ID A0A5J5N575_MUNRE Unreviewed; 849 AA.
AC A0A5J5N575;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE RecName: Full=Granulocyte colony-stimulating factor receptor {ECO:0000256|ARBA:ARBA00071023};
GN ORFNames=FD755_001705 {ECO:0000313|EMBL:KAB0386749.1};
OS Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Muntiacinae; Muntiacus.
OX NCBI_TaxID=9886 {ECO:0000313|EMBL:KAB0386749.1, ECO:0000313|Proteomes:UP000326062};
RN [1] {ECO:0000313|EMBL:KAB0386749.1, ECO:0000313|Proteomes:UP000326062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCam_UCB_Mr {ECO:0000313|EMBL:KAB0386749.1};
RC TISSUE=Fibroblast cell line {ECO:0000313|EMBL:KAB0386749.1};
RA Mudd A.B., Bredeson J.V., Baum R., Hockemeyer D., Rokhsar D.S.;
RT "Discovery of a novel chromosome fission-fusion reversal in muntjac.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00066227}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00008921}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
CC subfamily. {ECO:0000256|ARBA:ARBA00010890}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAB0386749.1}.
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DR EMBL; VCEB01000001; KAB0386749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5N575; -.
DR Proteomes; UP000326062; Chromosome 1.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:TreeGrafter.
DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR GO; GO:0019955; F:cytokine binding; IEA:TreeGrafter.
DR GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
DR FunFam; 2.60.40.10:FF:000879; Colony stimulating factor 3 receptor; 1.
DR FunFam; 2.60.40.10:FF:001209; Colony stimulating factor 3 receptor; 1.
DR FunFam; 2.60.40.10:FF:001234; Colony stimulating factor 3 receptor; 1.
DR FunFam; 2.60.40.10:FF:000997; Colony stimulating factor 3 receptor (Granulocyte); 1.
DR FunFam; 2.60.40.10:FF:000465; Granulocyte colony-stimulating factor receptor; 1.
DR FunFam; 2.60.40.10:FF:000839; granulocyte colony-stimulating factor receptor isoform X1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 InterPro; IPR050379; Type-I_Cytokine_Rcpt.
DR PANTHER; PTHR23036; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR23036:SF103; GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF06328; Lep_receptor_Ig; 1.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; Fibronectin type III; 4.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000326062};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 636..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..238
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 244..341
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 441..535
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 537..634
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 849 AA; 94183 MW; EA539060DC5A3340 CRC64;
MSFGKAQGAW HGLIGQIGLT GLVPRKMPEC LEQCGHILLS APIVRLGDQV MASCIINQNC
SHLVTEWRIV WKLEPELHPR ERQQHLPNGT LQSTITLPHF NHSRVLLSCC LHWGNSLQIL
DQAELQAGYP PIAPHNLSCI MNLTINSLIC QWEPGPDTHL STSFTLKSFK SQDQCQTQKD
SIPDCVPEDG QSHCSIPRRH LQLYQDMSIW VQAKNALGTS ISPKLCLAPM DVVKLEPPTL
WALEPSPGVA PPQPGCLRLR WETWKPSLYI EQKCELRHQP RLGEAGWDLV SALPARTPEH
ELCGLLPSTA YTLQMRCTRW PLPGHWSEWS PSLELITTQR APIVRLDTWW RQRQLDPQTV
AVQLFWKPIA LEEESGQIQG YLVSRRPSDQ AGAEPTLCDT TELNCTFQLP PEAREVLLQA
YNTAGSSHPT PVVFLESRGP PLGRLHATAR DPHSLWVGWE PPRPPPQGYV IEWGLSPPSP
NGSPMTWRLE HDGSIAGTLL QENIRPFQLY EITVTPLYQD TKGPSQHVYA YSQEMAPSHG
PELHLRHIGK TWAQLEWVPE APELGKSPFT HYTIFWTNTQ DQSFSTVLNA STHSFVLRGL
EPSSLYHVHL MAASQAGATN STILTLMTLA LEESELHIIL GLFGLLVLLI CLCGAAQFCC
RPSRKYSLWP SVPDPARSSL GSWVPTIAAE DIFQLPSLRD PGMPPITKIT VLEEEEKKPG
PWESNDGSGT GSLSTLVQAY VLQGDPRVPS TQPQPQSGNS DQVLYVQVLG SPTGPGPGHY
LRCDSTQPLL EGLTPSPKSY ENLWFQTSPL GAPEPLVPHP EDDSIFEPLL DFPLLQGLRV
SGAEGLGGF
//
