ID SRC_CHICK Reviewed; 533 AA.
AC P00523; Q90992; Q90993; Q91343; Q91345; Q92013; Q98915;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 24-JAN-2024, entry version 243.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=6299580; DOI=10.1016/0092-8674(83)90073-9;
RA Takeya T., Hanafusa H.;
RT "Structure and sequence of the cellular gene homologous to the RSV src gene
RT and the mechanism for generating the transforming virus.";
RL Cell 32:881-890(1983).
RN [2]
RP ERRATUM OF PUBMED:6299580, AND SEQUENCE REVISION TO 526.
RA Takeya T., Hanafusa H.;
RL Cell 34:319-319(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Pectoralis muscle;
RX PubMed=2115117; DOI=10.1128/mcb.10.8.4068-4079.1990;
RA Dorai T., Wang L.-H.;
RT "An alternative non-tyrosine protein kinase product of the c-src gene in
RT chicken skeletal muscle.";
RL Mol. Cell. Biol. 10:4068-4079(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PHOSPHORYLATION AT TYR-416 AND
RP TYR-436.
RX PubMed=8856081; DOI=10.1111/j.1432-1033.1996.0756h.x;
RA Weijland A., Neubauer G., Courtneidge S.A., Mann M., Wierenga R.K.,
RA Superti-Furga G.;
RT "The purification and characterization of the catalytic domain of Src
RT expressed in Schizosaccharomyces pombe. Comparison of unphosphorylated and
RT tyrosine phosphorylated species.";
RL Eur. J. Biochem. 240:756-764(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=6292480; DOI=10.1128/jvi.44.1.12-18.1982;
RA Takeya T., Hanafusa H.;
RT "DNA sequence of the viral and cellular src gene of chickens. II.
RT Comparison of the src genes of two strains of Avian sarcoma virus and of
RT the cellular homolog.";
RL J. Virol. 44:12-18(1982).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-19 AND 485-534 (ISOFORM 1).
RX PubMed=1712905; DOI=10.1128/mcb.11.8.4165-4176.1991;
RA Dorai T., Levy J.B., Kang L., Brugge J.S., Wang L.-H.;
RT "Analysis of cDNAs of the proto-oncogene c-src: heterogeneity in 5' exons
RT and possible mechanism for the genesis of the 3' end of v-src.";
RL Mol. Cell. Biol. 11:4165-4176(1991).
RN [7]
RP ATP-BINDING SITE.
RX PubMed=6431300; DOI=10.1038/310589a0;
RA Kamps M.P., Taylor S.S., Sefton B.M.;
RT "Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent
RT protein kinase have homologous ATP-binding sites.";
RL Nature 310:589-592(1984).
RN [8]
RP PHOSPHORYLATION AT SER-12.
RX PubMed=2996780; DOI=10.1016/0092-8674(85)90281-8;
RA Gould K.L., Woodgett J.R., Cooper J.A., Buss J.E., Shalloway D., Hunter T.;
RT "Protein kinase C phosphorylates pp60src at a novel site.";
RL Cell 42:849-857(1985).
RN [9]
RP PHOSPHORYLATION AT TYR-416.
RX PubMed=6273838; DOI=10.1073/pnas.78.10.6013;
RA Smart J.E., Oppermann H., Czernilofsky A.P., Purchio A.F., Erikson R.L.,
RA Bishop J.M.;
RT "Characterization of sites for tyrosine phosphorylation in the transforming
RT protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue
RT (pp60c-src).";
RL Proc. Natl. Acad. Sci. U.S.A. 78:6013-6017(1981).
RN [10]
RP PHOSPHORYLATION AT TYR-527.
RX PubMed=2420005; DOI=10.1126/science.2420005;
RA Cooper J.A., Gould K.L., Cartwright C.A., Hunter T.;
RT "Tyr527 is phosphorylated in pp60c-src: implications for regulation.";
RL Science 231:1431-1434(1986).
RN [11]
RP PHOSPHORYLATION AT THR-34; THR-46 AND SER-72.
RX PubMed=2470512; DOI=10.1016/0092-8674(89)90791-5;
RA Shenoy S., Choi J.K., Bagrodia S., Copeland T.D., Maller J.L.,
RA Shalloway D.;
RT "Purified maturation promoting factor phosphorylates pp60c-src at the sites
RT phosphorylated during fibroblast mitosis.";
RL Cell 57:763-774(1989).
RN [12]
RP FUNCTION IN THE NGF AND FGF SIGNALING PATHWAYS.
