CCN4_HUMAN
ID CCN4_HUMAN Reviewed; 367 AA.
AC O95388; A8KAG6; E7EMM5; Q5JBS6; Q5JBS7; Q5JBS8; Q9HCS3;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=CCN family member 4 {ECO:0000305};
DE AltName: Full=WNT1-inducible-signaling pathway protein 1;
DE Short=WISP-1;
DE AltName: Full=Wnt-1-induced secreted protein;
DE Flags: Precursor;
GN Name=CCN4 {ECO:0000312|HGNC:HGNC:12769}; Synonyms=WISP1;
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] (ISOFORM 1).
RC TISSUE=Fetal kidney, and Lung;
RX PubMed=9843955; DOI=10.1073/pnas.95.25.14717;
RA Pennica D., Swanson T.A., Welsh J.W., Roy M.A., Lawrence D.A., Lee J.,
RA Brush J., Taneyhill L.A., Deuel B., Lew M., Watanabe C., Cohen R.L.,
RA Melham M.F., Finley G.G., Quirke P., Goddard A.D., Hillan K.J.,
RA Gurney A.L., Botstein D., Levine A.J.;
RT "WISP genes are members of the connective tissue growth factor family that
RT are up-regulated in wnt-1-transformed cells and aberrantly expressed in
RT human colon tumors.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14717-14722(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Gastric carcinoma;
RX PubMed=11571650; DOI=10.1038/sj.onc.1204723;
RA Tanaka S., Sugimachi K., Saeki H., Kinoshita J., Ohga T., Shimada M.,
RA Maehara Y., Sugimachi K.;
RT "A novel variant of WISP1 lacking a Von Willebrand type C module
RT overexpressed in scirrhous gastric carcinoma.";
RL Oncogene 20:5525-5532(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5).
RA Li Z., Chiao P.J., Evans D.B.;
RT "Multiple alternatively spliced variants of WISP1 are overexpressed in
RT pancreatic cancer.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Synovium, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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 [8]
RP FUNCTION IN WNT1 SIGNALING.
RX PubMed=10716946;
RA Xu L., Corcoran R.B., Welsh J.W., Pennica D., Levine A.J.;
RT "WISP-1 is a Wnt-1- and beta-catenin-responsive oncogene.";
RL Genes Dev. 14:585-595(2000).
RN [9]
RP FUNCTION IN TP53-MEDIATED APOPTOSIS.
RX PubMed=11782444; DOI=10.1101/gad.942902;
RA Su F., Overholtzer M., Besser D., Levine A.J.;
RT "WISP-1 attenuates p53-mediated apoptosis in response to DNA damage through
RT activation of the Akt kinase.";
RL Genes Dev. 16:46-57(2002).
RN [10]
RP INTERACTION WITH DECORIN AND BIGLYCAN.
RX PubMed=11598131; DOI=10.1074/jbc.m108339200;
RA Desnoyers L., Arnott D., Pennica D.;
RT "WISP-1 binds to decorin and biglycan.";
RL J. Biol. Chem. 276:47599-47607(2001).
CC -!- FUNCTION: Downstream regulator in the Wnt/Frizzled-signaling pathway.
CC Associated with cell survival. Attenuates p53-mediated apoptosis in
CC response to DNA damage through activation of AKT kinase. Up-regulates
CC the anti-apoptotic Bcl-X(L) protein. Adheres to skin and melanoma
CC fibroblasts. In vitro binding to skin fibroblasts occurs through the
CC proteoglycans, decorin and biglycan. {ECO:0000269|PubMed:10716946,
CC ECO:0000269|PubMed:11782444}.
CC -!- INTERACTION:
CC O95388; P49639: HOXA1; NbExp=5; IntAct=EBI-1050638, EBI-740785;
CC O95388; P32242: OTX1; NbExp=3; IntAct=EBI-1050638, EBI-740446;
CC O95388-2; P06396: GSN; NbExp=3; IntAct=EBI-25863768, EBI-351506;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=O95388-1; Sequence=Displayed;
CC Name=2; Synonyms=WISP1v;
CC IsoId=O95388-2; Sequence=VSP_008008, VSP_008009;
CC Name=3;
CC IsoId=O95388-3; Sequence=VSP_042010;
CC Name=4;
CC IsoId=O95388-4; Sequence=VSP_045958, VSP_045959;
CC Name=5;
CC IsoId=O95388-5; Sequence=VSP_047706, VSP_047707;
CC -!- TISSUE SPECIFICITY: Expressed in heart, kidney, lung, pancreas,
CC placenta, ovary, small intestine and spleen. Isoform 2 is expressed
CC predominantly in scirrhous gastric carcinoma and, weakly in placenta.
