RCAN1_HUMAN
ID RCAN1_HUMAN Reviewed; 252 AA.
AC P53805; D3DSF9; O00582; O00583; Q53XT0; Q6IBC6; Q7Z555; Q96R03; Q9BU69;
AC Q9UF15; Q9UME4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 4.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Calcipressin-1;
DE AltName: Full=Adapt78;
DE AltName: Full=Down syndrome critical region protein 1;
DE AltName: Full=Myocyte-enriched calcineurin-interacting protein 1;
DE Short=MCIP1;
DE AltName: Full=Regulator of calcineurin 1;
GN Name=RCAN1; Synonyms=ADAPT78, CSP1, DSC1, DSCR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RX PubMed=8595418; DOI=10.1093/hmg/4.10.1935;
RA Fuentes J.-J., Pritchard M.A., Planas A.M., Bosch A., Ferrer I.,
RA Estivill X.;
RT "A new human gene from the Down syndrome critical region encodes a proline-
RT rich protein highly expressed in fetal brain and heart.";
RL Hum. Mol. Genet. 4:1935-1944(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 48-252 (ISOFORM 1), AND ALTERNATIVE SPLICING.
RX PubMed=9325060; DOI=10.1006/geno.1997.4866;
RA Fuentes J.-J., Pritchard M.A., Estivill X.;
RT "Genomic organization, alternative splicing, and expression patterns of the
RT DSCR1 (Down syndrome candidate region 1) gene.";
RL Genomics 44:358-361(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH PPP3CA
RP AND PPP3R1, PHOSPHORYLATION AT SER-163 AND SER-167, AND MUTAGENESIS OF
RP SER-163 AND SER-167.
RC TISSUE=Heart;
RX PubMed=12809556; DOI=10.1042/bj20030267;
RA Genesca L., Aubareda A., Fuentes J.J., Estivill X., De La Luna S.,
RA Perez-Riba M.;
RT "Phosphorylation of calcipressin 1 increases its ability to inhibit
RT calcineurin and decreases calcipressin half-life.";
RL Biochem. J. 374:567-575(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Hua F., Wu J., Zhou Y., Zhang B., Peng X., Qiang B., Yuan J., Qiang B.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-219 (ISOFORM 2).
RC TISSUE=Mammary gland;
RA Crawford D.R., Leahy K.P., Davies K.J.A.;
RT "Adapt78, a calcium and oxidant-inducible RNA.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-252 (ISOFORM 1).
RC TISSUE=Lung;
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-252 (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP CHARACTERIZATION.
RX PubMed=10861295; DOI=10.1093/hmg/9.11.1681;
RA Fuentes J.J., Genesca L., Kingsbury T.J., Cunningham K.W., Perez-Riba M.,
RA Estivill X., de la Luna S.;
RT "DSCR1, overexpressed in Down syndrome, is an inhibitor of calcineurin-
RT mediated signaling pathways.";
RL Hum. Mol. Genet. 9:1681-1690(2000).
RN [13]
RP INTERACTION WITH RAF1.
RX PubMed=15935327; DOI=10.1016/j.abb.2005.05.002;
RA Cho Y.J., Abe M., Kim S.Y., Sato Y.;
RT "Raf-1 is a binding partner of DSCR1.";
RL Arch. Biochem. Biophys. 439:121-128(2005).
CC -!- FUNCTION: Inhibits calcineurin-dependent transcriptional responses by
CC binding to the catalytic domain of calcineurin A (PubMed:12809556).
CC Could play a role during central nervous system development (By
CC similarity). {ECO:0000250|UniProtKB:Q9JHG6,
CC ECO:0000269|PubMed:12809556}.
CC -!- SUBUNIT: Interacts with RAF1 (PubMed:15935327). Interacts with PPP3CA
CC and PPP3R1 (PubMed:12809556). {ECO:0000269|PubMed:12809556,
CC ECO:0000269|PubMed:15935327}.
CC -!- INTERACTION:
CC P53805-2; P04049: RAF1; NbExp=4; IntAct=EBI-1541912, EBI-365996;
CC P53805-2; P53805-2: RCAN1; NbExp=6; IntAct=EBI-1541912, EBI-1541912;
CC P53805-2; Q61214: Dyrk1a; Xeno; NbExp=5; IntAct=EBI-1541912, EBI-80344;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=CALP1-L {ECO:0000303|PubMed:12809556};
CC IsoId=P53805-1; Sequence=Displayed;
CC Name=2; Synonyms=CALP1-S {ECO:0000303|PubMed:12809556};
CC IsoId=P53805-2; Sequence=VSP_001314;
CC Name=3;
CC IsoId=P53805-3; Sequence=VSP_001315;
CC Name=4;
CC IsoId=P53805-4; Sequence=VSP_001316;
CC -!- TISSUE SPECIFICITY: Highly expressed heart, brain and skeletal muscle.