RX PubMed=1717492; DOI=10.1083/jcb.115.3.809;
RA Kremer N.E., D'Arcangelo G., Thomas S.M., DeMarco M., Brugge J.S.,
RA Halegoua S.;
RT "Signal transduction by nerve growth factor and fibroblast growth factor in
RT PC12 cells requires a sequence of src and ras actions.";
RL J. Cell Biol. 115:809-819(1991).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=1378446; DOI=10.1083/jcb.118.2.321;
RA Kaplan K.B., Swedlow J.R., Varmus H.E., Morgan D.O.;
RT "Association of p60c-src with endosomal membranes in mammalian
RT fibroblasts.";
RL J. Cell Biol. 118:321-333(1992).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PXN.
RX PubMed=8325872; DOI=10.1016/s0021-9258(18)82425-5;
RA Weng Z., Taylor J.A., Turner C.E., Brugge J.S., Seidel-Dugan C.;
RT "Detection of Src homology 3-binding proteins, including paxillin, in
RT normal and v-Src-transformed Balb/c 3T3 cells.";
RL J. Biol. Chem. 268:14956-14963(1993).
RN [15]
RP FUNCTION IN THE EDN1 SIGNALING PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=8550628; DOI=10.1074/jbc.271.1.77;
RA Simonson M.S., Wang Y., Herman W.H.;
RT "Nuclear signaling by endothelin-1 requires Src protein-tyrosine kinases.";
RL J. Biol. Chem. 271:77-82(1996).
RN [16]
RP INTERACTION WITH AFAP-110.
RX PubMed=9655255;
RX DOI=10.1002/(sici)1098-2744(199806)22:2<110::aid-mc6>3.0.co;2-q;
RA Guappone A.C., Weimer T., Flynn D.C.;
RT "Formation of a stable src-AFAP-110 complex through either an amino-
RT terminal or a carboxy-terminal SH2-binding motif.";
RL Mol. Carcinog. 22:110-119(1998).
RN [17]
RP INTERACTION WITH GJA1.
RX PubMed=15492000; DOI=10.1074/jbc.m409552200;
RA Sorgen P.L., Duffy H.S., Sahoo P., Coombs W., Delmar M., Spray D.C.;
RT "Structural changes in the carboxyl terminus of the gap junction protein
RT connexin43 indicates signaling between binding domains for c-Src and zonula
RT occludens-1.";
RL J. Biol. Chem. 279:54695-54701(2004).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF TYR-527.
RX PubMed=19307596; DOI=10.1083/jcb.200810155;
RA Zhang Y., Tu Y., Zhao J., Chen K., Wu C.;
RT "Reversion-induced LIM interaction with Src reveals a novel Src
RT inactivation cycle.";
RL J. Cell Biol. 184:785-792(2009).
RN [19]
RP S-NITROSYLATION AT CYS-498, AND MUTAGENESIS OF CYS-498.
RX PubMed=19948721; DOI=10.1074/jbc.m109.059782;
RA Rahman M.A., Senga T., Ito S., Hyodo T., Hasegawa H., Hamaguchi M.;
RT "S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric
RT oxide-mediated cell invasion.";
RL J. Biol. Chem. 285:3806-3814(2010).
RN [20]
RP REVIEW ON FUNCTION.
RX PubMed=8672527; DOI=10.1016/0304-419x(96)00003-0;
RA Brown M.T., Cooper J.A.;
RT "Regulation, substrates and functions of src.";
RL Biochim. Biophys. Acta 1287:121-149(1996).
RN [21]
RP REVIEW ON FUNCTION.
RX PubMed=9442882; DOI=10.1146/annurev.cellbio.13.1.513;
RA Thomas S.M., Brugge J.S.;
RT "Cellular functions regulated by Src family kinases.";
RL Annu. Rev. Cell Dev. Biol. 13:513-609(1997).
RN [22]
RP REVIEW ON FUNCTION.
RX PubMed=11964124; DOI=10.1007/s00018-002-8438-2;
RA Ma Y.C., Huang X.Y.;
RT "Novel regulation and function of Src tyrosine kinase.";
RL Cell. Mol. Life Sci. 59:456-462(2002).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 83-533.
RX PubMed=9405157; DOI=10.1006/jmbi.1997.1426;
RA Williams J.C., Weijland A., Gonfloni S., Thompson A., Courtneidge S.A.,
RA Superti-Furga G., Wierenga R.K.;
RT "The 2.35 A crystal structure of the inactivated form of chicken Src: a
RT dynamic molecule with multiple regulatory interactions.";
RL J. Mol. Biol. 274:757-775(1997).
RN [24]
RP STRUCTURE BY NMR OF 81-140.
RX PubMed=8504863; DOI=10.1016/0014-5793(93)81538-b;
RA Yu H., Rosen M.K., Schreiber S.L.;
RT "1H and 15N assignments and secondary structure of the Src SH3 domain.";
RL FEBS Lett. 324:87-92(1993).
