ID   DDR2_MOUSE              Reviewed;         854 AA.
AC   Q62371; B2RSD7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   24-JAN-2024, entry version 205.
DE   RecName: Full=Discoidin domain-containing receptor 2;
DE            Short=Discoidin domain receptor 2;
DE            EC=2.7.10.1;
DE   AltName: Full=CD167 antigen-like family member B;
DE   AltName: Full=Neurotrophic tyrosine kinase, receptor-related 3;
DE   AltName: Full=Receptor protein-tyrosine kinase TKT;
DE   AltName: Full=Tyrosine-protein kinase TYRO10;
DE   AltName: CD_antigen=CD167b;
DE   Flags: Precursor;
GN   Name=Ddr2; Synonyms=Ntrkr3, Tkt, Tyro10;
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].
RX   PubMed=8247548;
RA   Karn T., Holtrich U., Braeuninger A., Boehme B., Wolf G.,
RA   Ruebsamen-Waigmann H., Strebhardt K.;
RT   "Structure, expression and chromosomal mapping of TKT from man and mouse: a
RT   new subclass of receptor tyrosine kinases with a factor VIII-like domain.";
RL   Oncogene 8:3433-3440(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=8108131;
RA   Lai C., Lemke G.E.;
RT   "Structure and expression of the Tyro 10 receptor tyrosine kinase.";
RL   Oncogene 9:877-883(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
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   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11375938; DOI=10.1093/embo-reports/kve094;
RA   Labrador J.P., Azcoitia V., Tuckermann J., Lin C., Olaso E., Manes S.,
RA   Bruckner K., Goergen J.L., Lemke G., Yancopoulos G., Angel P., Martinez C.,
RA   Klein R.;
RT   "The collagen receptor DDR2 regulates proliferation and its elimination
RT   leads to dwarfism.";
RL   EMBO Rep. 2:446-452(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=11723120; DOI=10.1074/jbc.m107571200;
RA   Olaso E., Labrador J.-P., Wang L., Ikeda K., Eng F.J., Klein R.,
RA   Lovett D.H., Lin H.C., Friedman S.L.;
RT   "Discoidin domain receptor 2 regulates fibroblast proliferation and
RT   migration through the extracellular matrix in association with
RT   transcriptional activation of matrix metalloproteinase-2.";
RL   J. Biol. Chem. 277:3606-3613(2002).
RN   [6]
RP   FUNCTION, INTERACTION WITH SRC AND SHC1, MUTAGENESIS OF TYR-471 AND
RP   LYS-608, AND PHOSPHORYLATION AT TYR-471.
RX   PubMed=11884411; DOI=10.1074/jbc.m201078200;
RA   Ikeda K., Wang L.H., Torres R., Zhao H., Olaso E., Eng F.J., Labrador P.,
RA   Klein R., Lovett D., Yancopoulos G.D., Friedman S.L., Lin H.C.;
RT   "Discoidin domain receptor 2 interacts with Src and Shc following its
RT   activation by type I collagen.";
RL   J. Biol. Chem. 277:19206-19212(2002).
RN   [7]
RP   FUNCTION IN UP-REGULATION OF MMP13.
RX   PubMed=15509586; DOI=10.1074/jbc.m411036200;
RA   Xu L., Peng H., Wu D., Hu K., Goldring M.B., Olsen B.R., Li Y.;
RT   "Activation of the discoidin domain receptor 2 induces expression of matrix
RT   metalloproteinase 13 associated with osteoarthritis in mice.";
RL   J. Biol. Chem. 280:548-555(2005).
RN   [8]
RP   INVOLVEMENT IN SLI, AND TISSUE SPECIFICITY.
RX   PubMed=18483174; DOI=10.1210/me.2007-0310;
RA   Kano K., Marin de Evsikova C., Young J., Wnek C., Maddatu T.P.,
RA   Nishina P.M., Naggert J.K.;
RT   "A novel dwarfism with gonadal dysfunction due to loss-of-function allele
RT   of the collagen receptor gene, Ddr2, in the mouse.";
RL   Mol. Endocrinol. 22:1866-1880(2008).