CC Also expressed in all other tissues.
CC -!- INDUCTION: By calcium.
CC -!- PTM: Phosphorylation increases its ability to inhibit calcineurin and
CC decreases protein half-life. {ECO:0000269|PubMed:12809556}.
CC -!- SIMILARITY: Belongs to the RCAN family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U28833; AAB81557.1; -; mRNA.
DR EMBL; U85265; AAB84370.1; -; mRNA.
DR EMBL; U85266; AAB84371.2; -; mRNA.
DR EMBL; U85267; AAB84372.1; -; mRNA.
DR EMBL; AY325903; AAP96743.1; -; mRNA.
DR EMBL; AF400429; AAK92478.1; -; mRNA.
DR EMBL; AK092184; BAG52494.1; -; mRNA.
DR EMBL; CR456878; CAG33159.1; -; mRNA.
DR EMBL; AP000326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09779.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09782.1; -; Genomic_DNA.
DR EMBL; U53821; AAF21218.1; -; Genomic_DNA.
DR EMBL; BC002864; AAH02864.1; -; mRNA.
DR EMBL; BT007363; AAP36027.1; -; mRNA.
DR CCDS; CCDS13637.1; -. [P53805-1]
DR CCDS; CCDS33551.1; -. [P53805-2]
DR CCDS; CCDS42921.1; -. [P53805-4]
DR CCDS; CCDS74790.1; -. [P53805-3]
DR RefSeq; NP_001272318.1; NM_001285389.2. [P53805-3]
DR RefSeq; NP_001272320.2; NM_001285391.2.
DR RefSeq; NP_001272321.1; NM_001285392.2. [P53805-4]
DR RefSeq; NP_001272322.1; NM_001285393.2. [P53805-4]
DR RefSeq; NP_004405.3; NM_004414.6. [P53805-1]
DR RefSeq; NP_981962.1; NM_203417.2. [P53805-4]
DR RefSeq; NP_981963.1; NM_203418.2. [P53805-2]
DR PDB; 6UUQ; X-ray; 1.85 A; B=183-219.
DR PDBsum; 6UUQ; -.
DR AlphaFoldDB; P53805; -.
DR SMR; P53805; -.
DR BioGRID; 108161; 34.
DR CORUM; P53805; -.
DR IntAct; P53805; 21.
DR MINT; P53805; -.
DR STRING; 9606.ENSP00000370527; -.
DR DrugBank; DB00975; Dipyridamole.
DR iPTMnet; P53805; -.
DR PhosphoSitePlus; P53805; -.
DR BioMuta; RCAN1; -.
DR DMDM; 215274235; -.
DR EPD; P53805; -.
DR jPOST; P53805; -.
DR MassIVE; P53805; -.
DR MaxQB; P53805; -.
DR PaxDb; P53805; -.
DR PeptideAtlas; P53805; -.
DR PRIDE; P53805; -.
DR ProteomicsDB; 56626; -. [P53805-1]
DR ProteomicsDB; 56627; -. [P53805-2]
DR ProteomicsDB; 56628; -. [P53805-3]
DR ProteomicsDB; 56629; -. [P53805-4]
DR Antibodypedia; 22959; 580 antibodies from 35 providers.
DR DNASU; 1827; -.
DR Ensembl; ENST00000313806.9; ENSP00000320768.4; ENSG00000159200.18. [P53805-1]
DR Ensembl; ENST00000381132.6; ENSP00000370524.2; ENSG00000159200.18. [P53805-2]
DR Ensembl; ENST00000399272.5; ENSP00000382214.1; ENSG00000159200.18. [P53805-3]
DR Ensembl; ENST00000443408.6; ENSP00000392438.2; ENSG00000159200.18. [P53805-4]
DR Ensembl; ENST00000482533.5; ENSP00000419624.1; ENSG00000159200.18. [P53805-4]
DR Ensembl; ENST00000487990.5; ENSP00000419252.1; ENSG00000159200.18. [P53805-4]
DR Ensembl; ENST00000620920.4; ENSP00000477646.1; ENSG00000159200.18. [P53805-4]
DR GeneID; 1827; -.
DR KEGG; hsa:1827; -.
DR MANE-Select; ENST00000313806.9; ENSP00000320768.4; NM_004414.7; NP_004405.3.
DR UCSC; uc002yuc.5; human. [P53805-1]
DR CTD; 1827; -.
DR DisGeNET; 1827; -.
DR GeneCards; RCAN1; -.
DR HGNC; HGNC:3040; RCAN1.
DR HPA; ENSG00000159200; Tissue enhanced (parathyroid).
