TIE1_MOUSE
ID TIE1_MOUSE Reviewed; 1134 AA.
AC Q06806; Q811F4; Q8BGI2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Tyrosine-protein kinase receptor Tie-1;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=Tie1; Synonyms=Tie, Tie-1;
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].
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=8415706; DOI=10.1073/pnas.90.20.9355;
RA Sato T.N., Qin Y., Kozak C.A., Andus K.L.;
RT "Tie-1 and tie-2 define another class of putative receptor tyrosine kinase
RT genes expressed in early embryonic vascular system.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9355-9358(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/cJ; TISSUE=Bone marrow;
RA Krivsov A.V., Ershler M.A., Visser J.W.M., Belyavsky A.V.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Fetal liver;
RX PubMed=8395828; DOI=10.1006/bbrc.1993.2045;
RA Iwama A., Hamaguchi I., Hashiyama M., Murayama Y., Yasunaga K., Suda T.;
RT "Molecular cloning and characterization of mouse TIE and TEK receptor
RT tyrosine kinase genes and their expression in hematopoietic stem cells.";
RL Biochem. Biophys. Res. Commun. 195:301-309(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=7655012;
RA Korhonen J., Lahtinen I., Halmekyto M., Alhonen L., Janne J., Dumont D.,
RA Alitalo K.;
RT "Endothelial-specific gene expression directed by the tie gene promoter in
RT vivo.";
RL Blood 86:1828-1835(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE OF 221-352 AND 740-890.
RX PubMed=1384789;
RA Korhonen J., Partanen J., Armstrong E., Vaahtokari A., Elenius K.,
RA Jalkanen M., Alitalo K.;
RT "Enhanced expression of the tie receptor tyrosine kinase in endothelial
RT cells during neovascularization.";
RL Blood 80:2548-2555(1992).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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: Transmembrane tyrosine-protein kinase that may modulate
CC TEK/TIE2 activity and contribute to the regulation of angiogenesis.
CC {ECO:0000250}.
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 -!- SUBUNIT: Heterodimer with TEK/TIE2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in developing vascular
CC endothelial cells. Abundantly expressed in lung and heart, moderately
CC in brain, liver and kidney, and weakly in thymus, spleen and testis.
CC {ECO:0000269|PubMed:8395828}.
CC -!- PTM: Phosphorylated on tyrosine residues in response to ANGPT1, most
CC likely by TEK/TIE2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Tie subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X71425; CAA50556.1; -; mRNA.
DR EMBL; X80764; CAA56739.1; -; mRNA.
DR EMBL; X73960; CAA52148.1; -; mRNA.
DR EMBL; AK052192; BAC34876.1; -; mRNA.
DR EMBL; AK052413; BAC34979.1; -; mRNA.
DR EMBL; AL627212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046452; AAH46452.2; -; mRNA.
DR EMBL; S79346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18553.1; -.
DR PIR; JN0711; JN0711.
DR RefSeq; NP_035717.2; NM_011587.2.
DR AlphaFoldDB; Q06806; -.
DR SMR; Q06806; -.
DR IntAct; Q06806; 1.
DR MINT; Q06806; -.
DR STRING; 10090.ENSMUSP00000037129; -.
DR BindingDB; Q06806; -.
DR ChEMBL; CHEMBL2034800; -.
DR GlyGen; Q06806; 5 sites.
DR iPTMnet; Q06806; -.
DR PhosphoSitePlus; Q06806; -.
DR CPTAC; non-CPTAC-3623; -.
DR MaxQB; Q06806; -.
DR PaxDb; Q06806; -.
DR PeptideAtlas; Q06806; -.
DR PRIDE; Q06806; -.
DR ProteomicsDB; 259025; -.
DR Antibodypedia; 32289; 729 antibodies from 39 providers.
DR DNASU; 21846; -.
DR Ensembl; ENSMUST00000047421; ENSMUSP00000037129; ENSMUSG00000033191.
DR GeneID; 21846; -.
DR KEGG; mmu:21846; -.
DR UCSC; uc008ukh.1; mouse.
DR CTD; 7075; -.
DR MGI; MGI:99906; Tie1.
DR VEuPathDB; HostDB:ENSMUSG00000033191; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000157693; -.
DR HOGENOM; CLU_008888_0_0_1; -.
DR InParanoid; Q06806; -.
DR OMA; AKVWWRL; -.
DR OrthoDB; 707342at2759; -.
DR PhylomeDB; Q06806; -.
DR TreeFam; TF317568; -.
DR BRENDA; 2.7.10.1; 3474.
DR BioGRID-ORCS; 21846; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Tie1; mouse.
DR PRO; PR:Q06806; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q06806; protein.
DR Bgee; ENSMUSG00000033191; Expressed in cardiac muscle of left ventricle and 195 other tissues.
DR ExpressionAtlas; Q06806; baseline and differential.
DR Genevisible; Q06806; MM.
