CDON_HUMAN
ID CDON_HUMAN Reviewed; 1287 AA.
AC Q4KMG0; O14631;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cell adhesion molecule-related/down-regulated by oncogenes;
DE Flags: Precursor;
GN Name=CDON; Synonyms=CDO;
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 2).
RC TISSUE=Fetal brain, and Fetal lung;
RX PubMed=9214393; DOI=10.1083/jcb.138.1.203;
RA Kang J.-S., Gao M., Feinleib J.L., Cotter P.D., Guadagno S.N., Krauss R.S.;
RT "CDO: an oncogene-, serum-, and anchorage-regulated member of the
RT Ig/fibronectin type III repeat family.";
RL J. Cell Biol. 138:203-213(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 826-924 IN COMPLEX WITH SHH, AND
RP INTERACTION WITH SHH.
RX PubMed=18794898; DOI=10.1038/nature07358;
RA McLellan J.S., Zheng X., Hauk G., Ghirlando R., Beachy P.A., Leahy D.J.;
RT "The mode of Hedgehog binding to Ihog homologues is not conserved across
RT different phyla.";
RL Nature 455:979-983(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 826-924 IN COMPLEXES WITH IHH AND
RP DHH, AND INTERACTION WITH IHH AND DHH.
RX PubMed=20519495; DOI=10.1074/jbc.m110.131680;
RA Kavran J.M., Ward M.D., Oladosu O.O., Mulepati S., Leahy D.J.;
RT "All mammalian Hedgehog proteins interact with cell adhesion molecule,
RT down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a conserved
RT manner.";
RL J. Biol. Chem. 285:24584-24590(2010).
RN [6]
RP VARIANTS HPE11 SER-684; ALA-689; MET-691; GLU-780; ALA-790 AND ARG-940.
RX PubMed=21802063; DOI=10.1016/j.ajhg.2011.07.001;
RA Bae G.U., Domene S., Roessler E., Schachter K., Kang J.S., Muenke M.,
RA Krauss R.S.;
RT "Mutations in CDON, encoding a hedgehog receptor, result in
RT holoprosencephaly and defective interactions with other hedgehog
RT receptors.";
RL Am. J. Hum. Genet. 89:231-240(2011).
CC -!- FUNCTION: Component of a cell-surface receptor complex that mediates
CC cell-cell interactions between muscle precursor cells. Promotes
CC differentiation of myogenic cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of a complex that contains BOC, CDON, NEO1, cadherins and
CC CTNNB1. Interacts with NTN3 (By similarity). Interacts with PTCH1 (By
CC similarity). Interacts with GAS1 (By similarity). Interacts with DHH,
CC IHH and SHH. {ECO:0000250, ECO:0000269|PubMed:18794898,
CC ECO:0000269|PubMed:20519495}.
CC -!- INTERACTION:
CC Q4KMG0; P00519: ABL1; NbExp=2; IntAct=EBI-7016840, EBI-375543;
CC Q4KMG0; O43323: DHH; NbExp=2; IntAct=EBI-7016840, EBI-11667804;
CC Q4KMG0; Q13635: PTCH1; NbExp=2; IntAct=EBI-7016840, EBI-8775406;
CC Q4KMG0; Q62226: Shh; Xeno; NbExp=7; IntAct=EBI-7016840, EBI-15610166;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4KMG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4KMG0-2; Sequence=VSP_018201;
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- DISEASE: Holoprosencephaly 11 (HPE11) [MIM:614226]: A structural
CC anomaly of the brain, in which the developing forebrain fails to
CC correctly separate into right and left hemispheres. Holoprosencephaly
CC is genetically heterogeneous and associated with several distinct
CC facies and phenotypic variability. {ECO:0000269|PubMed:21802063}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
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DR EMBL; AF004841; AAC34901.2; -; mRNA.
DR EMBL; AP000821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC098583; AAH98583.1; -; mRNA.
DR CCDS; CCDS58192.1; -. [Q4KMG0-1]
DR CCDS; CCDS8468.1; -. [Q4KMG0-2]
DR PIR; T03097; T03097.
