CSKI1_MOUSE
ID CSKI1_MOUSE Reviewed; 1431 AA.
AC Q6P9K8; Q6ZPU2; Q8BWU2; Q8BX99; Q9CXH0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Caskin-1;
DE AltName: Full=CASK-interacting protein 1;
GN Name=Caskin1; Synonyms=Kiaa1306;
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 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 667-1431 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Head, and Hippocampus;
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] OF 14-1431 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-1431 (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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1259 AND SER-1363, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND IDENTIFICATION BY
RP 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-358; SER-423; SER-432;
RP SER-637; SER-650; SER-728; SER-989; THR-1067; SER-1069; SER-1259; THR-1268
RP AND SER-1363, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, 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).
CC -!- FUNCTION: May link the scaffolding protein CASK to downstream
CC intracellular effectors. {ECO:0000250}.
CC -!- SUBUNIT: Binds the CaM kinase domain of CASK. Forms a ternary complex
CC with CASK and LIN7A, LIN7B or LIN7C. Competes with APBA1 that forms a
CC similar complex with CASK and LIN7 proteins. The tripartite complex
CC CASKIN1/CASK/LIN7(A/B/C) binds the cytoplasmic tail of NRXN1.
CC Polymerizes, via the tandem SAM domains, to form long, 8 nM wide
CC fibers, upon which other proteins can assemble (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6P9K8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P9K8-2; Sequence=VSP_013123;
CC Name=3;
CC IsoId=Q6P9K8-3; Sequence=VSP_013124;
CC Name=4;
CC IsoId=Q6P9K8-4; Sequence=VSP_013121, VSP_013122;
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DR EMBL; AK014376; BAB29308.1; -; mRNA.
DR EMBL; AK048449; BAC33340.1; -; mRNA.
DR EMBL; AK049987; BAC34019.1; -; mRNA.
DR EMBL; AK129327; BAC98137.1; -; mRNA.
DR EMBL; BC060720; AAH60720.1; -; mRNA.
DR CCDS; CCDS50013.1; -. [Q6P9K8-1]
DR CCDS; CCDS89007.1; -. [Q6P9K8-2]
DR RefSeq; NP_082213.2; NM_027937.2. [Q6P9K8-1]
DR RefSeq; XP_006524378.1; XM_006524315.3.
DR AlphaFoldDB; Q6P9K8; -.
DR SMR; Q6P9K8; -.
DR BioGRID; 234580; 14.
DR IntAct; Q6P9K8; 8.
DR MINT; Q6P9K8; -.
DR STRING; 10090.ENSMUSP00000024958; -.
DR iPTMnet; Q6P9K8; -.
DR PhosphoSitePlus; Q6P9K8; -.
DR MaxQB; Q6P9K8; -.
DR PaxDb; Q6P9K8; -.
DR PeptideAtlas; Q6P9K8; -.
DR PRIDE; Q6P9K8; -.
DR ProteomicsDB; 285318; -. [Q6P9K8-1]
DR ProteomicsDB; 285319; -. [Q6P9K8-2]
DR ProteomicsDB; 285320; -. [Q6P9K8-3]
DR ProteomicsDB; 285321; -. [Q6P9K8-4]
DR Antibodypedia; 61351; 26 antibodies from 15 providers.
DR DNASU; 268932; -.
DR Ensembl; ENSMUST00000024958; ENSMUSP00000024958; ENSMUSG00000033597. [Q6P9K8-1]
DR Ensembl; ENSMUST00000234717; ENSMUSP00000157196; ENSMUSG00000033597. [Q6P9K8-2]
DR GeneID; 268932; -.
DR KEGG; mmu:268932; -.
DR UCSC; uc008awm.1; mouse. [Q6P9K8-4]
DR UCSC; uc008awo.1; mouse. [Q6P9K8-2]
DR UCSC; uc008awp.2; mouse. [Q6P9K8-1]
DR CTD; 57524; -.
DR MGI; MGI:2442952; Caskin1.
DR VEuPathDB; HostDB:ENSMUSG00000033597; -.
DR eggNOG; KOG0507; Eukaryota.
DR GeneTree; ENSGT00940000158025; -.
DR HOGENOM; CLU_003619_1_1_1; -.
DR InParanoid; Q6P9K8; -.
DR OMA; KPPNHLP; -.
DR OrthoDB; 75723at2759; -.
DR PhylomeDB; Q6P9K8; -.
DR TreeFam; TF320582; -.
DR BioGRID-ORCS; 268932; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Caskin1; mouse.
DR PRO; PR:Q6P9K8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6P9K8; protein.
DR Bgee; ENSMUSG00000033597; Expressed in lumbar subsegment of spinal cord and 114 other tissues.
DR Genevisible; Q6P9K8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR CDD; cd09497; SAM_caskin1_2_repeat1; 1.
DR CDD; cd09498; SAM_caskin1_2_repeat2; 1.
DR CDD; cd12062; SH3_Caskin1; 1.
DR Gene3D; 1.10.150.50; -; 2.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR027013; Caskin-1/2.
DR InterPro; IPR032232; Caskin1-CID.
DR InterPro; IPR035497; Caskin1/2_SAM_1.
DR InterPro; IPR035498; Caskin1/2_SAM_2.