DR GO; GO:0016021; C:integral component of membrane; ISM:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0060854; P:branching involved in lymph vessel morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0060836; P:lymphatic endothelial cell differentiation; IMP:BHF-UCL.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI.
DR GO; GO:0045026; P:plasma membrane fusion; IMP:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0001936; P:regulation of endothelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:1901201; P:regulation of extracellular matrix assembly; IMP:BHF-UCL.
DR GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
DR GO; GO:0048771; P:tissue remodeling; IMP:BHF-UCL.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0001570; P:vasculogenesis; ISO:MGI.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR000742; EGF-like_dom.
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; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF00047; ig; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; ATP-binding; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..22
FT CHAIN 23..1134
FT /note="Tyrosine-protein kinase receptor Tie-1"
FT /id="PRO_0000024472"
FT TOPO_DOM 23..755
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 781..1134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..123
FT /note="Ig-like C2-type 1"
FT DOMAIN 212..254
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 256..301
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 303..343
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 349..440
FT /note="Ig-like C2-type 2"
FT DOMAIN 444..543
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 546..638
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 642..736
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 835..1114
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 975
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 841..849
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 866
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1003
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 226..235
FT /evidence="ECO:0000250"
FT DISULFID 229..242
FT /evidence="ECO:0000250"
FT DISULFID 244..253
FT /evidence="ECO:0000250"
FT DISULFID 266..276
FT /evidence="ECO:0000250"
FT DISULFID 270..289
FT /evidence="ECO:0000250"
FT DISULFID 291..300
FT /evidence="ECO:0000250"
FT DISULFID 313..325
FT /evidence="ECO:0000250"
FT DISULFID 319..331
FT /evidence="ECO:0000250"
FT DISULFID 333..342
FT /evidence="ECO:0000250"
FT CONFLICT 307
FT /note="G -> D (in Ref. 1; CAA50556/CAA56739, 3; CAA52148
FT and 6; AAH46452)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="R -> L (in Ref. 1; CAA50556)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="G -> D (in Ref. 1; CAA50556/CAA56739, 3; CAA52148
FT and 6; AAH46452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1134 AA; 124583 MW; 9669098A843B36F2 CRC64;
MVWWGSSLLL PTLFLASHVG ASVDLTLLAN LRITDPQRFF LTCVSGEAGA GRSSDPPLLL
EKDDRIVRTF PPGQPLYLAR NGSHQVTLRG FSKPSDLVGV FSCVGGAGAR RTRVLYVHNS
PGAHLFPDKV THTVNKGDTA VLSAHVHKEK QTDVIWKNNG SYFNTLDWQE ADDGRFQLQL
QNVQPPSSGI YSATYLEASP LGSAFFRLIV RGCGAGRWGP GCVKDCPGCL HGGVCHDHDG
ECVCPPGFTG TRCEQACREG RFGQSCQEQC PGTAGCRGLT FCLPDPYGCS CGSGWRGSQC
QEACAPGHFG ADCRLQCQCQ NGGTCDRFSG CVCPSGWHGV HCEKSDRIPQ ILSMATEVEF
NIGTMPRINC AAAGNPFPVR GSMKLRKPDG TMLLSTKVIV EPDRTTAEFE VPSLTLGDSG
FWECRVSTSG GQDSRRFKVN VKVPPVPLTA PRLLAKQSRQ LVVSPLVSFS GDGPISSVRL
HYRPQDSTIA WSAIVVDPSE NVTLMNLKPK TGYNVRVQLS RPGEGGEGGW GPSALMTTDC
PEPLLQPWLE SWHVEGPDRL RVSWSLPSVP LSGDGFLLRL WDGARGQERR ENISFPQART
ALLTGLTPGT HYQLDVRLYH CTLLGPASPP AHVHLPPSGP PAPRHLHAQA LSDSEIQLMW
QHPEAPSGPI SKYIVEIQVA GGSGDPQWMD VDRPEETSII VRGLNASTRY LFRVRASVQG
LGDWSNTVEE ATLGNGLQSE GPVRESRAAE EGLDQQLVLA VVGSVSATCL TILAALLALV
CIRRSCLHRR RTFTYQSGSG EETILQFSSG TLTLTRRPKP QPEPLSYPVL EWEDITFEDL
IGEGNFGQVI RAMIKKDGLK MNAAIKMLKE YASENDHRDF AGELEVLCKL GHHPNIINLL
GACENRGYLY IAIEYAPYGN LLDFLRKSRV LETDPAFARE HGTASTLSSR QLLRFASDAA
NGMQYLSEKQ FIHRDLAARN VLVGENLASK IADFGLSRGE EVYVKKTMGR LPVRWMAIES
LNYSVYTTKS DVWSFGVLLW EIVSLGGTPY CGMTCAELYE KLPQGYRMEQ PRNCDDEVYE
LMRQCWRDRP YERPPFAQIA LQLGRMLEAR KAYVNMSLFE NFTYAGIDAT AEEA
