRNADDVSTW VAAEIVTSHT SKLQVNLLSK
FLLIAKSCYE QRNFATAMQI LGGLEHLAVR QSPAWRILPA KIAEVMEELK AVEVFLKSDS
LCLMEGRRFR AQPTLPSAHL LAMHIQQLET GGFTMTNGAH RWSKLRNIAK VASQVHAFQE
NPYTFSPDPK LQAHLKQRIA RFSGADVSIL AADNRANFHQ IPGEKHSRKI QDKLRRMKAT
FQ
