CSF3R_HUMAN
ID CSF3R_HUMAN Reviewed; 836 AA.
AC Q99062;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 209.
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=GCSFR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Placenta;
RX PubMed=2147944; DOI=10.1084/jem.172.6.1559;
RA Larsen A., Davis T., Curtis B.M., Gimpel S., Sims J.E., Cosman D., Park L.,
RA Sorensen E., March C.J., Smith C.A.;
RT "Expression cloning of a human granulocyte colony-stimulating factor
RT receptor: a structural mosaic of hematopoietin receptor, immunoglobulin,
RT and fibronectin domains.";
RL J. Exp. Med. 172:1559-1570(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Placenta;
RX PubMed=1701053; DOI=10.1073/pnas.87.22.8702;
RA Fukunaga R., Seto Y., Mizushima S., Nagata S.;
RT "Three different mRNAs encoding human granulocyte colony-stimulating factor
RT receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8702-8706(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1530796;
RA Seto Y., Fukunaga R., Nagata S.;
RT "Chromosomal gene organization of the human granulocyte colony-stimulating
RT factor receptor.";
RL J. Immunol. 148:259-266(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-231; ASN-320; ARG-346;
RP LYS-405; GLN-440; HIS-510; HIS-562 AND CYS-583.
RG SeattleSNPs variation discovery resource;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 234-269.
RX PubMed=8554326; DOI=10.1006/abbi.1995.0047;
RA Haniu M., Horan T., Arakawa T., Le J., Katta V., Rohde M.F.;
RT "Extracellular domain of granulocyte-colony stimulating factor receptor.
RT Interaction with its ligand and identification of a domain in close
RT proximity of ligand-binding region.";
RL Arch. Biochem. Biophys. 324:344-356(1995).
RN [7]
RP DOMAINS.
RX PubMed=1717255; DOI=10.1002/j.1460-2075.1991.tb07835.x;
RA Fukunaga R., Ishizaka-Ikeda E., Pan C.-X., Seto Y., Nagata S.;
RT "Functional domains of the granulocyte colony-stimulating factor
RT receptor.";
RL EMBO J. 10:2855-2865(1991).
RN [8]
RP FUNCTION, AND POSSIBLE ASSOCIATION WITH SCN.
RX PubMed=7514305; DOI=10.1073/pnas.91.10.4480;
RA Dong F., Hoefsloot L.H., Schelen A.M., Broeders C.A., Meijer Y.,
RA Veerman A.J., Touw I.P., Lowenberg B.;
RT "Identification of a nonsense mutation in the granulocyte-colony-
RT stimulating factor receptor in severe congenital neutropenia.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4480-4484(1994).
RN [9]
RP REVIEW.
RX PubMed=17127321; DOI=10.2741/2103;
RA Touw I.P., van de Geijn G.J.;
RT "Granulocyte colony-stimulating factor and its receptor in normal myeloid
RT cell development, leukemia and related blood cell disorders.";
RL Front. Biosci. 12:800-815(2007).
RN [10]
RP POSSIBLE ASSOCIATION WITH SCN.
RX PubMed=19120359; DOI=10.1111/j.1365-2141.2008.07425.x;
RA Zeidler C., Germeshausen M., Klein C., Welte K.;
RT "Clinical implications of ELA2-, HAX1-, and G-CSF-receptor (CSF3R)
RT mutations in severe congenital neutropenia.";
RL Br. J. Haematol. 144:459-467(2009).
RN [11]
RP STRUCTURE BY NMR OF 227-334.
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 [12]
RP 3D-STRUCTURE MODELING OF 125-331.
RX PubMed=9368043; DOI=10.1074/jbc.272.47.29735;
RA Layton J.E., Iaria J., Smith D.K., Treutlein H.R.;
RT "Identification of a ligand-binding site on the granulocyte colony-
RT stimulating factor receptor by molecular modeling and mutagenesis.";
RL J. Biol. Chem. 272:29735-29741(1997).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-333 IN COMPLEX WITH CSF3,
RP GLYCOSYLATION AT ASN-134, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=16492764; DOI=10.1073/pnas.0511264103;
RA Tamada T., Honjo E., Maeda Y., Okamoto T., Ishibashi M., Tokunaga M.,
RA Kuroki R.;
RT "Homodimeric cross-over structure of the human granulocyte colony-
RT stimulating factor (GCSF) receptor signaling complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3135-3140(2006).
RN [14]
RP INVOLVEMENT IN SEVERE CONGENITAL NEUTROPENIA, VARIANT HIS-229, AND
RP CHARACTERIZATION OF VARIANT HIS-229.