DR RefSeq; NP_001230526.1; NM_001243597.1. [Q4KMG0-1]
DR RefSeq; NP_058648.4; NM_016952.4. [Q4KMG0-2]
DR RefSeq; XP_011541164.1; XM_011542862.2. [Q4KMG0-1]
DR RefSeq; XP_011541165.1; XM_011542863.2. [Q4KMG0-1]
DR RefSeq; XP_011541166.1; XM_011542864.2. [Q4KMG0-1]
DR RefSeq; XP_011541167.1; XM_011542865.2. [Q4KMG0-1]
DR RefSeq; XP_011541168.1; XM_011542866.2.
DR RefSeq; XP_016873362.1; XM_017017873.1. [Q4KMG0-1]
DR PDB; 3D1M; X-ray; 1.70 A; C/D=826-924.
DR PDB; 3N1F; X-ray; 1.60 A; C/D=826-924.
DR PDB; 3N1Q; X-ray; 2.89 A; C/D/F=826-924.
DR PDBsum; 3D1M; -.
DR PDBsum; 3N1F; -.
DR PDBsum; 3N1Q; -.
DR AlphaFoldDB; Q4KMG0; -.
DR SMR; Q4KMG0; -.
DR BioGRID; 119165; 17.
DR DIP; DIP-57226N; -.
DR IntAct; Q4KMG0; 12.
DR MINT; Q4KMG0; -.
DR STRING; 9606.ENSP00000376458; -.
DR GlyGen; Q4KMG0; 9 sites.
DR iPTMnet; Q4KMG0; -.
DR PhosphoSitePlus; Q4KMG0; -.
DR BioMuta; CDON; -.
DR DMDM; 308153422; -.
DR EPD; Q4KMG0; -.
DR MassIVE; Q4KMG0; -.
DR MaxQB; Q4KMG0; -.
DR PaxDb; Q4KMG0; -.
DR PeptideAtlas; Q4KMG0; -.
DR PRIDE; Q4KMG0; -.
DR ProteomicsDB; 62193; -. [Q4KMG0-1]
DR ProteomicsDB; 62194; -. [Q4KMG0-2]
DR Antibodypedia; 2227; 204 antibodies from 30 providers.
DR DNASU; 50937; -.
DR Ensembl; ENST00000263577.11; ENSP00000263577.7; ENSG00000064309.16. [Q4KMG0-2]
DR Ensembl; ENST00000392693.7; ENSP00000376458.3; ENSG00000064309.16. [Q4KMG0-1]
DR Ensembl; ENST00000531738.6; ENSP00000432901.2; ENSG00000064309.16. [Q4KMG0-2]
DR Ensembl; ENST00000684078.1; ENSP00000507318.1; ENSG00000064309.16. [Q4KMG0-1]
DR GeneID; 50937; -.
DR KEGG; hsa:50937; -.
DR MANE-Select; ENST00000531738.6; ENSP00000432901.2; NM_001378964.1; NP_001365893.1. [Q4KMG0-2]
DR UCSC; uc001qdc.5; human. [Q4KMG0-1]
DR CTD; 50937; -.
DR DisGeNET; 50937; -.
DR GeneCards; CDON; -.
DR GeneReviews; CDON; -.
DR HGNC; HGNC:17104; CDON.
DR HPA; ENSG00000064309; Low tissue specificity.
DR MalaCards; CDON; -.
DR MIM; 608707; gene.
DR MIM; 614226; phenotype.
DR neXtProt; NX_Q4KMG0; -.
DR OpenTargets; ENSG00000064309; -.
DR Orphanet; 93925; Alobar holoprosencephaly.
DR Orphanet; 93924; Lobar holoprosencephaly.
DR Orphanet; 280200; Microform holoprosencephaly.
DR Orphanet; 93926; Midline interhemispheric variant of holoprosencephaly.
DR Orphanet; 95496; Pituitary stalk interruption syndrome.
DR Orphanet; 220386; Semilobar holoprosencephaly.
DR Orphanet; 280195; Septopreoptic holoprosencephaly.
DR PharmGKB; PA26328; -.
DR VEuPathDB; HostDB:ENSG00000064309; -.
DR eggNOG; ENOG502QT4P; Eukaryota.
DR GeneTree; ENSGT00940000157114; -.
DR HOGENOM; CLU_008503_0_0_1; -.
DR InParanoid; Q4KMG0; -.
DR OMA; NGCAHLH; -.
