PTK7_MOUSE
ID PTK7_MOUSE Reviewed; 1062 AA.
AC Q8BKG3; Q3V422; Q6W8S9; Q8CHK5; Q8K178;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Inactive tyrosine-protein kinase 7;
DE AltName: Full=Protein chuzhoi;
DE AltName: Full=Protein-tyrosine kinase 7;
DE AltName: Full=Pseudo tyrosine kinase receptor 7;
DE AltName: Full=Tyrosine-protein kinase-like 7;
DE Flags: Precursor;
GN Name=Ptk7;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Liver;
RX PubMed=15019986; DOI=10.1016/j.gene.2003.12.006;
RA Jung J.-W., Shin W.S., Song J., Lee S.-T.;
RT "Cloning and characterization of the full-length mouse Ptk7 cDNA encoding a
RT defective receptor protein tyrosine kinase.";
RL Gene 328:75-84(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and 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].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 774-1062.
RC STRAIN=W/Wv;
RA Daigo Y., Takayama I., Fujino M.A.;
RT "Isolation and characterization of novel human and mouse genes, which are
RT expressed in the digestive tract.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15229603; DOI=10.1038/nature02677;
RA Lu X., Borchers A.G.M., Jolicoeur C., Rayburn H., Baker J.C.,
RA Tessier-Lavigne M.;
RT "PTK7/CCK-4 is a novel regulator of planar cell polarity in vertebrates.";
RL Nature 430:93-98(2004).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108 AND ASN-397.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98; ASN-275; ASN-397 AND
RP ASN-559.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19439496; DOI=10.1242/dev.030601;
RA Yen W.W., Williams M., Periasamy A., Conaway M., Burdsal C., Keller R.,
RA Lu X., Sutherland A.;
RT "PTK7 is essential for polarized cell motility and convergent extension
RT during mouse gastrulation.";
RL Development 136:2039-2048(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20704721; DOI=10.1186/1471-213x-10-87;
RA Paudyal A., Damrau C., Patterson V.L., Ermakov A., Formstone C.,
RA Lalanne Z., Wells S., Lu X., Norris D.P., Dean C.H., Henderson D.J.,
RA Murdoch J.N.;
RT "The novel mouse mutant, chuzhoi, has disruption of Ptk7 protein and
RT exhibits defects in neural tube, heart and lung development and abnormal
RT planar cell polarity in the ear.";
RL BMC Dev. Biol. 10:87-87(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1056, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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).
CC -!- FUNCTION: Inactive tyrosine kinase involved in Wnt signaling pathway.
CC Component of both the non-canonical (also known as the Wnt/planar cell
CC polarity signaling) and the canonical Wnt signaling pathway. Functions
CC in cell adhesion, cell migration, cell polarity, proliferation, actin
CC cytoskeleton reorganization and apoptosis. Has a role in embryogenesis,
CC epithelial tissue organization and angiogenesis.
CC {ECO:0000269|PubMed:15229603, ECO:0000269|PubMed:19439496,
CC ECO:0000269|PubMed:20704721}.
CC -!- SUBUNIT: Interacts with CTNNB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell junction {ECO:0000250}. Note=Colocalizes with MMP14 at cell
CC junctions. Also localizes at the leading edge of migrating cells.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in lung and un-pregnant
CC uterus among adult tissues, and in the tail, limbs, somites, gut and
CC craniofacial regions among embryonic tissues.
CC {ECO:0000269|PubMed:15019986}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- PTM: MMP14 cleaves PTK7 between Pro-613 and Leu-614 generating an N-
CC terminal soluble (70 kDa) fragment and a membrane C-terminal (50 kDa)
CC fragment. Proteolysis by MMP14 regulates PTK7 function in non-canonical
CC Wnt signaling pathway. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice die perinatally and display
CC craniorachischisis, a severe form of neural tube defect in which the
CC neural tube fails to close from the midbrain hindbrain boundary to the
CC base of the spine. Chuzhoi mutants also display disruption of planar
CC cell polarity in the inner ear, and defective heart and lung
CC development. {ECO:0000269|PubMed:15229603, ECO:0000269|PubMed:19439496,
CC ECO:0000269|PubMed:20704721}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27800.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF531873; AAQ10071.1; -; mRNA.
DR EMBL; AY303976; AAQ73496.1; -; Genomic_DNA.
DR EMBL; AK018379; BAE43251.1; -; mRNA.
DR EMBL; AK053044; BAC35248.1; -; mRNA.
DR EMBL; AK163135; BAE37208.1; -; mRNA.
DR EMBL; BC027800; AAH27800.1; ALT_INIT; mRNA.
DR EMBL; BC076578; AAH76578.1; -; mRNA.
DR EMBL; AB055408; BAC53806.1; -; mRNA.
DR CCDS; CCDS37637.1; -.
DR RefSeq; NP_780377.1; NM_175168.4.
DR AlphaFoldDB; Q8BKG3; -.
DR SMR; Q8BKG3; -.
DR BioGRID; 214723; 8.
DR STRING; 10090.ENSMUSP00000043703; -.
DR GlyConnect; 2391; 1 N-Linked glycan (2 sites).
DR GlyGen; Q8BKG3; 10 sites, 1 N-linked glycan (2 sites).
DR iPTMnet; Q8BKG3; -.
DR PhosphoSitePlus; Q8BKG3; -.
DR SwissPalm; Q8BKG3; -.
DR CPTAC; non-CPTAC-3932; -.
DR MaxQB; Q8BKG3; -.