RX PubMed=10449521; DOI=10.1084/jem.190.4.497;
RA Ward A.C., van Aesch Y.M., Gits J., Schelen A.M., de Koning J.P.,
RA van Leeuwen D., Freedman M.H., Touw I.P.;
RT "Novel point mutation in the extracellular domain of the granulocyte
RT colony-stimulating factor (G-CSF) receptor in a case of severe congenital
RT neutropenia hyporesponsive to G-CSF treatment.";
RL J. Exp. Med. 190:497-507(1999).
RN [15]
RP VARIANT NEUTROPHILIA ASN-640.
RX PubMed=19620628; DOI=10.1084/jem.20090693;
RA Plo I., Zhang Y., Le Couedic J.P., Nakatake M., Boulet J.M., Itaya M.,
RA Smith S.O., Debili N., Constantinescu S.N., Vainchenker W., Louache F.,
RA de Botton S.;
RT "An activating mutation in the CSF3R gene induces a hereditary chronic
RT neutrophilia.";
RL J. Exp. Med. 206:1701-1707(2009).
RN [16]
RP INVOLVEMENT IN SCN7, VARIANT SCN7 CYS-308, CHARACTERIZATION OF VARIANT SCN7
RP CYS-308, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=24753537; DOI=10.1182/blood-2013-11-535419;
RA Triot A., Jaervinen P.M., Arostegui J.I., Murugan D., Kohistani N.,
RA Dapena Diaz J.L., Racek T., Puchalka J., Gertz E.M., Schaeffer A.A.,
RA Kotlarz D., Pfeifer D., Diaz de Heredia Rubio C., Ozdemir M.A.,
RA Patiroglu T., Karakukcu M., Sanchez de Toledo Codina J., Yaguee J.,
RA Touw I.P., Unal E., Klein C.;
RT "Inherited biallelic CSF3R mutations in severe congenital neutropenia.";
RL Blood 123:3811-3817(2014).
RN [17]
RP INVOLVEMENT IN SCN7.
RX PubMed=26324699; DOI=10.1182/blood-2015-07-661264;
RA Klimiankou M., Klimenkova O., Uenalan M., Zeidler A., Mellor-Heineke S.,
RA Kandabarau S., Skokowa J., Zeidler C., Welte K.;
RT "GM-CSF stimulates granulopoiesis in a congenital neutropenia patient with
RT loss-of-function biallelic heterozygous CSF3R mutations.";
RL Blood 126:1865-1867(2015).
CC -!- FUNCTION: Receptor for granulocyte colony-stimulating factor (CSF3),
CC essential for granulocytic maturation. Plays a crucial role in the
CC proliferation, differientation and survival of cells along the
CC neutrophilic lineage. In addition it may function in some adhesion or
CC recognition events at the cell surface. {ECO:0000269|PubMed:7514305}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P40223, ECO:0000269|PubMed:16492764}.
CC -!- INTERACTION:
CC Q99062; P40763: STAT3; NbExp=4; IntAct=EBI-7331284, EBI-518675;
CC Q99062; P0CG48: UBC; NbExp=2; IntAct=EBI-7331284, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24753537};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist. Experimental confirmation
CC may be lacking for some isoforms.;
CC Name=1; Synonyms=GCSFR-1;
CC IsoId=Q99062-1; Sequence=Displayed;
CC Name=2; Synonyms=GCSFR-2;
CC IsoId=Q99062-2; Sequence=VSP_001674;
CC Name=3; Synonyms=GCSFR-3;
CC IsoId=Q99062-3; Sequence=VSP_001673;
CC Name=4; Synonyms=GCSFR-4, D7;
CC IsoId=Q99062-4; Sequence=VSP_001671, VSP_001672;
CC -!- TISSUE SPECIFICITY: One or several isoforms have been found in
CC myelogenous leukemia cell line KG-1, leukemia U-937 cell line, in bone
CC marrow cells, placenta, and peripheral blood granulocytes. Isoform
CC GCSFR-2 is found only in leukemia U-937 cells. Isoform GCSFR-3 is
CC highly expressed in placenta.
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. {ECO:0000269|PubMed:1717255}.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation. {ECO:0000269|PubMed:1717255}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:24753537}.
CC -!- DISEASE: Hereditary neutrophilia (NEUTROPHILIA) [MIM:162830]: A form of
CC lifelong, persistent neutrophilia, a condition characterized by an
CC increase in the number of neutrophils in the blood.