DR OrthoDB; 102649at2759; -.
DR PhylomeDB; Q4KMG0; -.
DR TreeFam; TF332268; -.
DR PathwayCommons; Q4KMG0; -.
DR Reactome; R-HSA-525793; Myogenesis.
DR Reactome; R-HSA-5632681; Ligand-receptor interactions.
DR Reactome; R-HSA-5635838; Activation of SMO.
DR SignaLink; Q4KMG0; -.
DR SIGNOR; Q4KMG0; -.
DR BioGRID-ORCS; 50937; 11 hits in 1063 CRISPR screens.
DR ChiTaRS; CDON; human.
DR EvolutionaryTrace; Q4KMG0; -.
DR GeneWiki; CDON; -.
DR GenomeRNAi; 50937; -.
DR Pharos; Q4KMG0; Tbio.
DR PRO; PR:Q4KMG0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q4KMG0; protein.
DR Bgee; ENSG00000064309; Expressed in ventricular zone and 150 other tissues.
DR ExpressionAtlas; Q4KMG0; baseline and differential.
DR Genevisible; Q4KMG0; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
DR GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0010172; P:embryonic body morphogenesis; IEA:Ensembl.
DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IEA:InterPro.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0043393; P:regulation of protein binding; IEA:Ensembl.
DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 8.
DR InterPro; IPR032983; CDO.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR44170:SF1; PTHR44170:SF1; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Glycoprotein; Holoprosencephaly; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1287
FT /note="Cell adhesion molecule-related/down-regulated by
FT oncogenes"
FT /id="PRO_0000234054"
FT TOPO_DOM 26..963
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 964..984
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 985..1287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..114
FT /note="Ig-like C2-type 1"
FT DOMAIN 120..204
FT /note="Ig-like C2-type 2"
FT DOMAIN 225..303
FT /note="Ig-like C2-type 3"
FT DOMAIN 310..396
FT /note="Ig-like C2-type 4"
FT DOMAIN 405..516
FT /note="Ig-like C2-type 5"
FT DOMAIN 579..677
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 723..821
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 826..926
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 531..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 873
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 141..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 243..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 333..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 426..500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1212..1234
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9214393"
FT /id="VSP_018201"
FT VARIANT 66
FT /note="K -> R (in dbSNP:rs7122277)"
FT /id="VAR_056038"
FT VARIANT 162
FT /note="E -> K (in dbSNP:rs3740909)"
FT /id="VAR_056039"
FT VARIANT 351
FT /note="P -> A (in dbSNP:rs35665264)"
FT /id="VAR_056040"
FT VARIANT 684
FT /note="T -> S (in HPE11; benign variant;
FT dbSNP:rs145983470)"
FT /evidence="ECO:0000269|PubMed:21802063"
FT /id="VAR_066497"
FT VARIANT 686
FT /note="A -> V (in dbSNP:rs12274923)"
FT /id="VAR_056041"
FT VARIANT 689
FT /note="P -> A (in HPE11; dbSNP:rs387906995)"
