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   27-MAR-2024, entry version 133.
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.ENSDARP00000093618; -.
DR   PaxDb; 7955-ENSDARP00000097596; -.
DR   GeneID; 325084; -.
DR   KEGG; dre:325084; -.
DR   AGR; ZFIN:ZDB-GENE-030131-3809; -.
DR   CTD; 6714; -.
DR   ZFIN; ZDB-GENE-030131-3809; src.
DR   eggNOG; KOG0197; Eukaryota.
DR   HOGENOM; CLU_000288_7_2_1; -.
DR   InParanoid; Q1JPZ3; -.
DR   OrthoDB; 1614410at2759; -.
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-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; Chromosome 23.
DR   Bgee; ENSDARG00000008107; Expressed in tail bud paraxial mesoderm and 33 other cell types or 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:0004715; F:non-membrane spanning 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   CDD; cd05071; PTKc_Src; 1.
DR   CDD; cd10365; SH2_Src_Src; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR24418:SF53; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC; 1.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
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; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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
//