DR InterPro; IPR035495; Caskin1_SH3.
DR InterPro; IPR032117; Caskin_C.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR24174:SF11; PTHR24174:SF11; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF16632; Caskin-tail; 1.
DR Pfam; PF16600; Caskin1-CID; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00454; SAM; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47769; SSF47769; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1431
FT /note="Caskin-1"
FT /id="PRO_0000066981"
FT REPEAT 48..77
FT /note="ANK 1"
FT REPEAT 81..110
FT /note="ANK 2"
FT REPEAT 114..143
FT /note="ANK 3"
FT REPEAT 147..176
FT /note="ANK 4"
FT REPEAT 188..217
FT /note="ANK 5"
FT REPEAT 220..249
FT /note="ANK 6"
FT DOMAIN 281..347
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 476..539
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 545..609
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 348..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..471
FT /note="CASK-binding"
FT /evidence="ECO:0000250"
FT REGION 420..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..864
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1233
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1285
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 398
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXD9"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHK2"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 741
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHK2"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXD9"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHK2"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHK2"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1067
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1268
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 351..365
FT /note="SRTGSEPSPPQGGGS -> KSTPLWREASRGHSA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013121"
FT VAR_SEQ 366..1431
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013122"
FT VAR_SEQ 477..547
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_013123"
FT VAR_SEQ 1284..1342
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013124"
FT CONFLICT 274
FT /note="K -> E (in Ref. 1; BAB29308)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="A -> S (in Ref. 1; BAC34019)"
FT /evidence="ECO:0000305"
FT CONFLICT 1235
FT /note="S -> A (in Ref. 3; BAC98137)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1431 AA; 150495 MW; F89BFB1B2B8926EF CRC64;
MGKEQELVQA VKAEDVGTAQ RLLQRPRPGK AKLLGSTKKI NVNFQDPDGF SALHHAALNG
NTELISLLLE AQAAVDIKDN KGMRPLHYAA WQGRKEPMKL VLKAGSAVNV PSDEGHIPLH
LAAQHGHYDV SEMLLQHQSN PCMVDNSGKT PLDLACEFGR VGVVQLLLSS NMCAALLEPR
PGDTTDPNGT SPLHLAAKNG HIDIIRLLLQ AGIDINRQTK SGTALHEAAL CGKTEVVRLL
LDSGINAQVR NTYSQTALDI VHQFTTSQAS KEIKQLLREA SAALQVRATK DYCNNYDLTS
LNVKAGDIIT VLEQHPDGRW KGCIHDNRTG NDRVGYFPSS LGEAIVKRAG SRTGSEPSPP
QGGGSLGPSA PPEEIWVLRK PFAGGDRSGS LSNVAGGRST GGHALHAGSE GVKLLATVLS
QKSVSESSPG DSPVKPPEGS SGAARSQPPA AHAGQVYGEQ PPKKLESASA SASEGKSAEA
VSQWLATFQL QLYAPNFTSA GYDLPTISRM TPEDLTAIGV TKPGHRKKIT AEISGLNIPD
WLPEHKPANL AVWLSMIGLA QYYKVLVDNG YENIDFITDI TWEDLQEIGI TKLGHQKKLM
LAVRKLAELQ KAEYSKYEGG PLRRKTPQSL EMMAIESPPP SEPAAAECQS PKMTTFQDSE
LSGELQAALS GPAEAGAAAV EKSSNHLPPT PRTTSRESSL SGRARHISSS QELLGDGPPG
PGSPMSRSQE YLLDEGMAPG TPPKEVRSSR HGHSVKRASV PPVPGKPRQV LPSGASHFTP
PQTPTKAQPG SPQALGGPHG PATAKVKPTP QLLPPTDRPM SPRSLPQSPT HRGFAYVLPQ
PVEGEVGPPA PGPAPPPVPA AVPTLCLPPE TDVEPGRPKK RAHSLNRYAA SDSEPERDEL
LVPAAAGPYA TVQRRVGRSH SVRAPAGTDK NVNRSQSFAV RPRKKGPPPP PPKRSSSAMA
SANLADEPAP DVEAEDGRLG VRAQRRRASD LAGSVDTGSA GSVKSIAAML ELSSIGGGGR
AIRRPPEGHP TPRPASPEPG RVATVLASVK HKEAIGPDGE VVNRRRTLSG PVTGLLATAR
RGSGEPAEQS HFMEDGTARQ RLRGPAKGEA SAEGPPLARV EASATLKRRI RAKQSQQENV
KFILTESDTV KRRPKAKEPD TGPEPPPPLS VYQNGTATVR RRPTSEQAGP PELPPPPPPA
EPPPADLMQL PPLPLPDGNA RKPVKPPVSP KPILSQPVSK IQGSPTPASK KVPLPGPGSP
EVKRAHGTPP PVSPKPPPPP TAPKPAKALA GLQSSSATPS PVPSPARQPP AALIKPASSP
PSQSASPVKP PSPGTPALHV PAKPPRAAAS VVSGPPVASD CASPGDSARQ KLEETSACLA
AALQAVEEKI RQEDGQGPRP SSIEEKSTGS ILEDIGSMFD DLADQLDAML E
