FER_RAT
ID FER_RAT Reviewed; 823 AA.
AC P09760; F1MA12;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Tyrosine-protein kinase Fer;
DE EC=2.7.10.2;
DE AltName: Full=Proto-oncogene c-Fer;
DE AltName: Full=Tyrosine-protein kinase FLK;
DE AltName: Full=p94-Fer;
GN Name=Fer; Synonyms=Fert2, Flk;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 501-823.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=2485255;
RA Letwin K., Yee S.P., Pawson T.;
RT "Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned
RT using anti-phosphotyrosine antibody.";
RL Oncogene 3:621-627(1988).
RN [3]
RP FUNCTION IN SYNAPSE ORGANIZATION AND SYNAPTIC TRANSMISSION.
RX PubMed=19047464; DOI=10.1083/jcb.200807188;
RA Lee S.H., Peng I.F., Ng Y.G., Yanagisawa M., Bamji S.X., Elia L.P.,
RA Balsamo J., Lilien J., Anastasiadis P.Z., Ullian E.M., Reichardt L.F.;
RT "Synapses are regulated by the cytoplasmic tyrosine kinase Fer in a pathway
RT mediated by p120catenin, Fer, SHP-2, and beta-catenin.";
RL J. Cell Biol. 183:893-908(2008).
RN [4]
RP INTERACTION WITH ARHGDIA.
RX PubMed=21122136; DOI=10.1186/1471-2091-11-48;
RA Fei F., Kweon S.M., Haataja L., De Sepulveda P., Groffen J.,
RA Heisterkamp N.;
RT "The Fer tyrosine kinase regulates interactions of Rho GDP-Dissociation
RT Inhibitor alpha with the small GTPase Rac.";
RL BMC Biochem. 11:48-48(2010).
CC -!- FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface
CC receptors for growth factors and plays a role in the regulation of the
CC actin cytoskeleton, microtubule assembly, lamellipodia formation, cell
CC adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT,
CC PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-
CC kappa-B and cell proliferation. May play a role in the regulation of
CC the mitotic cell cycle. Plays a role in the insulin receptor signaling
CC pathway and in activation of phosphatidylinositol 3-kinase. Acts
CC downstream of the activated FCER1 receptor and plays a role in FCER1
CC (high affinity immunoglobulin epsilon receptor)-mediated signaling in
CC mast cells. Plays a role in the regulation of mast cell degranulation.
CC Plays a role in leukocyte recruitment and diapedesis in response to
CC bacterial lipopolysaccharide (LPS). Plays a role in neuronal cell death
CC after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1,
CC PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate
CC STAT3, but the biological relevance of this clearly depends on cell
CC type and stimulus (By similarity). Plays a role in synapse
CC organization, trafficking of synaptic vesicles, the generation of
CC excitatory postsynaptic currents and neuron-neuron synaptic
CC transmission. {ECO:0000250, ECO:0000269|PubMed:19047464}.
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=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Homotrimer. Interacts with IRS1, JAK1, NRP1, PIK3R1, PLEC and
CC TMF1. Interacts with PPP1CA and regulates its phosphorylation at 'Thr-
CC 320'. Interacts with CTNND1, EGFR, FLT3, PECAM1, PDGFR and STAT3.
CC Interacts (via SH2 domain) with CTTN. Interacts with HSP90; this
CC stabilizes phosphorylated FER and protects FER against proteasomal
CC degradation. Component of a complex that contains at least FER, CTTN
CC and PTK2/FAK1 (By similarity). Interacts with ARHGDIA. {ECO:0000250,
CC ECO:0000269|PubMed:21122136}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection
CC {ECO:0000250}. Cell junction {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cell cortex
CC {ECO:0000250}. Note=Associated with the chromatin. Detected on
CC microtubules in polarized and motile vascular endothelial cells.
CC Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1
CC and CTNND1 at nascent cell-cell contacts (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The coiled coil domains mediate homooligomerization and are
CC required for location at microtubules. {ECO:0000250}.
CC -!- DOMAIN: The N-terminal region including the first coiled coil domain
CC mediates interaction with phosphoinositide-containing membranes.
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated; this leads to proteasomal degradation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; X13412; CAA31778.1; -; mRNA.
DR PIR; S04328; S04328.
DR RefSeq; XP_008765589.1; XM_008767367.2.
DR RefSeq; XP_008765592.1; XM_008767370.2.
DR AlphaFoldDB; P09760; -.
DR SMR; P09760; -.
DR IntAct; P09760; 3.
DR STRING; 10116.ENSRNOP00000021758; -.
DR ChEMBL; CHEMBL4523172; -.
DR iPTMnet; P09760; -.