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
CC (PubMed:1717492, PubMed:8550628). Involved in anchorage-independent
CC cell growth (PubMed:19307596). {ECO:0000250|UniProtKB:P12931,
CC ECO:0000269|PubMed:1717492, ECO:0000269|PubMed:19307596,
CC ECO:0000269|PubMed:8550628, ECO:0000305|PubMed:11964124,
CC ECO:0000305|PubMed:8672527, ECO:0000305|PubMed:9442882}.
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-527 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with polyoma virus middle T antigen. Interacts
CC with AFAP-110. Interacts with GJA1 and PXN.
CC {ECO:0000269|PubMed:15492000, ECO:0000269|PubMed:8325872,
CC ECO:0000269|PubMed:9655255}.
CC -!- INTERACTION:
CC P00523; Q90738: AFAP1; NbExp=3; IntAct=EBI-848039, EBI-8562073;
CC P00523; Q00944: PTK2; NbExp=3; IntAct=EBI-848039, EBI-2896409;
CC P00523; Q9QWY8-1: Asap1; Xeno; NbExp=3; IntAct=EBI-848039, EBI-698517;
CC P00523; Q9QWY8-2: Asap1; Xeno; NbExp=2; IntAct=EBI-848039, EBI-698524;
CC P00523; Q9NZA1: CLIC5; Xeno; NbExp=2; IntAct=EBI-848039, EBI-5658997;
CC P00523; P41240: CSK; Xeno; NbExp=7; IntAct=EBI-848039, EBI-1380630;
CC P00523; Q9Y4D1: DAAM1; Xeno; NbExp=3; IntAct=EBI-848039, EBI-2817289;
CC P00523; P03372: ESR1; Xeno; NbExp=2; IntAct=EBI-848039, EBI-78473;
CC P00523; O88703: Hcn2; Xeno; NbExp=5; IntAct=EBI-848039, EBI-771231;
CC P00523; P18052: Ptpra; Xeno; NbExp=2; IntAct=EBI-848039, EBI-6597520;
CC P00523; P18433: PTPRA; Xeno; NbExp=4; IntAct=EBI-848039, EBI-2609645;
CC P00523; Q9QWI6-2: Srcin1; Xeno; NbExp=2; IntAct=EBI-848039, EBI-775607;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1378446,
CC ECO:0000269|PubMed:8325872}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P05480}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P05480}. Endosome membrane
CC {ECO:0000269|PubMed:1378446}; Peripheral membrane protein
CC {ECO:0000269|PubMed:1378446}. Nucleus {ECO:0000269|PubMed:8550628}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8325872}. Cell junction,
CC focal adhesion {ECO:0000250|UniProtKB:P05480}. Cytoplasm, perinuclear
CC region {ECO:0000250|UniProtKB:P12931}. Note=Localizes to focal adhesion
CC sites following integrin engagement (By similarity). Localization to
CC focal adhesion sites requires myristoylation and the SH3 domain.
CC {ECO:0000250|UniProtKB:P05480, ECO:0000250|UniProtKB:P12931}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P00523-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P00523-2; Sequence=VSP_011844, VSP_011845;
CC -!- TISSUE SPECIFICITY: Expressed to high levels, and with a high degree of
CC kinase activity, in certain fully differentiated cells such as neurons,
CC platelets and macrophages. Isoform 1 is widely expressed. Isoform 2 is
CC expressed only in the muscle.
CC -!- PTM: Myristoylated at Gly-2, and this is essential for targeting to
CC membranes. {ECO:0000250}.
CC -!- PTM: Dephosphorylated at Tyr-527 by PTPRJ. Phosphorylated on Tyr-527 by
CC c-Src kinase (CSK). The phosphorylated form is termed pp60c-src.
CC Dephosphorylated by PTPRJ at Tyr-416. Normally maintained in an
CC inactive conformation with the SH2 domain engaged with Tyr-527, the SH3
CC domain engaged with the SH2-kinase linker, and Tyr-416
CC dephosphorylated. Dephosphorylation of Tyr-527 as a result of protein
CC tyrosine phosphatase (PTP) action disrupts the intramolecular
CC interaction between the SH2 domain and Tyr-527, Tyr-416 can then become
CC autophosphorylated, resulting in SRC activation. Phosphorylation of
CC Tyr-527 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 its kinase
CC activity. {ECO:0000269|PubMed:19948721}.
CC -!- MISCELLANEOUS: [Isoform 2]: Membrane-bound. {ECO:0000305}.
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; V00402; CAA23696.1; -; Genomic_DNA.
DR EMBL; J00908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M57290; AAA49078.1; -; mRNA.
DR EMBL; S43604; AAD13831.1; -; mRNA.