RN   [9]
RP   INVOLVEMENT IN SLI, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=19681157; DOI=10.1002/mrd.21093;
RA   Kano K., Kitamura A., Matsuwaki T., Morimatsu M., Naito K.;
RT   "Discoidin domain receptor 2 (DDR2) is required for maintenance of
RT   spermatogenesis in male mice.";
RL   Mol. Reprod. Dev. 77:29-37(2010).
CC   -!- FUNCTION: Tyrosine kinase that functions as a cell surface receptor for
CC       fibrillar collagen and regulates cell differentiation, remodeling of
CC       the extracellular matrix, cell migration and cell proliferation.
CC       Required for normal bone development. Regulates osteoblast
CC       differentiation and chondrocyte maturation via a signaling pathway that
CC       involves MAP kinases and leads to the activation of the transcription
CC       factor RUNX2. Regulates remodeling of the extracellular matrix by up-
CC       regulation of the collagenases MMP1, MMP2 and MMP13, and thereby
CC       facilitates cell migration and tumor cell invasion. Promotes fibroblast
CC       migration and proliferation, and thereby contributes to cutaneous wound
CC       healing. {ECO:0000269|PubMed:11375938, ECO:0000269|PubMed:11723120,
CC       ECO:0000269|PubMed:11884411, ECO:0000269|PubMed:15509586,
CC       ECO:0000269|PubMed:19681157}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- ACTIVITY REGULATION: Present in an inactive state in the absence of
CC       collagen binding and phosphorylation by SRC. Tyrosine phosphorylation
CC       enhances the affinity for ATP and the catalytic activity.
CC   -!- SUBUNIT: Binds hydroxyproline-rich sequence motifs in fibrillar,
CC       glycosylated collagen, such as the GQOGVMGFO motif, where O stands for
CC       hydroxyproline. Interacts with SRC. Interacts (tyrosine phosphorylated)
CC       with SHC1. {ECO:0000269|PubMed:11884411}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Detected in lung, ovary, skin and
CC       in testis Leydig cells (at protein level). Widely expressed. Detected
CC       at high levels in heart, lung, skeletal muscle, central nervous system
CC       (CNS) and kidney, and at lower levels in brain and testis. Detected in
CC       chondrocytes in tibia growth plates of young mice.
CC       {ECO:0000269|PubMed:11375938, ECO:0000269|PubMed:18483174,
CC       ECO:0000269|PubMed:19681157}.
CC   -!- INDUCTION: Up-regulated during osteoblast differentiation (in vitro).
CC       Up-regulated in cartilage from mice with osteoarthritis.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- PTM: Tyrosine phosphorylated in response to collagen binding.
CC       Phosphorylated by SRC; this is required for activation and subsequent
CC       autophosphorylation on additional tyrosine residues (By similarity).
CC       {ECO:0000250}.
CC   -!- DISEASE: Note=Defects in Ddr2 are the cause of the smallie (sli)
CC       phenotype. Smallie mice show distinct dwarfing, with reduced body mass
CC       and reduced bone mineral content. Mice also have mild craniofacial
CC       deformities, such as protuberant eyes and snub noses. Smallie mice have
CC       a reduced life span, with about half of them dying within 6 months.
CC       Matings between male and female smallie mice do not yield any
CC       offspring. The levels of circulating steroid hormones remain at a level
CC       corresponding to prepubertal wild-type mice. Adult testes exhibit much
CC       reduced numbers of spermatids with atrophy of spermatogonia, Sertoli
CC       and Leydig cells. Ovaries show an absence of corpora lutea.
CC   -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate, but
CC       fail to thrive, resulting in much reduced adult body weight and
CC       dwarfing. They exhibit shortening of long bones, irregular growth of
CC       flat bones and a shortened snout. Young mice show shortened growth
CC       plates in long bones and impaired chondrocyte proliferation. Likewise,
CC       cultured fibroblasts from mutant mice show reduced proliferation.
