SRC_DANRE
ID SRC_DANRE Reviewed; 534 AA.
AC Q1JPZ3; Q6EWH0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Proto-oncogene tyrosine-protein kinase Src;
DE EC=2.7.10.2;
DE AltName: Full=Proto-oncogene c-Src;
DE AltName: Full=pp60c-src;
DE Short=p60-Src;
GN Name=src;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15815683; DOI=10.1038/sj.embor.7400386;
RA Jopling C., den Hertog J.;
RT "Fyn/Yes and non-canonical Wnt signalling converge on RhoA in vertebrate
RT gastrulation cell movements.";
RL EMBO Rep. 6:426-431(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH AMOTL2, AND MUTAGENESIS OF TYR-528.
RX PubMed=17293535; DOI=10.1242/dev.02782;
RA Huang H., Lu F.I., Jia S., Meng S., Cao Y., Wang Y., Ma W., Yin K., Wen Z.,
RA Peng J., Thisse C., Thisse B., Meng A.;
RT "Amotl2 is essential for cell movements in zebrafish embryo and regulates
RT c-Src translocation.";
RL Development 134:979-988(2007).
CC -!- FUNCTION: Non-receptor protein tyrosine kinase which is activated
CC following engagement of many different classes of cellular receptors
CC including immune response receptors, integrins and other adhesion
CC receptors, receptor protein tyrosine kinases, G protein-coupled
CC receptors as well as cytokine receptors. Participates in signaling
CC pathways that control a diverse spectrum of biological activities
CC including gene transcription, immune response, cell adhesion, cell
CC cycle progression, apoptosis, migration, and transformation. Due to
CC functional redundancy between members of the SRC kinase family,
CC identification of the specific role of each src kinase is very
CC difficult. Src appears to be one of the primary kinases activated
CC following engagement of receptors and plays a role in the activation of
CC other protein tyrosine kinase (PTK) families. Receptor clustering or
CC dimerization leads to recruitment of src to the receptor complexes
CC where it phosphorylates the tyrosine residues within the receptor
CC cytoplasmic domains. Plays an important role in the regulation of
CC cytoskeletal organization through phosphorylation of specific
CC substrates involved in this process (Probable). When cells adhere via
CC focal adhesions to the extracellular matrix, signals are transmitted by
CC integrins into the cell resulting in tyrosine phosphorylation of a
CC number of focal adhesion proteins, including ptk2/fak1 and paxillin
CC (pxn) (By similarity). Also active at the sites of cell-cell contact
CC adherens junctions and at gap junctions. Implicated in the regulation
CC of pre-mRNA-processing (Probable). Might be involved not only in
CC mediating the transduction of mitogenic signals at the level of the
CC plasma membrane but also in controlling progression through the cell
CC cycle via interaction with regulatory proteins in the nucleus. Involved
CC in anchorage-independent cell growth (By similarity).
CC {ECO:0000250|UniProtKB:P12931, ECO:0000305}.
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 -!- ACTIVITY REGULATION: Becomes activated when its major tyrosine
CC phosphorylation site is not phosphorylated. It can also be activated by
CC point mutations as well as by truncations at the C-terminal end or by
CC other mutations. Heme regulates its activity by enhancing the
CC phosphorylation on Tyr-528 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with amotl2; this interaction promotes the
CC translocation of phosphorylated src to peripheral cell-matrix adhesion
CC sites. {ECO:0000269|PubMed:17293535}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P00523};
CC Lipid-anchor {ECO:0000250|UniProtKB:P05480}. Mitochondrion inner
CC membrane {ECO:0000250|UniProtKB:P05480}. Nucleus
CC {ECO:0000250|UniProtKB:P00523}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P00523}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:P05480}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P12931}. Note=Localizes to focal adhesion sites
CC following integrin engagement. Localization to focal adhesion sites
CC requires myristoylation and the SH3 domain.
CC {ECO:0000250|UniProtKB:P12931}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15815683}.
CC -!- DOMAIN: The SH2 and SH3 domains are important for the intramolecular
CC and intermolecular interactions that regulate catalytic activity,
CC localization, and substrate recruitment. {ECO:0000250}.
CC -!- PTM: Myristoylated at Gly-2, and this is essential for targeting to
CC membranes. {ECO:0000250}.
CC -!- PTM: Dephosphorylated at Tyr-528 by PTPRJ. Phosphorylated on Tyr-528 by
CC c-Src kinase (CSK). The phosphorylated form is termed pp60c-src.
CC Dephosphorylated by PTPRJ at Tyr-417. Normally maintained in an
CC inactive conformation with the SH2 domain engaged with Tyr-528, the SH3
CC domain engaged with the SH2-kinase linker, and Tyr-417
CC dephosphorylated. Dephosphorylation of Tyr-528 as a result of protein
CC tyrosine phosphatase (PTP) action disrupts the intramolecular
CC interaction between the SH2 domain and Tyr-528, Tyr-417 can then become
CC autophosphorylated, resulting in SRC activation. Phosphorylation of
CC Tyr-528 by CSK allows this interaction to reform, resulting in SRC
CC inactivation (By similarity). {ECO:0000250}.
CC -!- PTM: S-nitrosylation is important for activation of kinase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AJ620750; CAF06181.1; -; mRNA.
DR EMBL; BX548066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU302205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116544; AAI16545.1; -; mRNA.
DR RefSeq; NP_001003837.2; NM_001003837.2.
DR AlphaFoldDB; Q1JPZ3; -.
DR SMR; Q1JPZ3; -.
