ARVC_MOUSE
ID ARVC_MOUSE Reviewed; 962 AA.
AC P98203; Q6PGJ6; Q8BQ36; Q8BRF2; Q8C3U7; Q924L2; Q924L3; Q924L4; Q924L5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Splicing regulator ARVCF {ECO:0000305};
DE AltName: Full=Armadillo repeat protein deleted in velo-cardio-facial syndrome homolog;
GN Name=Arvcf;
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; 4 AND 5).
RC STRAIN=C57BL/6J;
RA Saint-Jore B., Puech A., Merscher S., Xu H., Kucherlapati R., Skoultchi A.;
RT "Developmental expression analysis of Arvcf, a candidate gene for velo-
RT cardio-facial syndrome.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Embryonic ganglion, and Embryonic lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 8-927 (ISOFORM 2).
RX PubMed=11058098; DOI=10.1242/jcs.113.22.4121;
RA Kaufmann U., Zuppinger C., Waibler Z., Rudiger M., Urbich C., Martin B.,
RA Jockusch B.M., Eppenberger H., Starzinski-Powitz A.;
RT "The armadillo repeat region targets ARVCF to cadherin-based cellular
RT junctions.";
RL J. Cell Sci. 113:4121-4135(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; SER-334; SER-337 AND
RP THR-643, 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 [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-171, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Contributes to the regulation of alternative splicing of pre-
CC mRNAs. {ECO:0000250|UniProtKB:O00192}.
CC -!- SUBUNIT: Component of a ribonucleoprotein complex containing mRNAs and
CC RNA-binding proteins including DDX5, HNRNPH2 and SRSF1 as well as ARVCF
CC (By similarity). Interacts (via the extreme C-terminus) with FRMPD2
CC (via the PDZ 2 domain). Interacts with CCDC85B (By similarity).
CC {ECO:0000250|UniProtKB:O00192}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:O00192}. Nucleus {ECO:0000250|UniProtKB:O00192}.
CC Cytoplasm {ECO:0000250|UniProtKB:O00192}. Note=In heart, localizes at
CC area composita, the mixed-type junctional structure composed of both
CC desmosomal and adherens junctional proteins.
CC {ECO:0000250|UniProtKB:B4F7F3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A1;
CC IsoId=P98203-1; Sequence=Displayed;
CC Name=2; Synonyms=A2;
CC IsoId=P98203-2; Sequence=VSP_014923;
CC Name=4; Synonyms=B2;
CC IsoId=P98203-4; Sequence=VSP_014922, VSP_014923;
CC Name=5; Synonyms=B1;
CC IsoId=P98203-5; Sequence=VSP_014922;
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AJ243418; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AF286212; AAK64214.1; -; mRNA.
DR EMBL; AF286213; AAK64215.1; -; mRNA.
DR EMBL; AF286214; AAK64216.1; -; mRNA.
DR EMBL; AF286215; AAK64217.1; -; mRNA.
DR EMBL; AK044982; BAC32169.1; -; mRNA.
DR EMBL; AK051627; BAC34696.1; -; mRNA.
DR EMBL; AK084886; BAC39302.1; -; mRNA.
DR EMBL; BC056980; AAH56980.1; -; mRNA.
DR EMBL; AJ243418; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS28020.1; -. [P98203-1]
DR CCDS; CCDS70693.1; -. [P98203-2]
DR CCDS; CCDS70694.1; -. [P98203-4]
DR CCDS; CCDS88894.1; -. [P98203-5]
DR RefSeq; NP_001258957.1; NM_001272028.1. [P98203-1]
DR RefSeq; NP_001258958.1; NM_001272029.1. [P98203-2]
DR RefSeq; NP_001258959.1; NM_001272030.1. [P98203-2]
DR RefSeq; NP_001258960.1; NM_001272031.1. [P98203-5]
DR RefSeq; NP_001258961.1; NM_001272032.1. [P98203-4]
DR RefSeq; NP_258435.2; NM_033474.3. [P98203-1]
DR AlphaFoldDB; P98203; -.
DR SMR; P98203; -.
DR BioGRID; 198214; 8.
DR IntAct; P98203; 3.
DR MINT; P98203; -.
DR STRING; 10090.ENSMUSP00000111276; -.
DR iPTMnet; P98203; -.
DR PhosphoSitePlus; P98203; -.
DR SwissPalm; P98203; -.
DR MaxQB; P98203; -.
DR PaxDb; P98203; -.
DR PeptideAtlas; P98203; -.
DR PRIDE; P98203; -.
DR ProteomicsDB; 265108; -. [P98203-1]
DR ProteomicsDB; 265109; -. [P98203-2]
DR ProteomicsDB; 265110; -. [P98203-4]
DR ProteomicsDB; 265111; -. [P98203-5]
DR Antibodypedia; 4255; 92 antibodies from 23 providers.
DR DNASU; 11877; -.
DR Ensembl; ENSMUST00000239533; ENSMUSP00000159425; ENSMUSG00000118669. [P98203-2]
DR Ensembl; ENSMUST00000239534; ENSMUSP00000159426; ENSMUSG00000118669. [P98203-1]
DR Ensembl; ENSMUST00000239535; ENSMUSP00000159427; ENSMUSG00000118669. [P98203-1]
DR Ensembl; ENSMUST00000239536; ENSMUSP00000159428; ENSMUSG00000118669. [P98203-2]
DR Ensembl; ENSMUST00000239538; ENSMUSP00000159429; ENSMUSG00000118669. [P98203-4]
DR Ensembl; ENSMUST00000239547; ENSMUSP00000159437; ENSMUSG00000118669. [P98203-4]
DR Ensembl; ENSMUST00000239548; ENSMUSP00000159438; ENSMUSG00000118669. [P98203-5]
DR GeneID; 11877; -.
