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Database: UniProt
Entry: P40223
LinkDB: P40223
Original site: P40223 
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   29-SEP-2021, entry version 171.
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   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; 659 antibodies.
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; CGSPFIP; -.
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; 0 hits in 61 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 126 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:0097186; P:amelogenesis; IEA:Ensembl.
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
//
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