CSF3R_MOUSE
ID CSF3R_MOUSE Reviewed; 837 AA.
AC P40223; A2A8Y3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Granulocyte colony-stimulating factor receptor;
DE Short=G-CSF receptor;
DE Short=G-CSF-R;
DE AltName: CD_antigen=CD114;
DE Flags: Precursor;
GN Name=Csf3r; Synonyms=Csfgr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2158861; DOI=10.1016/0092-8674(90)90814-u;
RA Fukunaga R., Ishizaka-Ikeda E., Seto Y., Nagata S.;
RT "Expression cloning of a receptor for murine granulocyte colony-stimulating
RT factor.";
RL Cell 61:341-350(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP INTERACTION WITH CEACAM1.
RX PubMed=21029969; DOI=10.1016/j.immuni.2010.10.009;
RA Pan H., Shively J.E.;
RT "Carcinoembryonic antigen-related cell adhesion molecule-1 regulates
RT granulopoiesis by inhibition of granulocyte colony-stimulating factor
RT receptor.";
RL Immunity 33:620-631(2010).
RN [4]
RP STRUCTURE BY NMR OF 225-333.
RX PubMed=9187659; DOI=10.1038/nsb0697-498;
RA Yamasaki K., Naito S., Anaguchi H., Ohkubo T., Ota Y.;
RT "Solution structure of an extracellular domain containing the WSxWS motif
RT of the granulocyte colony-stimulating factor receptor and its interaction
RT with ligand.";
RL Nat. Struct. Biol. 4:498-504(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 120-334 IN COMPLEX WITH CSF3,
RP SUBUNIT, GLYCOSYLATION AT ASN-129, AND DISULFIDE BONDS.
RX PubMed=10537111; DOI=10.1038/44394;
RA Aritomi M., Kunishima N., Okamoto T., Kuroki R., Ota Y., Morikawa K.;
RT "Atomic structure of the GCSF-receptor complex showing a new cytokine-
RT receptor recognition scheme.";
RL Nature 401:713-717(1999).
CC -!- FUNCTION: Receptor for granulocyte colony-stimulating factor (CSF3). In
CC addition it may function in some adhesion or recognition events at the
CC cell surface.
CC -!- SUBUNIT: Homodimer. The dimeric receptor binds two CSF3 molecules.
CC Interacts with CEACAM1; down-regulates the CSF3R-STAT3 pathway through
CC recruitment of PTPN6 that dephosphorylates CSF3R (PubMed:21029969).
CC {ECO:0000269|PubMed:10537111, ECO:0000269|PubMed:21029969}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Found in bone marrow.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q99062}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; M58288; AAA37673.1; -; mRNA.
DR EMBL; AL627101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18640.1; -.
DR PIR; A34898; A34898.
DR RefSeq; NP_031808.2; NM_007782.3.
DR RefSeq; XP_006502771.1; XM_006502708.3.
DR RefSeq; XP_006502772.1; XM_006502709.2.
DR RefSeq; XP_006502773.1; XM_006502710.3.
DR RefSeq; XP_006502774.1; XM_006502711.3.
DR RefSeq; XP_006502775.1; XM_006502712.3.
DR RefSeq; XP_006502776.1; XM_006502713.2.
DR RefSeq; XP_006502777.1; XM_006502714.2.
DR RefSeq; XP_011238723.1; XM_011240421.2.
DR RefSeq; XP_011238724.1; XM_011240422.2.
DR RefSeq; XP_017175433.1; XM_017319944.1.
DR PDB; 1CD9; X-ray; 2.80 A; B/D=120-334.
DR PDB; 1CTO; NMR; -; A=228-333.
DR PDB; 1GCF; NMR; -; A=228-333.
DR PDB; 1PGR; X-ray; 3.50 A; B/D/F/H=120-334.
DR PDBsum; 1CD9; -.
DR PDBsum; 1CTO; -.
DR PDBsum; 1GCF; -.
DR PDBsum; 1PGR; -.
DR AlphaFoldDB; P40223; -.
DR SMR; P40223; -.
DR BioGRID; 198935; 3.
DR DIP; DIP-61167N; -.
DR ELM; P40223; -.
DR IntAct; P40223; 1.
DR STRING; 10090.ENSMUSP00000101768; -.
DR GlyGen; P40223; 11 sites.
DR iPTMnet; P40223; -.
DR PhosphoSitePlus; P40223; -.
DR MaxQB; P40223; -.
DR PaxDb; P40223; -.
DR PRIDE; P40223; -.
DR ProteomicsDB; 277903; -.
DR Antibodypedia; 4479; 658 antibodies from 40 providers.
DR DNASU; 12986; -.
DR Ensembl; ENSMUST00000030673; ENSMUSP00000030673; ENSMUSG00000028859.
DR Ensembl; ENSMUST00000106162; ENSMUSP00000101768; ENSMUSG00000028859.
DR GeneID; 12986; -.