DR EMBL; S43616; AAD13835.1; -; mRNA.
DR EMBL; S43587; AAD13830.1; -; mRNA.
DR EMBL; S43609; AAD13832.1; -; mRNA.
DR EMBL; S43614; AAD13834.1; -; mRNA.
DR EMBL; S43579; AAB19353.2; -; mRNA.
DR PIR; A00630; TVCHS.
DR RefSeq; NP_990788.2; NM_205457.2. [P00523-1]
DR RefSeq; XP_015151834.1; XM_015296348.1. [P00523-1]
DR PDB; 1F1W; X-ray; 2.10 A; A=145-247.
DR PDB; 1F2F; X-ray; 1.70 A; A=145-247.
DR PDB; 1NLO; NMR; -; C=81-140.
DR PDB; 1NLP; NMR; -; C=81-140.
DR PDB; 1P13; X-ray; 1.63 A; A/B=145-246.
DR PDB; 1PRL; NMR; -; C=77-140.
DR PDB; 1PRM; NMR; -; C=77-140.
DR PDB; 1RLP; NMR; -; C=77-140.
DR PDB; 1RLQ; NMR; -; C=77-140.
DR PDB; 1SRL; NMR; -; A=77-140.
DR PDB; 1SRM; NMR; -; A=77-140.
DR PDB; 2HWO; X-ray; 2.50 A; A/B=251-533.
DR PDB; 2HWP; X-ray; 2.48 A; A/B=251-533.
DR PDB; 2OIQ; X-ray; 2.07 A; A/B=251-533.
DR PDB; 2PTK; X-ray; 2.35 A; A=81-533.
DR PDB; 2QI8; X-ray; 2.32 A; A/B=251-533.
DR PDB; 2QLQ; X-ray; 2.33 A; A/B=251-533.
DR PDB; 2QQ7; X-ray; 2.38 A; A/B=251-533.
DR PDB; 3D7T; X-ray; 2.90 A; B=251-533.
DR PDB; 3D7U; X-ray; 4.11 A; B/D=260-523.
DR PDB; 3DQW; X-ray; 2.02 A; A/B/C/D=251-533.
DR PDB; 3DQX; X-ray; 2.30 A; A/B=251-533.
DR PDB; 3EL7; X-ray; 2.80 A; A=251-533.
DR PDB; 3EL8; X-ray; 2.30 A; A/B=251-533.
DR PDB; 3EN4; X-ray; 2.55 A; A/B=251-533.
DR PDB; 3EN5; X-ray; 2.66 A; A/B=251-533.
DR PDB; 3EN6; X-ray; 2.39 A; A/B=251-533.
DR PDB; 3EN7; X-ray; 2.81 A; A/B=251-533.
DR PDB; 3F3T; X-ray; 2.50 A; A/B=251-533.
DR PDB; 3F3U; X-ray; 2.50 A; A/B=251-533.
DR PDB; 3F3V; X-ray; 2.60 A; A/B=251-533.
DR PDB; 3F3W; X-ray; 2.60 A; A/B=251-533.
DR PDB; 3F6X; X-ray; 2.35 A; A/B/C/D=251-533.
DR PDB; 3FJ5; X-ray; 1.65 A; A/B=85-140.
DR PDB; 3G5D; X-ray; 2.20 A; A/B=251-533.
DR PDB; 3G6G; X-ray; 2.31 A; A/B=251-533.
DR PDB; 3G6H; X-ray; 2.35 A; A/B=251-533.
DR PDB; 3GEQ; X-ray; 2.20 A; A/B=251-533.
DR PDB; 3LOK; X-ray; 2.48 A; A/B=251-533.
DR PDB; 3OEZ; X-ray; 2.40 A; A/B=251-533.
DR PDB; 3OF0; X-ray; 2.70 A; A/B=251-533.
DR PDB; 3QLF; X-ray; 2.75 A; A/B=251-533.
DR PDB; 3QLG; X-ray; 2.75 A; A/B=251-533.
DR PDB; 3SVV; X-ray; 2.20 A; A/B=251-533.
DR PDB; 3TZ7; X-ray; 3.30 A; A/B=251-533.
DR PDB; 3TZ8; X-ray; 2.70 A; A/B=251-533.
DR PDB; 3TZ9; X-ray; 3.10 A; A/B=251-533.
DR PDB; 3U4W; X-ray; 1.90 A; A=259-533.
DR PDB; 3U51; X-ray; 2.24 A; A/B=259-533.
DR PDB; 3UQF; X-ray; 2.27 A; A/B=251-533.
DR PDB; 3UQG; X-ray; 2.20 A; A/B=251-533.
DR PDB; 4AGW; X-ray; 2.60 A; A/B=251-533.