FT /evidence="ECO:0000269|PubMed:21802063"
FT /id="VAR_066498"
FT VARIANT 691
FT /note="V -> M (in HPE11; dbSNP:rs139323558)"
FT /evidence="ECO:0000269|PubMed:21802063"
FT /id="VAR_066499"
FT VARIANT 780
FT /note="V -> E (in HPE11; dbSNP:rs387906996)"
FT /evidence="ECO:0000269|PubMed:21802063"
FT /id="VAR_066500"
FT VARIANT 790
FT /note="T -> A (in HPE11; dbSNP:rs387906997)"
FT /evidence="ECO:0000269|PubMed:21802063"
FT /id="VAR_066501"
FT VARIANT 940
FT /note="S -> R (in HPE11; dbSNP:rs369673018)"
FT /evidence="ECO:0000269|PubMed:21802063"
FT /id="VAR_066502"
FT CONFLICT 75
FT /note="V -> I (in Ref. 1; AAC34901 and 3; AAH98583)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="G -> E (in Ref. 3; AAH98583)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="K -> E (in Ref. 1; AAC34901)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="L -> I (in Ref. 1; AAC34901)"
FT /evidence="ECO:0000305"
FT CONFLICT 1244
FT /note="I -> N (in Ref. 3; AAH98583)"
FT /evidence="ECO:0000305"
FT STRAND 831..837
FT /evidence="ECO:0007829|PDB:3N1F"
FT STRAND 839..841
FT /evidence="ECO:0007829|PDB:3N1F"
FT STRAND 843..848
FT /evidence="ECO:0007829|PDB:3N1F"
FT HELIX 852..854
FT /evidence="ECO:0007829|PDB:3N1F"
FT STRAND 861..868
FT /evidence="ECO:0007829|PDB:3N1F"
FT HELIX 874..876
FT /evidence="ECO:0007829|PDB:3N1F"
FT STRAND 878..883
FT /evidence="ECO:0007829|PDB:3N1F"
FT STRAND 887..891
FT /evidence="ECO:0007829|PDB:3N1F"
FT STRAND 899..908
FT /evidence="ECO:0007829|PDB:3N1F"
FT STRAND 919..922
FT /evidence="ECO:0007829|PDB:3N1F"
SQ SEQUENCE 1287 AA; 139147 MW; B7870C66F5224BBE CRC64;
MHPDLGPLCT LLYVTLTILC SSVSSDLAPY FTSEPLSAVQ KLGGPVVLHC SAQPVTTRIS
WLHNGKTLDG NLEHVKIHQG TLTILSLNSS LLGYYQCLAN NSIGAIVSGP ATVSVAVLGD
FGSSTKHVIT AEEKSAGFIG CRVPESNPKA EVRYKIRGKW LEHSTENYLI LPSGNLQILN
VSLEDKGSYK CAAYNPVTHQ LKVEPIGRKL LVSRPSSDDV HILHPTHSQA LAVLSRSPVT
LECVVSGVPA PQVYWLKDGQ DIAPGSNWRR LYSHLATDSV DPADSGNYSC MAGNKSGDVK
YVTYMVNVLE HASISKGLQD QIVSLGATVH FTCDVHGNPA PNCTWFHNAQ PIHPSARHLT
AGNGLKISGV TVEDVGMYQC VADNGIGFMH STGRLEIEND GGFKPVIITA PVSAKVADGD
FVTLSCNASG LPVPVIRWYD SHGLITSHPS QVLRSKSRKS QLSRPEGLNL EPVYFVLSQA
GASSLHIQAV TQEHAGKYIC EAANEHGTTQ AEASLMVVPF ETNTKAETVT LPDAAQNDDR
SKRDGSETGL LSSFPVKVHP SAVESAPEKN ASGISVPDAP IILSPPQTHT PDTYNLVWRA
GKDGGLPINA YFVKYRKLDD GVGMLGSWHT VRVPGSENEL HLAELEPSSL YEVLMVARSA
AGEGQPAMLT FRTSKEKTAS SKNTQASSPP VGIPKYPVVS EAANNNFGVV LTDSSRHSGV
PEAPDRPTIS TASETSVYVT WIPRANGGSP ITAFKVEYKR MRTSNWLVAA EDIPPSKLSV
EVRSLEPGST YKFRVIAINH YGESFRSSAS RPYQVVGFPN RFSSRPITGP HIAYTEAVSD
TQIMLKWTYI PSSNNNTPIQ GFYIYYRPTD SDNDSDYKRD VVEGSKQWHM IGHLQPETSY
DIKMQCFNEG GESEFSNVMI CETKVKRVPG ASEYPVKDLS TPPNSLGSGG NVGPATSPAR
SSDMLYLIVG CVLGVMVLIL MVFIAMCLWK NRQQNTIQKY DPPGYLYQGS DMNGQMVDYT
TLSGASQING NVHGGFLTNG GLSSGYSHLH HKVPNAVNGI VNGSLNGGLY SGHSNSLTRT
HVDFEHPHHL VNGGGMYTAV PQIDPLECVN CRNCRNNNRC FTKTNSTFSS SPPPVVPVVA
PYPQDGLEMK PLSHVKVPVC LTSAVPDCGQ LPEESVKDNV EPVPTQRTCC QDIVNDVSSD
GSEDPAEFSR GQEGMINLRI PDHLQLAKSC VWEGDSCAHS ETEINIVSWN ALILPPVPEG
CAEKTMWSPP GIPLDSPTEV LQQPRET
