ID A0A8I5ZP95_RAT Unreviewed; 968 AA. AC A0A8I5ZP95; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 03-MAY-2023, entry version 6. DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902}; DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902}; GN Name=Csf1r {ECO:0000313|Ensembl:ENSRNOP00000079769.1, GN ECO:0000313|RGD:2425}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000079769.1, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000079769.1, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000079769.1, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000079769.1} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000079769.1}; RG Ensembl; RL Submitted (JAN-2023) to UniProtKB. 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=2.7.10.1; CC Evidence={ECO:0000256|ARBA:ARBA00001171}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. CC Membrane {ECO:0000256|ARBA:ARBA00004479, CC ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. CSF-1/PDGF receptor subfamily. CC {ECO:0000256|RuleBase:RU000311}. 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 Ensembl; ENSRNOT00000094400.1; ENSRNOP00000079769.1; ENSRNOG00000018414.8. DR RGD; 2425; Csf1r. DR GeneTree; ENSGT00940000155506; -. DR Proteomes; UP000002494; Chromosome 18. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0019955; F:cytokine binding; IEA:InterPro. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro. DR GO; GO:0048513; P:animal organ development; IEA:UniProt. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:InterPro. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR GO; GO:0048731; P:system development; IEA:UniProt. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro. DR CDD; cd05106; PTKc_CSF-1R; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 5. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR030658; CSF-1_receptor. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013151; Immunoglobulin. 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; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS. DR PANTHER; PTHR24416:SF47; MACROPHAGE COLONY-STIMULATING FACTOR 1 RECEPTOR; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF00047; ig; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PIRSF; PIRSF500947; CSF-1_receptor; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1. DR SMART; SM00409; IG; 5. DR SMART; SM00408; IGc2; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF48726; Immunoglobulin; 5. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50835; IG_LIKE; 4. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|PIRSR:PIRSR500947-51, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR500947-52}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319, KW ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00023137}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR500947-51, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A8I5ZP95}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Transferase {ECO:0000256|ARBA:ARBA00023137}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000311}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}. FT TRANSMEM 501..526 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 11..75 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 97..178 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 193..284 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 390..490 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 570..904 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 910..948 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 911..938 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 766 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR500947-50" FT BINDING 576..584 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51" FT BINDING 604 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51, FT ECO:0000256|PROSITE-ProRule:PRU10141" FT DISULFID 32..74 FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52" FT DISULFID 117..167 FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52" FT DISULFID 214..268 FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52" FT DISULFID 407..473 FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52" SQ SEQUENCE 968 AA; 108335 MW; 236C0EC953DB59B5 CRC64; MWIHDSSQGA PVIEPSGPEL VVEPGATVTL RCVSNGSVEW DGPISPYWTL DSESPGSILI TKNATFKNTG TYRCTELEDP MRGSTAIHLY VKDPVRPWNL LAQEVTVFEG QEAVLPCLIT DPTLKDSVSL VREWGRPVSR KTVYSFLPWR GFIIHKAKFL DSHTYMCKAV VNARESTSIG IRLKVNRAHP GPPHIILEPT KLVRIRGEAA QIVCSATHSE VEFNVILKRG DTKLEIPINS DFQDNAYKKV LTLNLNAVDF QDAGIYSCVA NNAAGSNTAT MNFQVVESAY LNLTSEQSLL QEVSVGENLD LTVIADAYPG LQRYNWTYLG PFFEDPHNLE FRTQWTTYSY SFKLHLNRVK PLEAGRYSLM AQNKAGWNNL TFELTLRYPP EVSVTWIPVN GSDVLLCDVS GYPQPNVTWM ECRGHTDRCD EAQASQVWDD TQPEVLSQKP FHRVILQSQL PIGTLKHNMT YVCRAHNNVG NSSQFFRAIS LGQSKQLPDE YLFTPVVVAC ISVMSLLVLL LLLLLYKYKQ KPKYQVRWKI IESYEGNNYT FIDPTQLPYN EKWEFPRNNL QFGKTLGAGA FGKVVEATAF GLGKEDAVLK VAVKMLKSTA HADEKEALMS ELKIMSHLGQ HENIVNLLGA CTHGGPVLVI TEYCCYGDLL NFLRRKAEAM LGPSLSPGQD PEGDSSYKNI HLEKKYVRRD SGFSSQGVDT YVEMRPVSTS SNDSFFKQDL DKEASRPLEL WDLLHFSSQV AQGMAFLASK NCIHRDVAAR NVLLTSGHVA KIGDFGLARD IMNDSNYVVK GNARLPVKWM APESIFDCVY TVQSDVWSYG ILLWEIFSLG LNPYPGILVN NKFYKLVKDG YQMAQPVFAP ENIYSIMQSC WDLEPTKRPT FQQICFLLQE QARLERREQD YANLPSSSSS SSSSSDSGGG SGGSSSEPEE ESSSEHLACC EPGDIAQPLL QPNNYQFC //