DR PDB; 4DGG; X-ray; 2.65 A; A/B=251-533.
DR PDB; 4FIC; X-ray; 2.50 A; A/B=251-533.
DR PDB; 4HVU; X-ray; 0.98 A; A=85-141.
DR PDB; 4HVV; X-ray; 1.10 A; A=85-140.
DR PDB; 4HVW; X-ray; 0.98 A; A=85-141.
DR PDB; 4JZ3; X-ray; 1.85 A; A=85-141.
DR PDB; 4JZ4; X-ray; 1.56 A; A/B=85-141.
DR PDB; 4LE9; X-ray; 1.34 A; A=85-141.
DR PDB; 4LGG; X-ray; 2.41 A; A/B=264-533.
DR PDB; 4LGH; X-ray; 2.84 A; A/B=257-533.
DR PDB; 4MCV; X-ray; 2.73 A; A/B=256-533.
DR PDB; 4O2P; X-ray; 2.10 A; A/B=251-533.
DR PDB; 4OML; X-ray; 1.60 A; A=85-141.
DR PDB; 4OMM; X-ray; 1.90 A; A=85-140.
DR PDB; 4OMN; X-ray; 1.50 A; A=85-140.
DR PDB; 4OMO; X-ray; 1.04 A; A/B=85-141.
DR PDB; 4OMP; X-ray; 2.00 A; A=85-139.
DR PDB; 4OMQ; X-ray; 2.00 A; A=85-140.
DR PDB; 4QT7; X-ray; 1.55 A; A=85-141.
DR PDB; 4RTU; X-ray; 2.45 A; A=85-141.
DR PDB; 4RTV; X-ray; 1.37 A; A=85-141.
DR PDB; 4RTW; X-ray; 1.24 A; A/C=85-141.
DR PDB; 4RTX; X-ray; 1.32 A; A/B/C/D=85-141.
DR PDB; 4RTY; X-ray; 1.28 A; A=85-141.
DR PDB; 4RTZ; X-ray; 0.98 A; A=85-141.
DR PDB; 4U5J; X-ray; 2.26 A; A/B=251-533.
DR PDB; 4YBJ; X-ray; 2.61 A; A/B=251-533.
DR PDB; 4YBK; X-ray; 2.50 A; A=251-533.
DR PDB; 5BMM; X-ray; 2.50 A; A/B=251-533.
DR PDB; 5D10; X-ray; 2.70 A; A/B=251-533.
DR PDB; 5D11; X-ray; 2.30 A; A/B=251-533.
DR PDB; 5D12; X-ray; 3.00 A; A/B=251-533.
DR PDB; 5EC7; X-ray; 1.65 A; A/B/C=85-140.
DR PDB; 5ECA; X-ray; 1.16 A; A=85-141.
DR PDB; 5I11; X-ray; 1.95 A; A=85-141.
DR PDB; 5J5S; X-ray; 2.15 A; A/B=251-533.
DR PDB; 5K9I; X-ray; 2.50 A; A/B=251-533.
DR PDB; 5OAV; X-ray; 0.95 A; A/C=85-141.
DR PDB; 5OB0; X-ray; 1.17 A; A=85-141.
DR PDB; 5OB1; X-ray; 1.17 A; A=85-141.
DR PDB; 5OB2; X-ray; 1.80 A; A/C=85-141.
DR PDB; 5SWH; X-ray; 2.50 A; A/B=252-533.
DR PDB; 5SYS; X-ray; 2.80 A; A/B=251-533.
DR PDB; 5T0P; X-ray; 2.50 A; A/B=251-533.
DR PDB; 5TEH; X-ray; 2.99 A; A/B=251-533.
DR PDB; 5XP5; X-ray; 2.10 A; A/B=251-533.
DR PDB; 5XP7; X-ray; 2.01 A; A/B=251-533.
DR PDB; 6HVE; X-ray; 1.90 A; A/B=251-533.
DR PDB; 6HVF; X-ray; 2.10 A; A/B=251-533.
DR PDB; 6L8L; X-ray; 2.89 A; A/B/C/D=251-533.
DR PDB; 6WIW; X-ray; 2.30 A; A/B=251-533.
DR PDB; 6XVM; X-ray; 0.90 A; A/B/C/D=82-141.
DR PDB; 6XVN; X-ray; 1.70 A; A/B=82-141.
DR PDB; 6XVO; X-ray; 1.70 A; A=82-141.
DR PDB; 6XX2; X-ray; 1.25 A; A=85-141.
DR PDB; 6XX3; X-ray; 1.36 A; A=85-141.
DR PDB; 6XX4; X-ray; 1.05 A; A=85-141.
DR PDB; 6XX5; X-ray; 1.30 A; A=85-141.
