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Granulocyte colony-stimulating factor receptor (G-CSF receptor) (G-CSF-R) (CD antigen CD114)

 CSF3R_MOUSE             Reviewed;         837 AA.
P40223; A2A8Y3;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 155.
RecName: Full=Granulocyte colony-stimulating factor receptor;
Short=G-CSF receptor;
Short=G-CSF-R;
AltName: CD_antigen=CD114;
Flags: Precursor;
Name=Csf3r; Synonyms=Csfgr;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2158861; DOI=10.1016/0092-8674(90)90814-U;
Fukunaga R., Ishizaka-Ikeda E., Seto Y., Nagata S.;
"Expression cloning of a receptor for murine granulocyte colony-
stimulating factor.";
Cell 61:341-350(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
INTERACTION WITH CEACAM1.
PubMed=21029969; DOI=10.1016/j.immuni.2010.10.009;
Pan H., Shively J.E.;
"Carcinoembryonic antigen-related cell adhesion molecule-1 regulates
granulopoiesis by inhibition of granulocyte colony-stimulating factor
receptor.";
Immunity 33:620-631(2010).
[4]
STRUCTURE BY NMR OF 225-333.
PubMed=9187659; DOI=10.1038/nsb0697-498;
Yamasaki K., Naito S., Anaguchi H., Ohkubo T., Ota Y.;
"Solution structure of an extracellular domain containing the WSxWS
motif of the granulocyte colony-stimulating factor receptor and its
interaction with ligand.";
Nat. Struct. Biol. 4:498-504(1997).
[5]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 120-334 IN COMPLEX WITH CSF3,
SUBUNIT, GLYCOSYLATION AT ASN-129, AND DISULFIDE BONDS.
PubMed=10537111; DOI=10.1038/44394;
Aritomi M., Kunishima N., Okamoto T., Kuroki R., Ota Y., Morikawa K.;
"Atomic structure of the GCSF-receptor complex showing a new cytokine-
receptor recognition scheme.";
Nature 401:713-717(1999).
-!- FUNCTION: Receptor for granulocyte colony-stimulating factor
(CSF3). In addition it may function in some adhesion or
recognition events at the cell surface.
-!- SUBUNIT: Homodimer. The dimeric receptor binds two CSF3 molecules.
Interacts with CEACAM1; down-regulates the CSF3R-STAT3 pathway
through recruitment of PTPN6 that dephosphorylates CSF3R
(PubMed:21029969). {ECO:0000269|PubMed:10537111,
ECO:0000269|PubMed:21029969}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Found in bone marrow.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q99062}.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M58288; AAA37673.1; -; mRNA.
EMBL; AL627101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS18640.1; -.
PIR; A34898; A34898.
RefSeq; NP_031808.2; NM_007782.3.
RefSeq; XP_006502771.1; XM_006502708.3.
RefSeq; XP_006502772.1; XM_006502709.2.
RefSeq; XP_006502773.1; XM_006502710.3.
RefSeq; XP_006502774.1; XM_006502711.3.
RefSeq; XP_006502775.1; XM_006502712.3.
RefSeq; XP_006502776.1; XM_006502713.2.
RefSeq; XP_006502777.1; XM_006502714.2.
RefSeq; XP_011238723.1; XM_011240421.2.
RefSeq; XP_011238724.1; XM_011240422.2.
RefSeq; XP_017175433.1; XM_017319944.1.
UniGene; Mm.271701; -.
PDB; 1CD9; X-ray; 2.80 A; B/D=120-334.
PDB; 1CTO; NMR; -; A=228-333.
PDB; 1GCF; NMR; -; A=228-333.
PDB; 1PGR; X-ray; 3.50 A; B/D/F/H=120-334.
PDBsum; 1CD9; -.
PDBsum; 1CTO; -.
PDBsum; 1GCF; -.
PDBsum; 1PGR; -.
ProteinModelPortal; P40223; -.
SMR; P40223; -.
BioGrid; 198935; 3.
DIP; DIP-61167N; -.
ELM; P40223; -.
IntAct; P40223; 1.
STRING; 10090.ENSMUSP00000030673; -.
iPTMnet; P40223; -.
PhosphoSitePlus; P40223; -.
MaxQB; P40223; -.
PaxDb; P40223; -.
PRIDE; P40223; -.