CC Overexpression is associated with several cancers including breast
CC cancer and colon tumors. Isoform 2 is overexpressed in scirrhous
CC gastric carcinoma.
CC -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
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DR EMBL; AF100779; AAC96321.1; -; mRNA.
DR EMBL; AB034725; BAB17849.1; -; mRNA.
DR EMBL; AY196486; AAP43924.1; -; mRNA.
DR EMBL; AY196487; AAP43925.1; -; mRNA.
DR EMBL; AY196488; AAP43926.1; -; mRNA.
DR EMBL; AK293031; BAF85720.1; -; mRNA.
DR EMBL; AK301508; BAG63017.1; -; mRNA.
DR EMBL; AF192304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW92162.1; -; Genomic_DNA.
DR EMBL; BC074840; AAH74840.1; -; mRNA.
DR EMBL; BC074841; AAH74841.1; -; mRNA.
DR CCDS; CCDS56555.1; -. [O95388-4]
DR CCDS; CCDS56556.1; -. [O95388-3]
DR CCDS; CCDS6371.1; -. [O95388-1]
DR CCDS; CCDS6372.1; -. [O95388-2]
DR RefSeq; NP_001191798.1; NM_001204869.1. [O95388-4]
DR RefSeq; NP_001191799.1; NM_001204870.1. [O95388-3]
DR RefSeq; NP_003873.1; NM_003882.3. [O95388-1]
DR RefSeq; NP_543028.1; NM_080838.2. [O95388-2]
DR AlphaFoldDB; O95388; -.
DR SMR; O95388; -.
DR BioGRID; 114367; 4.
DR IntAct; O95388; 4.
DR MINT; O95388; -.
DR STRING; 9606.ENSP00000250160; -.
DR GlyGen; O95388; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O95388; -.
DR PhosphoSitePlus; O95388; -.
DR BioMuta; WISP1; -.
DR MassIVE; O95388; -.
DR PaxDb; O95388; -.
DR PeptideAtlas; O95388; -.
DR PRIDE; O95388; -.
DR ProteomicsDB; 16974; -.
DR ProteomicsDB; 50837; -. [O95388-1]
DR ProteomicsDB; 50838; -. [O95388-2]
DR ProteomicsDB; 50839; -. [O95388-3]
DR ProteomicsDB; 62990; -.
DR Antibodypedia; 1567; 327 antibodies from 35 providers.
DR DNASU; 8840; -.
DR Ensembl; ENST00000220856.6; ENSP00000220856.6; ENSG00000104415.14. [O95388-2]
DR Ensembl; ENST00000250160.11; ENSP00000250160.5; ENSG00000104415.14. [O95388-1]
DR Ensembl; ENST00000517423.5; ENSP00000427744.1; ENSG00000104415.14. [O95388-4]
DR Ensembl; ENST00000519433.1; ENSP00000429185.1; ENSG00000104415.14. [O95388-3]
DR GeneID; 8840; -.
DR KEGG; hsa:8840; -.
DR MANE-Select; ENST00000250160.11; ENSP00000250160.5; NM_003882.4; NP_003873.1.
DR UCSC; uc003yub.4; human. [O95388-1]
DR CTD; 8840; -.
DR DisGeNET; 8840; -.
DR GeneCards; CCN4; -.
DR HGNC; HGNC:12769; CCN4.
DR HPA; ENSG00000104415; Low tissue specificity.
DR MIM; 603398; gene.
DR neXtProt; NX_O95388; -.
DR OpenTargets; ENSG00000104415; -.
DR PharmGKB; PA37372; -.
DR VEuPathDB; HostDB:ENSG00000104415; -.
DR eggNOG; ENOG502QQQQ; Eukaryota.
DR GeneTree; ENSGT00940000158587; -.
DR HOGENOM; CLU_063247_3_1_1; -.
DR InParanoid; O95388; -.
DR OMA; IEVRFEC; -.