DR PDB; 7A30; X-ray; 1.67 A; A=82-141.
DR PDB; 7A31; X-ray; 0.94 A; A/B=82-141.
DR PDB; 7A32; X-ray; 1.15 A; A/B/C/D=82-141.
DR PDB; 7A33; X-ray; 0.96 A; A/B=82-141.
DR PDB; 7A34; X-ray; 1.85 A; A=82-141.
DR PDB; 7A35; X-ray; 1.31 A; A/B=82-141.
DR PDB; 7A36; X-ray; 1.50 A; A/B=82-141.
DR PDB; 7A37; X-ray; 1.52 A; A/B=82-141.
DR PDB; 7A38; X-ray; 1.62 A; A/B=82-141.
DR PDB; 7A39; X-ray; 1.65 A; A/B=82-141.
DR PDB; 7A3A; X-ray; 1.80 A; A=82-141.
DR PDB; 7A3B; X-ray; 1.91 A; A=82-141.
DR PDB; 7A3C; X-ray; 1.80 A; A/B/C/D=81-141.
DR PDB; 7A3D; X-ray; 2.20 A; A/B=82-141.
DR PDB; 7A3E; X-ray; 1.52 A; A=81-141.
DR PDB; 7AH3; X-ray; 1.95 A; A/B=251-533.
DR PDB; 7D57; X-ray; 2.10 A; A/B=251-533.
DR PDB; 7D5O; X-ray; 2.69 A; A/B=251-533.
DR PDB; 7NER; X-ray; 1.55 A; A=81-141.
DR PDB; 7NES; X-ray; 1.35 A; A=81-141.
DR PDB; 7NET; X-ray; 1.50 A; A/B=81-141.
DR PDB; 7PVW; X-ray; 1.50 A; A/B=82-141.
DR PDB; 7PVX; X-ray; 1.43 A; A/C=82-141.
DR PDB; 7PVY; X-ray; 1.40 A; A=81-141.
DR PDB; 7PVZ; X-ray; 2.00 A; A/B=81-141.
DR PDB; 7PW0; X-ray; 1.70 A; A/B/C/D/E/F/G/H=82-141.
DR PDB; 7WF5; X-ray; 1.80 A; A/B=251-533.
DR PDBsum; 1F1W; -.
DR PDBsum; 1F2F; -.
DR PDBsum; 1NLO; -.
DR PDBsum; 1NLP; -.
DR PDBsum; 1P13; -.
DR PDBsum; 1PRL; -.
DR PDBsum; 1PRM; -.
DR PDBsum; 1RLP; -.
DR PDBsum; 1RLQ; -.
DR PDBsum; 1SRL; -.
DR PDBsum; 1SRM; -.
DR PDBsum; 2HWO; -.
DR PDBsum; 2HWP; -.
DR PDBsum; 2OIQ; -.
DR PDBsum; 2PTK; -.
DR PDBsum; 2QI8; -.
DR PDBsum; 2QLQ; -.
DR PDBsum; 2QQ7; -.
DR PDBsum; 3D7T; -.
DR PDBsum; 3D7U; -.
DR PDBsum; 3DQW; -.
DR PDBsum; 3DQX; -.
DR PDBsum; 3EL7; -.
DR PDBsum; 3EL8; -.
DR PDBsum; 3EN4; -.
DR PDBsum; 3EN5; -.
DR PDBsum; 3EN6; -.
DR PDBsum; 3EN7; -.
DR PDBsum; 3F3T; -.
DR PDBsum; 3F3U; -.
DR PDBsum; 3F3V; -.
DR PDBsum; 3F3W; -.
DR PDBsum; 3F6X; -.
DR PDBsum; 3FJ5; -.
DR PDBsum; 3G5D; -.
DR PDBsum; 3G6G; -.
DR PDBsum; 3G6H; -.
DR PDBsum; 3GEQ; -.
DR PDBsum; 3LOK; -.
DR PDBsum; 3OEZ; -.
DR PDBsum; 3OF0; -.
DR PDBsum; 3QLF; -.
DR PDBsum; 3QLG; -.
DR PDBsum; 3SVV; -.
DR PDBsum; 3TZ7; -.
DR PDBsum; 3TZ8; -.
DR PDBsum; 3TZ9; -.
DR PDBsum; 3U4W; -.
DR PDBsum; 3U51; -.
DR PDBsum; 3UQF; -.
DR PDBsum; 3UQG; -.
DR PDBsum; 4AGW; -.
DR PDBsum; 4DGG; -.
DR PDBsum; 4FIC; -.
DR PDBsum; 4HVU; -.
DR PDBsum; 4HVV; -.
DR PDBsum; 4HVW; -.
DR PDBsum; 4JZ3; -.
DR PDBsum; 4JZ4; -.