CC       {ECO:0000269|PubMed:11375938}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   -!- CAUTION: According to PubMed:18483174 Ddr2 is required for male and
CC       female fertility, since smallie mice with a 150 kb deletion that
CC       extends into the Ddr2 gene are sterile. Smallie males have defects in
CC       spermatogenesis (PubMed:19681157). On the other hand, the fertility
CC       status of mice with a targeted disruption of the Ddr2 gene has not been
CC       mentioned (PubMed:11375938). Thus, the infertility of smallie mice may
CC       be due to some additional, not yet identified defect.
CC       {ECO:0000305|PubMed:11375938, ECO:0000305|PubMed:19681157}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA54040.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X76505; CAA54040.1; ALT_INIT; mRNA.
DR   EMBL; BC138826; AAI38827.1; -; mRNA.
DR   EMBL; BC138827; AAI38828.1; -; mRNA.
DR   CCDS; CCDS48436.1; -.
DR   PIR; I48859; I48859.
DR   RefSeq; NP_072075.2; NM_022563.2.
DR   RefSeq; XP_006496759.1; XM_006496696.3.
DR   RefSeq; XP_006496760.1; XM_006496697.3.
DR   RefSeq; XP_006496761.1; XM_006496698.3.
DR   AlphaFoldDB; Q62371; -.
DR   SMR; Q62371; -.
DR   BioGRID; 201871; 2.
DR   STRING; 10090.ENSMUSP00000141443; -.
DR   GlyCosmos; Q62371; 5 sites, No reported glycans.
DR   GlyGen; Q62371; 5 sites.
DR   iPTMnet; Q62371; -.
DR   PhosphoSitePlus; Q62371; -.
DR   SwissPalm; Q62371; -.
DR   MaxQB; Q62371; -.
DR   PaxDb; 10090-ENSMUSP00000129624; -.
DR   PeptideAtlas; Q62371; -.
DR   ProteomicsDB; 277968; -.
DR   Pumba; Q62371; -.
DR   Antibodypedia; 4177; 514 antibodies from 36 providers.
DR   DNASU; 18214; -.
DR   Ensembl; ENSMUST00000027985.8; ENSMUSP00000027985.3; ENSMUSG00000026674.10.
DR   Ensembl; ENSMUST00000170800.8; ENSMUSP00000129624.2; ENSMUSG00000026674.10.
DR   Ensembl; ENSMUST00000194690.6; ENSMUSP00000141443.2; ENSMUSG00000026674.10.
DR   GeneID; 18214; -.
DR   KEGG; mmu:18214; -.
DR   UCSC; uc007dlu.2; mouse.
DR   AGR; MGI:1345277; -.
DR   CTD; 4921; -.
DR   MGI; MGI:1345277; Ddr2.
DR   VEuPathDB; HostDB:ENSMUSG00000026674; -.
DR   eggNOG; KOG1094; Eukaryota.
DR   GeneTree; ENSGT00940000154842; -.
DR   HOGENOM; CLU_008873_2_0_1; -.
DR   InParanoid; Q62371; -.
DR   OMA; HEPPNSC; -.
DR   OrthoDB; 2999496at2759; -.
DR   PhylomeDB; Q62371; -.
DR   TreeFam; TF317840; -.
DR   BRENDA; 2.7.10.1; 3474.
DR   Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR   BioGRID-ORCS; 18214; 2 hits in 80 CRISPR screens.
DR   ChiTaRS; Ddr2; mouse.
DR   PRO; PR:Q62371; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q62371; Protein.
DR   Bgee; ENSMUSG00000026674; Expressed in vault of skull and 239 other cell types or tissues.
DR   ExpressionAtlas; Q62371; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005518; F:collagen binding; IDA:MGI.
DR   GO; GO:0038062; F:protein tyrosine kinase collagen receptor activity; IDA:UniProtKB.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0031214; P:biomineral tissue development; IMP:UniProtKB.
DR   GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR   GO; GO:0035988; P:chondrocyte proliferation; IMP:UniProtKB.
DR   GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
DR   GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0003416; P:endochondral bone growth; IMP:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; ISO:MGI.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IMP:UniProtKB.
DR   GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:UniProtKB.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:UniProtKB.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR   GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; ISO:MGI.