DR MIM; 602917; gene.
DR neXtProt; NX_P53805; -.
DR OpenTargets; ENSG00000159200; -.
DR PharmGKB; PA162400946; -.
DR VEuPathDB; HostDB:ENSG00000159200; -.
DR eggNOG; KOG4019; Eukaryota.
DR GeneTree; ENSGT00940000159870; -.
DR HOGENOM; CLU_2215801_0_0_1; -.
DR InParanoid; P53805; -.
DR OMA; DMPPVVC; -.
DR OrthoDB; 1585262at2759; -.
DR PhylomeDB; P53805; -.
DR TreeFam; TF313579; -.
DR PathwayCommons; P53805; -.
DR SignaLink; P53805; -.
DR SIGNOR; P53805; -.
DR BioGRID-ORCS; 1827; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; RCAN1; human.
DR GeneWiki; DSCR1; -.
DR GenomeRNAi; 1827; -.
DR Pharos; P53805; Tbio.
DR PRO; PR:P53805; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P53805; protein.
DR Bgee; ENSG00000159200; Expressed in cortical plate and 209 other tissues.
DR ExpressionAtlas; P53805; baseline and differential.
DR Genevisible; P53805; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; IEA:Ensembl.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR GO; GO:0007614; P:short-term memory; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR CDD; cd12708; RRM_RCAN1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR006931; Calcipressin.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR031271; RCAN1.
DR InterPro; IPR034906; RCAN1_RRM.
DR PANTHER; PTHR10300; PTHR10300; 1.
DR PANTHER; PTHR10300:SF4; PTHR10300:SF4; 1.
DR Pfam; PF04847; Calcipressin; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Phosphoprotein; Reference proteome.
FT CHAIN 1..252
FT /note="Calcipressin-1"
FT /id="PRO_0000211414"
FT REGION 219..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12809556"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12809556"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHG6"
FT VAR_SEQ 1..135
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8595418,
FT ECO:0000303|PubMed:9325060"
FT /id="VSP_001316"
FT VAR_SEQ 1..84
FT /note="MEDGVAGPQLGAAAEAAEAAEARARPGVTLRPFAPLSGAAEADEGGGDWSFI
FT DCEMEEVDLQDLPSATIACHLDPRVFVDGLCR -> MVY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8595418, ECO:0000303|Ref.4,
FT ECO:0000303|Ref.6"
FT /id="VSP_001315"
FT VAR_SEQ 1..83
FT /note="MEDGVAGPQLGAAAEAAEAAEARARPGVTLRPFAPLSGAAEADEGGGDWSFI
FT DCEMEEVDLQDLPSATIACHLDPRVFVDGLC -> MHFRNFNYSFSSLIACVANSDIFS
FT ESET (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9325060"
FT /id="VSP_001314"
FT MUTAGEN 163
FT /note="S->A: Loss of phosphorylation, no loss of
FT interaction with PPP3CA and PPP3R1, reduced ability to
FT inhibit calcineurin and increased protein half-life; alone
FT or when associated with A-167."
FT /evidence="ECO:0000269|PubMed:12809556"
FT MUTAGEN 163
FT /note="S->E: No loss of phosphorylation and no effect on
FT protein half-life; alone or when associated with E-167."
FT /evidence="ECO:0000269|PubMed:12809556"
FT MUTAGEN 167
FT /note="S->A: Loss of phosphorylation, no loss of
FT interaction with PPP3CA and PPP3R1, reduced ability to
FT inhibit calcineurin and increased protein half-life; alone
FT or when associated with A-163."
FT /evidence="ECO:0000269|PubMed:12809556"
FT MUTAGEN 167
FT /note="S->E: No loss of phosphorylation and no effect on
FT protein half-life; alone or when associated with E-163."
FT /evidence="ECO:0000269|PubMed:12809556"
FT CONFLICT 202
FT /note="H -> R (in Ref. 3; AAK92478)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="H -> Q (in Ref. 7; AAF21218)"
FT /evidence="ECO:0000305"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6UUQ"
SQ SEQUENCE 252 AA; 28079 MW; 0B17133D03BD7AFA CRC64;
MEDGVAGPQL GAAAEAAEAA EARARPGVTL RPFAPLSGAA EADEGGGDWS FIDCEMEEVD
LQDLPSATIA CHLDPRVFVD GLCRAKFESL FRTYDKDITF QYFKSFKRVR INFSNPFSAA
DARLQLHKTE FLGKEMKLYF AQTLHIGSSH LAPPNPDKQF LISPPASPPV GWKQVEDATP
VINYDLLYAI SKLGPGEKYE LHAATDTTPS VVVHVCESDQ EKEEEEEMER MRRPKPKIIQ
TRRPEYTPIH LS