CC {ECO:0000269|PubMed:19620628}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Neutropenia, severe congenital 7, autosomal recessive (SCN7)
CC [MIM:617014]: A form of severe congenital neutropenia, a disorder of
CC hematopoiesis characterized by maturation arrest of granulopoiesis at
CC the level of promyelocytes with peripheral blood absolute neutrophil
CC counts below 0.5 x 10(9)/l and early onset of severe bacterial
CC infections. {ECO:0000269|PubMed:24753537, ECO:0000269|PubMed:26324699}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: Mutations in CSF3R acquired in multipotent hematopoietic
CC progenitor cells and resulting in truncated hyper-responsive forms of
CC the receptor, have been identified in most cases of severe congenital
CC neutropenia (SCN). Patients carrying these mutations are at risk for
CC developing myelodysplastic syndromes and/or acute myeloid leukemia.
CC Constitutive mutations leading to hyporesponsive forms of the receptor
CC are responsible for the refractoriness to CSF3 treatment observed in
CC some SCN patients.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/csf3r/";
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DR EMBL; X55721; CAA39253.1; -; mRNA.
DR EMBL; X55720; CAA39252.1; -; mRNA.
DR EMBL; M59818; AAA63176.1; -; mRNA.
DR EMBL; M59819; AAA63177.1; -; mRNA.
DR EMBL; M59820; AAA63178.1; -; mRNA.
DR EMBL; S71484; AAB20660.1; -; Genomic_DNA.
DR EMBL; AY148100; AAN05790.1; -; Genomic_DNA.
DR EMBL; BC053585; AAH53585.1; -; mRNA.
DR CCDS; CCDS412.1; -. [Q99062-4]
DR CCDS; CCDS413.1; -. [Q99062-1]
DR CCDS; CCDS414.1; -. [Q99062-3]
DR PIR; B38252; B38252.
DR PIR; C38252; C38252.
DR PIR; JH0329; JH0329.
DR RefSeq; NP_000751.1; NM_000760.3. [Q99062-1]
DR RefSeq; NP_724781.1; NM_156039.3. [Q99062-3]
DR RefSeq; NP_758519.1; NM_172313.2. [Q99062-4]
DR RefSeq; XP_011539050.1; XM_011540748.2. [Q99062-3]
DR RefSeq; XP_016855859.1; XM_017000370.1. [Q99062-3]
DR PDB; 2D9Q; X-ray; 2.80 A; B=25-332.
DR PDBsum; 2D9Q; -.
DR AlphaFoldDB; Q99062; -.
DR SMR; Q99062; -.
DR BioGRID; 107828; 20.
DR CORUM; Q99062; -.
DR DIP; DIP-5788N; -.
DR ELM; Q99062; -.
DR IntAct; Q99062; 3.
DR MINT; Q99062; -.
DR STRING; 9606.ENSP00000362195; -.
DR BindingDB; Q99062; -.
DR ChEMBL; CHEMBL1996; -.
DR DrugBank; DB05249; FavId.
DR DrugBank; DB00099; Filgrastim.
DR DrugBank; DB13144; Lenograstim.
DR DrugBank; DB13200; Lipegfilgrastim.
DR DrugBank; DB00019; Pegfilgrastim.
DR DrugCentral; Q99062; -.
DR GuidetoPHARMACOLOGY; 1719; -.
DR GlyGen; Q99062; 8 sites.
DR iPTMnet; Q99062; -.
DR PhosphoSitePlus; Q99062; -.
DR BioMuta; CSF3R; -.
DR DMDM; 729564; -.
DR MassIVE; Q99062; -.
DR PaxDb; Q99062; -.
DR PeptideAtlas; Q99062; -.
DR PRIDE; Q99062; -.
DR ProteomicsDB; 78226; -. [Q99062-1]
DR ProteomicsDB; 78227; -. [Q99062-2]
DR ProteomicsDB; 78228; -. [Q99062-3]
DR ProteomicsDB; 78229; -. [Q99062-4]
DR ABCD; Q99062; 2 sequenced antibodies.
DR Antibodypedia; 4479; 658 antibodies from 40 providers.
DR DNASU; 1441; -.
DR Ensembl; ENST00000331941.6; ENSP00000332180.5; ENSG00000119535.18. [Q99062-4]
DR Ensembl; ENST00000361632.8; ENSP00000355406.4; ENSG00000119535.18. [Q99062-1]
DR Ensembl; ENST00000373103.5; ENSP00000362195.1; ENSG00000119535.18. [Q99062-3]
DR Ensembl; ENST00000373104.5; ENSP00000362196.1; ENSG00000119535.18. [Q99062-4]
DR Ensembl; ENST00000373106.6; ENSP00000362198.2; ENSG00000119535.18. [Q99062-1]
DR GeneID; 1441; -.