DR   GO; GO:1904899; P:positive regulation of hepatic stellate cell proliferation; ISO:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR   GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0090303; P:positive regulation of wound healing; ISO:MGI.
DR   GO; GO:0030500; P:regulation of bone mineralization; ISS:UniProtKB.
DR   GO; GO:0034103; P:regulation of tissue remodeling; ISO:MGI.
DR   GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:MGI.
DR   CDD; cd00057; FA58C; 1.
DR   Gene3D; 2.60.120.1190; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR048525; DDR1-2_DS-like.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF295; DISCOIDIN DOMAIN-CONTAINING RECEPTOR 2; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF21114; DDR1-2_DS-like; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
DR   Genevisible; Q62371; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Osteogenesis; Phosphoprotein; Receptor;
KW   Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..854
FT                   /note="Discoidin domain-containing receptor 2"
FT                   /id="PRO_0000016747"
FT   TOPO_DOM        22..399
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        400..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..854
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..185
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DOMAIN          563..848
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          452..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        709
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         569..577
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         608
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         471
FT                   /note="Phosphotyrosine; by SRC and autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:11884411"
FT   MOD_RES         735
FT                   /note="Phosphotyrosine; by SRC and autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q16832"
FT   MOD_RES         739
FT                   /note="Phosphotyrosine; by SRC and autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q16832"
FT   MOD_RES         740
FT                   /note="Phosphotyrosine; by SRC and autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q16832"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DISULFID        73..177
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   MUTAGEN         471
FT                   /note="Y->F: Reduces tyrosine phosphorylation by 90%; when
FT                   associated with E-608."
FT                   /evidence="ECO:0000269|PubMed:11884411"
FT   MUTAGEN         608
FT                   /note="K->E: Abolishes kinase activity. Reduces tyrosine
FT                   phosphorylation by 90%; when associated with F-471."
FT                   /evidence="ECO:0000269|PubMed:11884411"
SQ   SEQUENCE   854 AA;  96482 MW;  45CFD2BE9ED524D4 CRC64;
     MIPIPRMPLV LLLLLLILGS AKAQVNPAIC RYPLGMSGGH IPDEDITASS QWSESTAAKY
     GRLDSEEGDG AWCPEIPVQP DDLKEFLQID LRTLHFITLV GTQGRHAGGH GIEFAPMYKI
     NYSRDGSRWI SWRNRHGKQV LDGNSNPYDV FLKDLEPPIV ARFVRLIPVT DHSMNVCMRV
     ELYGCVWLDG LVSYNAPAGQ QFVLPGGSII YLNDSVYDGA VGYSMTEGLG QLTDGVSGLD
     DFTQTHEYHV WPGYDYVGWR NESATNGFIE IMFEFDRIRN FTTMKVHCNN MFAKGVKIFK
     EVQCYFRSEA SEWEPTAVYF PLVLDDVNPS ARFVTVPLHH RMASAIKCQY HFADTWMMFS
     EITFQSDAAM YNNSGALPTS PMAPTTYDPM LKVDDSNTRI LIGCLVAIIF ILLAIIVIIL
     WRQFWQKMLE KASRRMLDDE MTVSLSLPSE SSMFNNNRSS SPSEQESNST YDRIFPLRPD
     YQEPSRLIRK LPEFAPGEEE SGCSGVVKPA QPNGPEGVPH YAEADIVNLQ GVTGGNTYCV
     PAVTMDLLSG KDVAVEEFPR KLLAFKEKLG EGQFGEVHLC EVEGMEKFKD KDFALDVSAN
     QPVLVAVKML RADANKNARN DFLKEIKIMS RLKDPNIIRL LAVCITEDPL CMITEYMENG
     DLNQFLSRHE PLSSCSSDAT VSYANLKFMA TQIASGMKYL SSLNFVHRDL ATRNCLVGKN
     YTIKIADFGM SRNLYSGDYY RIQGRAVLPI RWMSWESILL GKFTTASDVW AFGVTLWETF
     TFCQEQPYSQ LSDEQVIENT GEFFRDQGRQ IYLPQPALCP DSVYKLMLSC WRRETKHRPS
     FQEIHLLLLQ QGAE
//