DR KEGG; mmu:12986; -.
DR UCSC; uc008usd.3; mouse.
DR CTD; 1441; -.
DR MGI; MGI:1339755; Csf3r.
DR VEuPathDB; HostDB:ENSMUSG00000028859; -.
DR eggNOG; ENOG502QT3H; Eukaryota.
DR GeneTree; ENSGT00940000158915; -.
DR HOGENOM; CLU_017990_0_0_1; -.
DR InParanoid; P40223; -.
DR OMA; WKPSLYI; -.
DR OrthoDB; 144839at2759; -.
DR PhylomeDB; P40223; -.
DR TreeFam; TF338122; -.
DR Reactome; R-MMU-449836; Other interleukin signaling.
DR Reactome; R-MMU-9674555; Signaling by CSF3 (G-CSF).
DR Reactome; R-MMU-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR BioGRID-ORCS; 12986; 1 hit in 72 CRISPR screens.
DR EvolutionaryTrace; P40223; -.
DR PRO; PR:P40223; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P40223; protein.
DR Bgee; ENSMUSG00000028859; Expressed in granulocyte and 69 other tissues.
DR Genevisible; P40223; MM.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0051916; F:granulocyte colony-stimulating factor binding; IPI:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IGI:MGI.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 6.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR010457; IgC2-like_lig-bd.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF06328; Lep_receptor_Ig; 1.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..837
FT /note="Granulocyte colony-stimulating factor receptor"
FT /id="PRO_0000010875"
FT TOPO_DOM 26..626
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..837
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..118
FT /note="Ig-like C2-type"
FT DOMAIN 126..231
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 236..331
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 334..433
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 434..529
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 530..624
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 319..323
FT /note="WSXWS motif"
FT MOTIF 658..666
FT /note="Box 1 motif"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10537111"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..52
FT /evidence="ECO:0000250"
FT DISULFID 46..102
FT /evidence="ECO:0000250"
FT DISULFID 132..143
FT /evidence="ECO:0000269|PubMed:10537111"
FT DISULFID 168..219
FT /evidence="ECO:0000269|PubMed:10537111"
FT DISULFID 178..187
FT /evidence="ECO:0000269|PubMed:10537111"
FT DISULFID 249..296
FT /evidence="ECO:0000269|PubMed:10537111"
FT DISULFID 267..310
FT /evidence="ECO:0000269|PubMed:10537111"
FT CONFLICT 379
FT /note="S -> N (in Ref. 1; AAA37673)"
FT /evidence="ECO:0000305"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:1CD9"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:1CD9"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1CD9"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1CD9"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1GCF"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:1CTO"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:1CD9"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 265..275
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 304..315
FT /evidence="ECO:0007829|PDB:1CD9"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1CD9"
SQ SEQUENCE 837 AA; 93379 MW; F46E9D62A3DC4C3F CRC64;
MVGLGACTLT GVTLIFLLLP RSLESCGHIE ISPPVVRLGD PVLASCTISP NCSKLDQQAK
ILWRLQDEPI QPGDRQHHLP DGTQESLITL PHLNYTQAFL FCLVPWEDSV QLLDQAELHA
GYPPASPSNL SCLMHLTTNS LVCQWEPGPE THLPTSFILK SFRSRADCQY QGDTIPDCVA
KKRQNNCSIP RKNLLLYQYM AIWVQAENML GSSESPKLCL DPMDVVKLEP PMLQALDIGP
DVVSHQPGCL WLSWKPWKPS EYMEQECELR YQPQLKGANW TLVFHLPSSK DQFELCGLHQ
APVYTLQMRC IRSSLPGFWS PWSPGLQLRP TMKAPTIRLD TWCQKKQLDP GTVSVQLFWK
PTPLQEDSGQ IQGYLLSWSS PDHQGQDIHL CNTTQLSCIF LLPSEAQNVT LVAYNKAGTS
SPTTVVFLEN EGPAVTGLHA MAQDLNTIWV DWEAPSLLPQ GYLIEWEMSS PSYNNSYKSW
MIEPNGNITG ILLKDNINPF QLYRITVAPL YPGIVGPPVN VYTFAGERAP PHAPALHLKH
VGTTWAQLEW VPEAPRLGMI PLTHYTIFWA DAGDHSFSVT LNISLHDFVL KHLEPASLYH
VYLMATSRAG STNSTGLTLR TLDPSDLNIF LGILCLVLLS TTCVVTWLCC KRRGKTSFWS
DVPDPAHSSL SSWLPTIMTE ETFQLPSFWD SSVPSITKIT ELEEDKKPTH WDSESSGNGS
LPALVQAYVL QGDPREISNQ SQPPSRTGDQ VLYGQVLESP TSPGVMQYIR SDSTQPLLGG
PTPSPKSYEN IWFHSRPQET FVPQPPNQED DCVFGPPFDF PLFQGLQVHG VEEQGGF