DR KEGG; hsa:1441; -.
DR MANE-Select; ENST00000373106.6; ENSP00000362198.2; NM_000760.4; NP_000751.1.
DR UCSC; uc001cav.3; human. [Q99062-1]
DR CTD; 1441; -.
DR DisGeNET; 1441; -.
DR GeneCards; CSF3R; -.
DR HGNC; HGNC:2439; CSF3R.
DR HPA; ENSG00000119535; Group enriched (bone marrow, lung, lymphoid tissue, placenta).
DR MalaCards; CSF3R; -.
DR MIM; 138971; gene.
DR MIM; 162830; phenotype.
DR MIM; 617014; phenotype.
DR neXtProt; NX_Q99062; -.
DR OpenTargets; ENSG00000119535; -.
DR Orphanet; 98824; Atypical chronic myeloid leukemia.
DR Orphanet; 420702; Autosomal recessive severe congenital neutropenia due to CSF3R deficiency.
DR Orphanet; 86829; Chronic neutrophilic leukemia.
DR Orphanet; 279943; Hereditary neutrophilia.
DR PharmGKB; PA26942; -.
DR VEuPathDB; HostDB:ENSG00000119535; -.
DR eggNOG; ENOG502QT3H; Eukaryota.
DR GeneTree; ENSGT00940000158915; -.
DR HOGENOM; CLU_017990_0_0_1; -.
DR InParanoid; Q99062; -.
DR OMA; WKPSLYI; -.
DR OrthoDB; 144839at2759; -.
DR PhylomeDB; Q99062; -.
DR TreeFam; TF338122; -.
DR PathwayCommons; Q99062; -.
DR Reactome; R-HSA-449836; Other interleukin signaling.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-9674555; Signaling by CSF3 (G-CSF).
DR Reactome; R-HSA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR SignaLink; Q99062; -.
DR SIGNOR; Q99062; -.
DR BioGRID-ORCS; 1441; 11 hits in 1067 CRISPR screens.
DR ChiTaRS; CSF3R; human.
DR EvolutionaryTrace; Q99062; -.
DR GeneWiki; Granulocyte_colony-stimulating_factor_receptor; -.
DR GenomeRNAi; 1441; -.
DR Pharos; Q99062; Tclin.
DR PRO; PR:Q99062; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99062; protein.
DR Bgee; ENSG00000119535; Expressed in granulocyte and 119 other tissues.
DR ExpressionAtlas; Q99062; baseline and differential.
DR Genevisible; Q99062; HS.
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:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
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; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
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:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR CDD; cd00063; FN3; 4.
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; 5.
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; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT CHAIN 25..836
FT /note="Granulocyte colony-stimulating factor receptor"
FT /id="PRO_0000010874"
FT TOPO_DOM 25..627
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..836
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..117
FT /note="Ig-like C2-type"
FT DOMAIN 125..230
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 233..332
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 334..430
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 431..528
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 530..623
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 318..322
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 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16492764"
FT CARBOHYD 389
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 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..52
FT /evidence="ECO:0000269|PubMed:16492764"
FT DISULFID 46..101
FT /evidence="ECO:0000269|PubMed:16492764"
FT DISULFID 131..142
FT /evidence="ECO:0000269|PubMed:16492764"
FT DISULFID 167..218
FT /evidence="ECO:0000269|PubMed:16492764"
FT DISULFID 177..186
FT /evidence="ECO:0000269|PubMed:16492764"
FT DISULFID 248..295
FT /evidence="ECO:0000269|PubMed:16492764"
FT DISULFID 266..309
FT /evidence="ECO:0000269|PubMed:16492764"
FT VAR_SEQ 622..836
FT /note="EGSELHIILGLFGLLLLLTCLCGTAWLCCSPNRKNPLWPSVPDPAHSSLGSW
FT VPTIMEEDAFQLPGLGTPPITKLTVLEEDEKKPVPWESHNSSETCGLPTLVQTYVLQGD
FT PRAVSTQPQSQSGTSDQVLYGQLLGSPTSPGPGHYLRCDSTQPLLAGLTPSPKSYENLW
FT FQASPLGTLVTPAPSQEDDCVFGPLLNFPLLQGIRVHGMEALGSF -> APTGRIPSGQ