DR KEGG; mmu:11877; -.
DR UCSC; uc007ynl.2; mouse. [P98203-1]
DR UCSC; uc007ynm.2; mouse. [P98203-2]
DR UCSC; uc007ynq.2; mouse. [P98203-5]
DR UCSC; uc007yns.2; mouse. [P98203-4]
DR CTD; 421; -.
DR MGI; MGI:109620; Arvcf.
DR VEuPathDB; HostDB:ENSMUSG00000000325; -.
DR eggNOG; KOG1048; Eukaryota.
DR GeneTree; ENSGT00940000157027; -.
DR HOGENOM; CLU_009111_1_0_1; -.
DR InParanoid; P98203; -.
DR OMA; CGQPLPM; -.
DR OrthoDB; 233858at2759; -.
DR PhylomeDB; P98203; -.
DR TreeFam; TF321877; -.
DR BioGRID-ORCS; 11877; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Arvcf; mouse.
DR PRO; PR:P98203; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P98203; protein.
DR ExpressionAtlas; P98203; baseline and differential.
DR Genevisible; P98203; MM.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045296; F:cadherin binding; ISS:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR028444; ARVCF.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR PANTHER; PTHR10372:SF5; PTHR10372:SF5; 1.
DR Pfam; PF00514; Arm; 4.
DR SMART; SM00185; ARM; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Coiled coil; Cytoplasm;
KW Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..962
FT /note="Splicing regulator ARVCF"
FT /id="PRO_0000064295"
FT REPEAT 350..389
FT /note="ARM 1"
FT REPEAT 392..431
FT /note="ARM 2"
FT REPEAT 435..469
FT /note="ARM 3"
FT REPEAT 470..510
FT /note="ARM 4"
FT REPEAT 528..567
FT /note="ARM 5"
FT REPEAT 577..623
FT /note="ARM 6"
FT REPEAT 647..687
FT /note="ARM 7"
FT REPEAT 700..739
FT /note="ARM 8"
FT REPEAT 740..782
FT /note="ARM 9"
FT REPEAT 783..827
FT /note="ARM 10"
FT REGION 95..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..962
FT /note="Required for interaction with RNA-binding proteins
FT DDX5, HNRNPH2 and SRSF1 and with mRNAs"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT REGION 844..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 11..46
FT /evidence="ECO:0000255"
FT MOTIF 608..624
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 99..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 105
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 171
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 643
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 872
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT VAR_SEQ 1..70
FT /note="MEDCNVHSAASILASVKEQEARFERLTRALEQERRHVALQLERAQQPGMSSG
FT GMVGSGQPLPMAWQQLVL -> MPAELR (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_014922"
FT VAR_SEQ 625..630
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11058098,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_014923"
FT CONFLICT 72
FT /note="E -> G (in Ref. 3; AAH56980)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="P -> T (in Ref. 2; BAC39302)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="R -> L (in Ref. 1; AAK64214/AAK64215/AAK64216/
FT AAK64217)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="V -> E (in Ref. 2; BAC39302)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="N -> K (in Ref. 2; BAC39302)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 962 AA; 105066 MW; 8F43E9DC34709406 CRC64;
MEDCNVHSAA SILASVKEQE ARFERLTRAL EQERRHVALQ LERAQQPGMS SGGMVGSGQP
LPMAWQQLVL QEQSPGSQAS LATMPEAPEV LEETVTVEED PGTPTSHVSI VTSEDGTTRR
TETKVTKTVK TVTTRTVRQV PLGPDGLPLL DGGPPLGSFA DGPLDRHYLL RGGGGPAATL
SRTYHSSGGG FPDGPESRDI PSYGSLSRGL GVRPPRTGLL GPGPGDGCFT LPGRREAFPM
GSESGPPSGR SLPEHFQAEP YGLEDDTRSL AADDEGGPDL EPDYSTATRR RPEYGRGLRA
RAFEDTADDA GELIEERPPF PAATAPLAQP ERGSLGSLDR VVRRSPSVDS TRKEPRWRDP
ELPEVLAMLR HPVDPVKANA AAYLQHLCFE NEGIKRRVRQ LRGLPLLVAL LDHPRAEVRR
RACGALRNLS YGRDTDNKAA IRDCGGVPAL VRLLRAARDN EVRELVTGTL WNLSSYEPLK
MVIIDHGLQT LTHEVIVPHS GWEREPNEDS KPRDAEWTTV FKNTSGCLRN VSSDGAEARR
RLRECEGLVD ALLHALQSAV GRKDTDNKSV ENCVCIMRNL SYHVHKEVPG ADRYQEAEPG
IPGSTTSQRR RKDDASCFGG KKAKEEWFHQ GKKDAEMDRN FDTLDLPKRT EAAKGFELLY
QPEVVRLYLS LLTESRNFNT LEAAAGALQN LSAGNWTWAT YIRATVRKER GLPVLVELLQ
SETDKVVRAV AIALRNLSLD QRNKDLIGSY AMTELVRNVR NAQAPAHPSA HLEEDTVVAV
LNTIHEIVSD SLDNARSLLQ ARGVPALVAL VASSQSVREA KAASHVLQTV WSYKELRGAL
QRDGWTKSRF QSASTAKGPK GTPSSGGFDD STLPLVDKSL DGEKSNTRDV IPMDTLGPDG
YATVDRRERR TLGSDSTGDT SEKELLRPDP GRKAPPPGPS RPSVRLVDAV GDTKPQPVDS
WV