DR OrthoDB; 601212at2759; -.
DR PhylomeDB; O95388; -.
DR TreeFam; TF326070; -.
DR PathwayCommons; O95388; -.
DR SignaLink; O95388; -.
DR SIGNOR; O95388; -.
DR BioGRID-ORCS; 8840; 13 hits in 1062 CRISPR screens.
DR ChiTaRS; WISP1; human.
DR GeneWiki; WNT1-inducible-signaling_pathway_protein_1; -.
DR GenomeRNAi; 8840; -.
DR Pharos; O95388; Tbio.
DR PRO; PR:O95388; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O95388; protein.
DR Bgee; ENSG00000104415; Expressed in cartilage tissue and 113 other tissues.
DR ExpressionAtlas; O95388; baseline and differential.
DR Genevisible; O95388; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0060548; P:negative regulation of cell death; IBA:GO_Central.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl.
DR GO; GO:0001817; P:regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 1.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR006208; Glyco_hormone_CN.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR012395; IGFBP_CNN.
DR InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
DR InterPro; IPR043973; TSP1_CCN.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF00007; Cys_knot; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF19035; TSP1_CCN; 1.
DR Pfam; PF00093; VWC; 1.
DR PIRSF; PIRSF036495; IGFBP_rP_CNN; 1.
DR SMART; SM00041; CT; 1.
DR SMART; SM00121; IB; 1.
DR SMART; SM00209; TSP1; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS00222; IGFBP_N_1; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS50092; TSP1; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Disulfide bond; Glycoprotein;
KW Proto-oncogene; Reference proteome; Secreted; Signal;
KW Wnt signaling pathway.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..367
FT /note="CCN family member 4"
FT /id="PRO_0000014406"
FT DOMAIN 40..118
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 121..186
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 215..260
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 273..347
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 273..310
FT /evidence="ECO:0000250"
FT DISULFID 290..324
FT /evidence="ECO:0000250"
FT DISULFID 301..340
FT /evidence="ECO:0000250"
FT DISULFID 304..342
FT /evidence="ECO:0000250"
FT DISULFID 309..346
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..31
FT /note="MRWFLPWTLAAVTAAAASTVLATALSPAPTT -> MPVPLTSRHEVVPALDA
FT GSSDSSSRQHRPGH (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_047706"
FT VAR_SEQ 24..268
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_042010"
FT VAR_SEQ 32..203
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_047707"
FT VAR_SEQ 117..155
FT /note="QVVGVGCVLDGVRYNNGQSFQPNCKYNCTCIDGAVGCTP -> RREEVSGCV
FT PARGIHELHTCGLHQHTLLSTQVLWSLHGQ (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_045958"
FT VAR_SEQ 117
FT /note="Q -> H (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11571650"
FT /id="VSP_008008"
FT VAR_SEQ 118..204
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11571650"
FT /id="VSP_008009"
FT VAR_SEQ 156..367
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_045959"
FT VARIANT 205
FT /note="A -> S (in dbSNP:rs35513885)"
FT /id="VAR_061265"
FT CONFLICT 91
FT /note="A -> V (in Ref. 3; AAP43926)"
FT /evidence="ECO:0000305"
FT CONFLICT O95388-4:155
FT /note="Q -> QQVLHPLQV (in Ref. 3; AAP43926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 40331 MW; 9F29CA94D69C0502 CRC64;
MRWFLPWTLA AVTAAAASTV LATALSPAPT TMDFTPAPLE DTSSRPQFCK WPCECPPSPP
RCPLGVSLIT DGCECCKMCA QQLGDNCTEA AICDPHRGLY CDYSGDRPRY AIGVCAQVVG
VGCVLDGVRY NNGQSFQPNC KYNCTCIDGA VGCTPLCLRV RPPRLWCPHP RRVSIPGHCC
EQWVCEDDAK RPRKTAPRDT GAFDAVGEVE AWHRNCIAYT SPWSPCSTSC GLGVSTRISN
VNAQCWPEQE SRLCNLRPCD VDIHTLIKAG KKCLAVYQPE ASMNFTLAGC ISTRSYQPKY
CGVCMDNRCC IPYKSKTIDV SFQCPDGLGF SRQVLWINAC FCNLSCRNPN DIFADLESYP
DFSEIAN