Ensembl; ENSMUST00000030673; ENSMUSP00000030673; ENSMUSG00000028859.
Ensembl; ENSMUST00000106162; ENSMUSP00000101768; ENSMUSG00000028859.
GeneID; 12986; -.
KEGG; mmu:12986; -.
UCSC; uc008usd.3; mouse.
CTD; 1441; -.
MGI; MGI:1339755; Csf3r.
eggNOG; ENOG410IGHT; Eukaryota.
eggNOG; ENOG410XVIU; LUCA.
GeneTree; ENSGT00550000074436; -.
HOGENOM; HOG000231142; -.
HOVERGEN; HBG051130; -.
InParanoid; P40223; -.
KO; K05061; -.
OMA; YLRCDST; -.
OrthoDB; EOG091G01XM; -.
TreeFam; TF338122; -.
Reactome; R-MMU-449836; Other interleukin signaling.
EvolutionaryTrace; P40223; -.
PRO; PR:P40223; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028859; Expressed in 85 organ(s), highest expression level in blood.
Genevisible; P40223; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
GO; GO:0051916; F:granulocyte colony-stimulating factor binding; IPI:MGI.
GO; GO:0097186; P:amelogenesis; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
GO; GO:0045637; P:regulation of myeloid cell differentiation; IGI:MGI.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR010457; IgC2-like_lig-bd.
Pfam; PF00041; fn3; 1.
Pfam; PF06328; Lep_receptor_Ig; 1.
SMART; SM00060; FN3; 4.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF49265; SSF49265; 4.
PROSITE; PS50853; FN3; 5.
PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Complete proteome; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 837 Granulocyte colony-stimulating factor
receptor.
/FTId=PRO_0000010875.
TOPO_DOM 26 626 Extracellular. {ECO:0000255}.
TRANSMEM 627 650 Helical. {ECO:0000255}.
TOPO_DOM 651 837 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 118 Ig-like C2-type.
DOMAIN 126 231 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 236 331 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 334 433 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 434 529 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 530 624 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 319 323 WSXWS motif.
MOTIF 658 666 Box 1 motif.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10537111}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 474 474 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 487 487 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 582 582 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 613 613 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 26 52 {ECO:0000250}.
DISULFID 46 102 {ECO:0000250}.
DISULFID 132 143 {ECO:0000269|PubMed:10537111}.
DISULFID 168 219 {ECO:0000269|PubMed:10537111}.
DISULFID 178 187 {ECO:0000269|PubMed:10537111}.
DISULFID 249 296 {ECO:0000269|PubMed:10537111}.
DISULFID 267 310 {ECO:0000269|PubMed:10537111}.
CONFLICT 379 379 S -> N (in Ref. 1; AAA37673).
{ECO:0000305}.
STRAND 128 135 {ECO:0000244|PDB:1CD9}.
TURN 136 139 {ECO:0000244|PDB:1CD9}.
STRAND 140 146 {ECO:0000244|PDB:1CD9}.
STRAND 156 163 {ECO:0000244|PDB:1CD9}.
HELIX 166 168 {ECO:0000244|PDB:1CD9}.
STRAND 174 179 {ECO:0000244|PDB:1CD9}.
STRAND 186 190 {ECO:0000244|PDB:1CD9}.
HELIX 191 193 {ECO:0000244|PDB:1CD9}.
STRAND 200 208 {ECO:0000244|PDB:1CD9}.
STRAND 211 214 {ECO:0000244|PDB:1CD9}.
STRAND 218 220 {ECO:0000244|PDB:1CD9}.
HELIX 222 225 {ECO:0000244|PDB:1CD9}.
STRAND 227 229 {ECO:0000244|PDB:1GCF}.
STRAND 232 235 {ECO:0000244|PDB:1CD9}.
STRAND 242 244 {ECO:0000244|PDB:1CTO}.
STRAND 250 255 {ECO:0000244|PDB:1CD9}.
HELIX 258 260 {ECO:0000244|PDB:1CD9}.
STRAND 265 275 {ECO:0000244|PDB:1CD9}.
STRAND 281 288 {ECO:0000244|PDB:1CD9}.
STRAND 290 295 {ECO:0000244|PDB:1CD9}.
STRAND 304 315 {ECO:0000244|PDB:1CD9}.
STRAND 326 328 {ECO:0000244|PDB:1CD9}.
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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