DR PhosphoSitePlus; P09760; -.
DR PaxDb; P09760; -.
DR PRIDE; P09760; -.
DR Ensembl; ENSRNOT00000097737; ENSRNOP00000090379; ENSRNOG00000015898.
DR GeneID; 301737; -.
DR CTD; 2241; -.
DR RGD; 1306273; Fer.
DR eggNOG; KOG0194; Eukaryota.
DR GeneTree; ENSGT00940000154997; -.
DR HOGENOM; CLU_005265_0_0_1; -.
DR InParanoid; P09760; -.
DR OrthoDB; 556386at2759; -.
DR TreeFam; TF315363; -.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR PRO; PR:P09760; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Genevisible; P09760; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0045098; C:type III intermediate filament; IPI:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045296; F:cadherin binding; IPI:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:RGD.
DR GO; GO:0070097; F:delta-catenin binding; IPI:RGD.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0045295; F:gamma-catenin binding; IPI:RGD.
DR GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:RGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IPI:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0034333; P:adherens junction assembly; IEP:RGD.
DR GO; GO:0120179; P:adherens junction disassembly; IEP:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; ISO:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISS:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0050904; P:diapedesis; ISS:UniProtKB.
DR GO; GO:0035426; P:extracellular matrix-cell signaling; ISS:UniProtKB.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007281; P:germ cell development; IEP:RGD.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase; ISS:UniProtKB.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISO:RGD.
DR GO; GO:0038109; P:Kit signaling pathway; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; ISS:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010762; P:regulation of fibroblast migration; ISO:RGD.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0043304; P:regulation of mast cell degranulation; IBA:GO_Central.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0036119; P:response to platelet-derived growth factor; ISS:UniProtKB.
DR GO; GO:0060009; P:Sertoli cell development; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; ISO:RGD.
DR CDD; cd07686; F-BAR_Fer; 1.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR028539; Fer.
DR InterPro; IPR037452; Fer_F-BAR.
DR InterPro; IPR035849; Fes/Fps/Fer_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016250; Tyr-prot_kinase_Fes/Fps.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418:SF227; PTHR24418:SF227; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PIRSF; PIRSF000632; TyrPK_fps; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell junction; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Kinase; Lipid-binding; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW SH2 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation.
FT CHAIN 1..823
FT /note="Tyrosine-protein kinase Fer"
FT /id="PRO_0000088093"
FT DOMAIN 1..259
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 461..551
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 564..815
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..300
FT /note="Important for interaction with membranes containing
FT phosphoinositides"
FT /evidence="ECO:0000250"
FT COILED 123..185
FT /evidence="ECO:0000255"
FT COILED 301..382
FT /evidence="ECO:0000255"
FT ACT_SITE 685
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 570..578
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 402
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16591"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16591"
FT MOD_RES 616
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P70451"
FT MOD_RES 715
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P70451"
FT CONFLICT 501
FT /note="G -> R (in Ref. 2; CAA31778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 823 AA; 94314 MW; CA4F31E375F747DA CRC64;
MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC NQVDKDSTVQ
VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSYVGIHQQ
IEAEMIKVTK TELEKLKSSY RQLIKEMNSA KEKYKEALAK GKETEKAKER CDKATMKLHM
LHNQYVLALK GAQLHQSQYY DTTLPLLLDS VQKMQEEMIK ALKGIFDEYS EITSLVTEEI
VNVHKEIQMS VDQIDPSTEY NDFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL
TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES SETCAKKSDI VLLLGQKQAL
EELKQSVQQL RCTEAKCAAQ KELLEQKVQE NDGKEPPPVV NYEEDARSVT SMERKERLSK
FESIRHSIAG IIKSPKSVLG SSTQLSDVIS VGEKPLAEHD WYHGAIPRIE AQELLKQQGD
FLVRESHGKP GEYVLSVYSD GQRRHFIIQF VDNLYRFEGT GFSNIPQLID HHFNTKQVIT
KKSGVVLLNP IPKDKKWVLN HEDVSLGELL GKGNFGEVYK GTLKDKTPVA VKTCKEDLPQ
ELKIKFLQEA KILKQYDHPN IVKLIGVCTQ RQPVYIIMEL VPGGDFLSFL RKRKDELKLK
QLVRFSLDVA AGMLYLEGKN CIHRDLAARN CLVGENNTLK ISDFGMSRQE DGGVYSSSGL
KQIPIKWTAP EALNYGRYSS ESDVWSFGIL LWETFSLGVC PYPGMTNQQA REQVERGYRM
SAPQNCPEEI FTIMMKCWDY KPENRPKFSD LHKELTAIKK KIT