DR STRING; 7955.ENSDARP00000097596; -.
DR PaxDb; Q1JPZ3; -.
DR PRIDE; Q1JPZ3; -.
DR Ensembl; ENSDART00000102843; ENSDARP00000093618; ENSDARG00000008107.
DR Ensembl; ENSDART00000184254; ENSDARP00000151348; ENSDARG00000008107.
DR GeneID; 325084; -.
DR KEGG; dre:325084; -.
DR CTD; 6714; -.
DR ZFIN; ZDB-GENE-030131-3809; src.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000158250; -.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; Q1JPZ3; -.
DR OMA; GMMNMEV; -.
DR OrthoDB; 539311at2759; -.
DR PhylomeDB; Q1JPZ3; -.
DR TreeFam; TF351634; -.
DR Reactome; R-DRE-1227986; Signaling by ERBB2.
DR Reactome; R-DRE-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-DRE-1253288; Downregulation of ERBB4 signaling.
DR Reactome; R-DRE-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DRE-1295596; Spry regulation of FGF signaling.
DR Reactome; R-DRE-1433557; Signaling by SCF-KIT.
DR Reactome; R-DRE-1433559; Regulation of KIT signaling.
DR Reactome; R-DRE-177929; Signaling by EGFR.
DR Reactome; R-DRE-180292; GAB1 signalosome.
DR Reactome; R-DRE-186763; Downstream signal transduction.
DR Reactome; R-DRE-191650; Regulation of gap junction activity.
DR Reactome; R-DRE-210990; PECAM1 interactions.
DR Reactome; R-DRE-354192; Integrin signaling.
DR Reactome; R-DRE-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-DRE-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-DRE-389356; CD28 co-stimulation.
DR Reactome; R-DRE-389513; CTLA4 inhibitory signaling.
DR Reactome; R-DRE-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DRE-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-DRE-3928664; Ephrin signaling.
DR Reactome; R-DRE-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-DRE-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-DRE-418594; G alpha (i) signalling events.
DR Reactome; R-DRE-418885; DCC mediated attractive signaling.
DR Reactome; R-DRE-430116; GP1b-IX-V activation signalling.
DR Reactome; R-DRE-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DRE-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-DRE-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-5673000; RAF activation.
DR Reactome; R-DRE-5674135; MAP2K and MAPK activation.
DR Reactome; R-DRE-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-DRE-69231; Cyclin D associated events in G1.
DR Reactome; R-DRE-8853659; RET signaling.
DR Reactome; R-DRE-8874081; MET activates PTK2 signaling.
DR Reactome; R-DRE-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-DRE-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-DRE-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DRE-9603381; Activated NTRK3 signals through PI3K.
DR PRO; PR:Q1JPZ3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000008107; Expressed in tail bud paraxial mesoderm and 33 other tissues.
DR ExpressionAtlas; Q1JPZ3; baseline and differential.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070851; F:growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0045453; P:bone resorption; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0036035; P:osteoclast development; IBA:GO_Central.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0043114; P:regulation of vascular permeability; IMP:ZFIN.
DR GO; GO:0001878; P:response to yeast; IDA:ZFIN.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 3.30.505.10; -; 1.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell adhesion; Cell cycle; Cell junction; Cell membrane;
KW Cytoplasm; Cytoskeleton; Kinase; Lipoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Myristate; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; S-nitrosylation; SH2 domain;
KW SH3 domain; Transferase; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..534
FT /note="Proto-oncogene tyrosine-protein kinase Src"
FT /id="PRO_0000418880"
FT DOMAIN 82..143
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 149..253
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 268..521
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 274..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 74
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250"
FT MOD_RES 185
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 417
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 417
FT /note="Phosphotyrosine; by FAK2"
FT /evidence="ECO:0000250"
FT MOD_RES 437
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 499
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 520
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 528
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT MUTAGEN 528
FT /note="Y->F: Lower affinity for AMOTL2-binding compared
FT with wild-type."
FT /evidence="ECO:0000269|PubMed:17293535"
FT CONFLICT 4
FT /note="V -> A (in Ref. 3; AAI16545)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="L -> M (in Ref. 3; AAI16545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 60147 MW; EC09B5A1BC01A38A CRC64;
MGGVKSKPKE LGQRSRSLDD GTGGHHHHTP NPTSFTPNRS PPVEGSRRGT QPNIINAEQA
LFGGVNSTTN SITSPNRIGI LGGVTTFVAL YDYESRTASD LSFRKGERLQ IVNNTEGDWW
LARSLTTGES GYIPSNYVAP SDSIQAEEWY FGKITRRDSE RLLLNLENRR GTFLVRESET
TKGAYCLSVL DYDNVKGLNV KHYKIRKLDS GGFYITSRTQ FSTLQQLVNH YRQHADGLCH
SLTDVCPVLK PPTQGLARDA WEIPRDSLRL DVKLGQGCFG EVWMGTWNGT TRVAIKTLKP
GTMSPEAFLQ EAQVMKKLRH EKLVQLYAVV SEEPIYIVTE YMGQGSLLDF LKGDMGKMLR
LPQLVDMASQ IASGMAYVER MNYVHRDLRA ANILVGDNLV CKVADFGLAR LIEDNEYTAR
QGAKFPIKWT APEAALYGRF TIKSDVWSFG ILLTELTTKG RVPYPGMVNR EVLDQVERGY
RMPCPAECPD SLHELMLTCW RKEPEERPTF EYLQGFLEDY FTSTEPQYQP GENL