FT VSQTQLTAAWAPGCPQSWRRMPSSCPALARHPSPSSQCWRRMKRSRCPGSPITAQRPVA
FT SPLWSRPMCSRGTQEQFPPSPNPSLAPAIRSFMGSCWAAPQAQGQGTISAVTPLSPSWR
FT ASPPAPSPMRTSGSRPAPWGPW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1701053"
FT /id="VSP_001674"
FT VAR_SEQ 680
FT /note="E -> ELPGPRQGQWLGQTSEMSRALTPHPCVQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1701053"
FT /id="VSP_001673"
FT VAR_SEQ 750..783
FT /note="VLYGQLLGSPTSPGPGHYLRCDSTQPLLAGLTPS -> AGPPRRSAYFKDQI
FT MLHPAPPNGLLCLFPITSVL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:2147944"
FT /id="VSP_001671"
FT VAR_SEQ 784..836
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:2147944"
FT /id="VSP_001672"
FT VARIANT 229
FT /note="P -> H (probable disease-associated variant found in
FT a patient with apparently autosomal dominant severe
FT congenital neutropenia; affects CSF3 mediated proliferation
FT and survival of myeloid cells; abrogates receptor signaling
FT by altering ligand binding; dominant negative effect;
FT dbSNP:rs764202764)"
FT /evidence="ECO:0000269|PubMed:10449521"
FT /id="VAR_062517"
FT VARIANT 231
FT /note="M -> T (in dbSNP:rs3917973)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014325"
FT VARIANT 308
FT /note="R -> C (in SCN7; decreases localization to plasma
FT membrane; decreases receptor signaling; dbSNP:rs606231473)"
FT /evidence="ECO:0000269|PubMed:24753537"
FT /id="VAR_077011"
FT VARIANT 320
FT /note="D -> N (in dbSNP:rs3918018)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014326"
FT VARIANT 346
FT /note="Q -> R (in dbSNP:rs3917974)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014327"
FT VARIANT 405
FT /note="E -> K (in dbSNP:rs3918019)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014328"
FT VARIANT 440
FT /note="R -> Q (in dbSNP:rs3918020)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014329"
FT VARIANT 510
FT /note="D -> H (in dbSNP:rs3917991)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014330"
FT VARIANT 562
FT /note="Y -> H (in dbSNP:rs3917996)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014331"
FT VARIANT 583
FT /note="R -> C (in dbSNP:rs3917997)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014332"
FT VARIANT 640
FT /note="T -> N (in neutrophilia; dbSNP:rs121918426)"
FT /evidence="ECO:0000269|PubMed:19620628"
FT /id="VAR_063065"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 94..119
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:2D9Q"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:2D9Q"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2D9Q"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:2D9Q"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 264..275
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 303..311
FT /evidence="ECO:0007829|PDB:2D9Q"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:2D9Q"
SQ SEQUENCE 836 AA; 92156 MW; 3531ADDC979D4BC3 CRC64;
MARLGNCSLT WAALIILLLP GSLEECGHIS VSAPIVHLGD PITASCIIKQ NCSHLDPEPQ
ILWRLGAELQ PGGRQQRLSD GTQESIITLP HLNHTQAFLS CCLNWGNSLQ ILDQVELRAG
YPPAIPHNLS CLMNLTTSSL ICQWEPGPET HLPTSFTLKS FKSRGNCQTQ GDSILDCVPK
DGQSHCCIPR KHLLLYQNMG IWVQAENALG TSMSPQLCLD PMDVVKLEPP MLRTMDPSPE
AAPPQAGCLQ LCWEPWQPGL HINQKCELRH KPQRGEASWA LVGPLPLEAL QYELCGLLPA
TAYTLQIRCI RWPLPGHWSD WSPSLELRTT ERAPTVRLDT WWRQRQLDPR TVQLFWKPVP
LEEDSGRIQG YVVSWRPSGQ AGAILPLCNT TELSCTFHLP SEAQEVALVA YNSAGTSRPT
PVVFSESRGP ALTRLHAMAR DPHSLWVGWE PPNPWPQGYV IEWGLGPPSA SNSNKTWRME
QNGRATGFLL KENIRPFQLY EIIVTPLYQD TMGPSQHVYA YSQEMAPSHA PELHLKHIGK
TWAQLEWVPE PPELGKSPLT HYTIFWTNAQ NQSFSAILNA SSRGFVLHGL EPASLYHIHL
MAASQAGATN STVLTLMTLT PEGSELHIIL GLFGLLLLLT CLCGTAWLCC SPNRKNPLWP
SVPDPAHSSL GSWVPTIMEE DAFQLPGLGT PPITKLTVLE EDEKKPVPWE SHNSSETCGL
PTLVQTYVLQ GDPRAVSTQP QSQSGTSDQV LYGQLLGSPT SPGPGHYLRC DSTQPLLAGL
TPSPKSYENL WFQASPLGTL VTPAPSQEDD CVFGPLLNFP LLQGIRVHGM EALGSF