DR PDBsum; 4LE9; -.
DR PDBsum; 4LGG; -.
DR PDBsum; 4LGH; -.
DR PDBsum; 4MCV; -.
DR PDBsum; 4O2P; -.
DR PDBsum; 4OML; -.
DR PDBsum; 4OMM; -.
DR PDBsum; 4OMN; -.
DR PDBsum; 4OMO; -.
DR PDBsum; 4OMP; -.
DR PDBsum; 4OMQ; -.
DR PDBsum; 4QT7; -.
DR PDBsum; 4RTU; -.
DR PDBsum; 4RTV; -.
DR PDBsum; 4RTW; -.
DR PDBsum; 4RTX; -.
DR PDBsum; 4RTY; -.
DR PDBsum; 4RTZ; -.
DR PDBsum; 4U5J; -.
DR PDBsum; 4YBJ; -.
DR PDBsum; 4YBK; -.
DR PDBsum; 5BMM; -.
DR PDBsum; 5D10; -.
DR PDBsum; 5D11; -.
DR PDBsum; 5D12; -.
DR PDBsum; 5EC7; -.
DR PDBsum; 5ECA; -.
DR PDBsum; 5I11; -.
DR PDBsum; 5J5S; -.
DR PDBsum; 5K9I; -.
DR PDBsum; 5OAV; -.
DR PDBsum; 5OB0; -.
DR PDBsum; 5OB1; -.
DR PDBsum; 5OB2; -.
DR PDBsum; 5SWH; -.
DR PDBsum; 5SYS; -.
DR PDBsum; 5T0P; -.
DR PDBsum; 5TEH; -.
DR PDBsum; 5XP5; -.
DR PDBsum; 5XP7; -.
DR PDBsum; 6HVE; -.
DR PDBsum; 6HVF; -.
DR PDBsum; 6L8L; -.
DR PDBsum; 6WIW; -.
DR PDBsum; 6XVM; -.
DR PDBsum; 6XVN; -.
DR PDBsum; 6XVO; -.
DR PDBsum; 6XX2; -.
DR PDBsum; 6XX3; -.
DR PDBsum; 6XX4; -.
DR PDBsum; 6XX5; -.
DR PDBsum; 7A30; -.
DR PDBsum; 7A31; -.
DR PDBsum; 7A32; -.
DR PDBsum; 7A33; -.
DR PDBsum; 7A34; -.
DR PDBsum; 7A35; -.
DR PDBsum; 7A36; -.
DR PDBsum; 7A37; -.
DR PDBsum; 7A38; -.
DR PDBsum; 7A39; -.
DR PDBsum; 7A3A; -.
DR PDBsum; 7A3B; -.
DR PDBsum; 7A3C; -.
DR PDBsum; 7A3D; -.
DR PDBsum; 7A3E; -.
DR PDBsum; 7AH3; -.
DR PDBsum; 7D57; -.
DR PDBsum; 7D5O; -.
DR PDBsum; 7NER; -.
DR PDBsum; 7NES; -.
DR PDBsum; 7NET; -.
DR PDBsum; 7PVW; -.
DR PDBsum; 7PVX; -.
DR PDBsum; 7PVY; -.
DR PDBsum; 7PVZ; -.
DR PDBsum; 7PW0; -.
DR PDBsum; 7WF5; -.
DR AlphaFoldDB; P00523; -.
DR BMRB; P00523; -.
DR SMR; P00523; -.
DR BioGRID; 676691; 4.
DR DIP; DIP-449N; -.
DR ELM; P00523; -.
DR IntAct; P00523; 19.
DR MINT; P00523; -.
DR STRING; 9031.ENSGALP00000006117; -.
DR BindingDB; P00523; -.
DR ChEMBL; CHEMBL3655; -.
DR DrugCentral; P00523; -.
DR iPTMnet; P00523; -.
DR PaxDb; 9031-ENSGALP00000006117; -.
DR GeneID; 396442; -.
DR KEGG; gga:396442; -.
DR CTD; 6714; -.
DR VEuPathDB; HostDB:geneid_396442; -.
DR eggNOG; KOG0197; Eukaryota.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; P00523; -.
DR PhylomeDB; P00523; -.
DR TreeFam; TF351634; -.
DR BRENDA; 2.7.10.2; 1306.
DR Reactome; R-GGA-1227986; Signaling by ERBB2.
DR Reactome; R-GGA-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-GGA-1253288; Downregulation of ERBB4 signaling.
DR Reactome; R-GGA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-GGA-1433557; Signaling by SCF-KIT.
DR Reactome; R-GGA-1433559; Regulation of KIT signaling.
DR Reactome; R-GGA-177929; Signaling by EGFR.
