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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //