CSF3_CANLF
ID CSF3_CANLF Reviewed; 175 AA.
AC P35834;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Granulocyte colony-stimulating factor;
DE Short=G-CSF;
GN Name=CSF3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=7504736; DOI=10.1006/jmbi.1993.1617;
RA Lovejoy B., Cascio D., Eisenberg D.;
RT "Crystal structure of canine and bovine granulocyte-colony stimulating
RT factor (G-CSF).";
RL J. Mol. Biol. 234:640-653(1993).
CC -!- FUNCTION: Granulocyte/macrophage colony-stimulating factors are
CC cytokines that act in hematopoiesis by controlling the production,
CC differentiation, and function of 2 related white cell populations of
CC the blood, the granulocytes and the monocytes-macrophages. This CSF
CC induces granulocytes.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: O-glycosylated.
CC -!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
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DR PDB; 1BGD; X-ray; 2.30 A; A=1-175.
DR PDB; 1BGE; X-ray; 2.20 A; A/B=1-175.
DR PDBsum; 1BGD; -.
DR PDBsum; 1BGE; -.
DR AlphaFoldDB; P35834; -.
DR SMR; P35834; -.
DR STRING; 9612.ENSCAFP00000023945; -.
DR PaxDb; P35834; -.
DR eggNOG; ENOG502SCNA; Eukaryota.
DR InParanoid; P35834; -.
DR EvolutionaryTrace; P35834; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005130; F:granulocyte colony-stimulating factor receptor binding; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0045639; P:positive regulation of myeloid cell differentiation; IBA:GO_Central.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR040117; GCSF/MGF.
DR InterPro; IPR030474; IL-6/GCSF/MGF.
DR InterPro; IPR030473; IL6/GCSF/MGF_CS.
DR PANTHER; PTHR10511; PTHR10511; 1.
DR Pfam; PF16647; GCSF; 1.
DR PRINTS; PR00433; IL6GCSFMGF.
DR SMART; SM00126; IL6; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00254; INTERLEUKIN_6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokine; Disulfide bond; Glycoprotein; Growth factor;
KW Reference proteome; Secreted.
FT CHAIN 1..175
FT /note="Granulocyte colony-stimulating factor"
FT /id="PRO_0000058759"
FT CARBOHYD 134
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT DISULFID 37..43
FT DISULFID 65..75
FT HELIX 12..39
FT /evidence="ECO:0007829|PDB:1BGE"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:1BGE"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1BGE"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1BGE"
FT HELIX 72..92
FT /evidence="ECO:0007829|PDB:1BGE"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1BGE"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1BGE"
FT HELIX 101..125
FT /evidence="ECO:0007829|PDB:1BGE"
FT HELIX 144..171
FT /evidence="ECO:0007829|PDB:1BGE"
SQ SEQUENCE 175 AA; 18858 MW; 28C26B24990C6DB3 CRC64;
MAPLGPTGPL PQSFLLKCLE QMRKVQADGT ALQETLCATH QLCHPEELVL LGHALGIPQP
PLSSCSSQAL QLMGCLRQLH SGLFLYQGLL QALAGISPEL APTLDTLQLD TTDFAINIWQ
QMEDLGMAPA VPPTQGTMPA FTSAFQRRAG GVLVASNLQS FLELAYRALR HFAKP