DR Reactome; R-GGA-180292; GAB1 signalosome.
DR Reactome; R-GGA-186763; Downstream signal transduction.
DR Reactome; R-GGA-191650; Regulation of gap junction activity.
DR Reactome; R-GGA-2029481; FCGR activation.
DR Reactome; R-GGA-210990; PECAM1 interactions.
DR Reactome; R-GGA-354192; Integrin signaling.
DR Reactome; R-GGA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-GGA-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-GGA-389356; CD28 co-stimulation.
DR Reactome; R-GGA-389513; CTLA4 inhibitory signaling.
DR Reactome; R-GGA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-GGA-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-GGA-3928664; Ephrin signaling.
DR Reactome; R-GGA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-GGA-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-GGA-418594; G alpha (i) signalling events.
DR Reactome; R-GGA-430116; GP1b-IX-V activation signalling.
DR Reactome; R-GGA-437239; Recycling pathway of L1.
DR Reactome; R-GGA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-GGA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-GGA-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-GGA-5673000; RAF activation.
DR Reactome; R-GGA-5674135; MAP2K and MAPK activation.
DR Reactome; R-GGA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-GGA-69231; Cyclin D associated events in G1.
DR Reactome; R-GGA-8853659; RET signaling.
DR Reactome; R-GGA-8874081; MET activates PTK2 signaling.
DR Reactome; R-GGA-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-GGA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-GGA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-GGA-9603381; Activated NTRK3 signals through PI3K.
DR EvolutionaryTrace; P00523; -.
DR PRO; PR:P00523; -.
DR Proteomes; UP000000539; Chromosome 20.
DR Bgee; ENSGALG00000003855; Expressed in cerebellum and 12 other cell types or tissues.
DR ExpressionAtlas; P00523; baseline.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IDA: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:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0071253; F:connexin binding; IPI:CAFA.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
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:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR CDD; cd05071; PTKc_Src; 1.
DR CDD; cd10365; SH2_Src_Src; 1.
DR CDD; cd12008; SH3_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 3D-structure; Alternative splicing; ATP-binding; Cell adhesion; Cell cycle;
KW Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; Endosome; Immunity;
KW Kinase; Lipoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; S-nitrosylation; SH2 domain; SH3 domain; Transferase;
KW Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..533
FT /note="Proto-oncogene tyrosine-protein kinase Src"
FT /id="PRO_0000088144"
FT DOMAIN 81..142
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 148..245
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 267..520
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 273..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 12
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:2996780"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:2470512"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:2470512"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2470512"
FT MOD_RES 416
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:6273838,
FT ECO:0000269|PubMed:8856081"
FT MOD_RES 436
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8856081"
FT MOD_RES 498
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:19948721"
FT MOD_RES 527
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000269|PubMed:2420005"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 183..193
FT /note="AYCLSVSDFDN -> DPCIPLPSCLC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2115117"
FT /id="VSP_011844"
FT VAR_SEQ 194..533
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2115117"
FT /id="VSP_011845"
FT MUTAGEN 498
FT /note="C->A: Significant reduction in S-nitrosylation."
FT /evidence="ECO:0000269|PubMed:19948721"
FT MUTAGEN 527
FT /note="Y->F: Constitutively active."
FT /evidence="ECO:0000269|PubMed:19307596"
FT CONFLICT 301
FT /note="T -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="K -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:6XVM"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:6XVM"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:6XVM"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4LE9"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:6XVM"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:6XVM"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:6XVM"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6XVM"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6XVM"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2PTK"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1F1W"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:1P13"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2PTK"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1P13"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1P13"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:1P13"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1P13"
FT STRAND 196..206
FT /evidence="ECO:0007829|PDB:1P13"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1P13"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1P13"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:1P13"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1P13"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2PTK"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:3GEQ"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:7WF5"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:7WF5"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2QI8"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:7WF5"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:7WF5"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:7WF5"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 304..316
FT /evidence="ECO:0007829|PDB:7WF5"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:7WF5"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:7WF5"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 360..379
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:7WF5"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:7WF5"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:2QI8"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:3U4W"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:3U4W"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:5BMM"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 431..436
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 441..456
FT /evidence="ECO:0007829|PDB:7WF5"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:3U4W"
FT HELIX 468..476
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 489..498
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 509..517
FT /evidence="ECO:0007829|PDB:7WF5"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:7WF5"
SQ SEQUENCE 533 AA; 60010 MW; ABDB036F7D63C30A CRC64;
MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL
FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL SFKKGERLQI VNNTEGDWWL
AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT
KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR
LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL KGEMGKYLRL
PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ
GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERGYR
MPCPPECPES LHDLMCQCWR KDPEERPTFE YLQAFLEDYF TSTEPQYQPG ENL
//