DR PaxDb; Q8BKG3; -.
DR PeptideAtlas; Q8BKG3; -.
DR PRIDE; Q8BKG3; -.
DR ProteomicsDB; 301934; -.
DR Antibodypedia; 1008; 593 antibodies from 38 providers.
DR DNASU; 71461; -.
DR Ensembl; ENSMUST00000044442; ENSMUSP00000043703; ENSMUSG00000023972.
DR GeneID; 71461; -.
DR KEGG; mmu:71461; -.
DR UCSC; uc008cth.2; mouse.
DR CTD; 5754; -.
DR MGI; MGI:1918711; Ptk7.
DR VEuPathDB; HostDB:ENSMUSG00000023972; -.
DR eggNOG; KOG1026; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT00940000157908; -.
DR HOGENOM; CLU_012268_0_0_1; -.
DR InParanoid; Q8BKG3; -.
DR OMA; VPTPQVW; -.
DR OrthoDB; 530072at2759; -.
DR PhylomeDB; Q8BKG3; -.
DR TreeFam; TF326835; -.
DR BioGRID-ORCS; 71461; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Ptk7; mouse.
DR PRO; PR:Q8BKG3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BKG3; protein.
DR Bgee; ENSMUSG00000023972; Expressed in embryonic post-anal tail and 124 other tissues.
DR Genevisible; Q8BKG3; MM.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0003401; P:axis elongation; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
DR GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
DR GO; GO:0060026; P:convergent extension; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:MGI.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0060484; P:lung-associated mesenchyme development; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IGI:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IGI:MGI.
DR Gene3D; 2.60.40.10; -; 7.
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 InterPro; IPR013106; Ig_V-set.
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 Pfam; PF07679; I-set; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 7.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 7.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1062
FT /note="Inactive tyrosine-protein kinase 7"
FT /id="PRO_0000260435"
FT TOPO_DOM 23..696
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..1062
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..112
FT /note="Ig-like C2-type 1"
FT DOMAIN 120..210
FT /note="Ig-like C2-type 2"
FT DOMAIN 217..309
FT /note="Ig-like C2-type 3"
FT DOMAIN 301..399
FT /note="Ig-like C2-type 4"
FT DOMAIN 404..489
FT /note="Ig-like C2-type 5"
FT DOMAIN 495..578
FT /note="Ig-like C2-type 6"
FT DOMAIN 570..672
FT /note="Ig-like C2-type 7"
FT DOMAIN 788..1058
FT /note="Protein kinase; inactive"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 728..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..1062
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 1039..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 613..614
FT /note="Cleavage; by MMP14"
FT /evidence="ECO:0000250"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 142..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 238..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 335..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 425..473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 516..562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 605..656
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 818
FT /note="L -> R (in Ref. 4; BAC53806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1062 AA; 117532 MW; 138E25198A21E6A1 CRC64;
MGARPLTLLR ALLLPLLAGA QAAIVFIKEP SSQDALQGRR ALLRCEVEAP DPVHVYWLLN
GVPVQDTERR FAQGSSLSFA AVDRLQDSGA FQCVARDNVT GEEVRSTNAS FNIKWIEAGP
VVLKHPASEA EIQPQTQVTL RCHIDGHPRP TYQWFRDGTP LSDDQSTHTV SSRERNLTLR
PASPEHSGLY SCCAHNAFGQ ACSSQNFTLS VADESFARVV LAPQDVVVAR NEEAMFHCQF
SAQPPPSLQW VFEDETPITN RSRPPHLRRA VVFANGSLLL TQVRPRNAGV YRCIGQGQRG
PPIVLEATLH LAEIEDMLPF EPRVFIAGDE ERVTCPAPQG LPTPSVWWEH AGVPLPAHGR
VHQKGLELVF VTIAESDTGV YTCHASNLAG QRRQDVNITV ATVPTWLRKP QDSQLEEGKP
GYLHCLTQAT PKPTVIWYRN QMLISEDSRF EVSKNGTLRI NSVEVYDGTL YRCVSSTPAG
SIEAQARVQV LEKLKFTPPP QPQQCMEFDK EATVPCSATG REKPTVKWVR ADGSSLPEWV
TDNAGTLHFA RVTRDDAGNY TCIASNEPQG QIRAHVQLTV AVFITFKVEP ERTTVYQGHT
ALLRCEAQGD PKPLIQWKGK DRILDPTKLG PRMHIFQNGS LVIHDVAPED SGSYTCIAGN
SCNIRHTEAP LLVVDKPVME DSEGPGSPPP YKMIQTIGLS VGAAVAYIIA VLGLMFYCKK
RCKAKRLQKQ PEGEEPEMEC LNGGPLQNGQ PSAEIQEEVA LTSLGSGPPA TNKRHSAGDR
MHFPRASLQP ITTLGKSEFG EVFLAKAQGV EEGATETLVL VKSLQSRDEQ QQLDFRREVE
MFGKLNHANV VRLLGLCREA EPHYMVLEYV DLGDLKQFLR ISKNKDEKLK SQPLSTKQKV
ALCSQVALGM EHLSNNRFVH KDLAARNCLI SAQRQVKVSA LGLSKDVYNS EYYHFRQAWV
PLRWMSPEAV LEGDFSTKSD VWAFGVLMWE VFTHGEMPHG GQADDEVLAD LQAGKARLPQ
PEGCPSKLYR LMQRCWAPNP KDRPSFSEIA STLGDSPADS KQ
