##gff-version 3 P07141 UniProtKB Signal peptide 1 32 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3925458;Dbxref=PMID:3925458 P07141 UniProtKB Chain 33 552 . . . ID=PRO_0000005858;Note=Macrophage colony-stimulating factor 1 P07141 UniProtKB Chain 33 447 . . . ID=PRO_0000296232;Note=Processed macrophage colony-stimulating factor 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8JZQ0 P07141 UniProtKB Chain 33 255 . . . ID=PRO_0000457792;Note=Macrophage colony-stimulating factor 1 43 kDa subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09603 P07141 UniProtKB Topological domain 33 492 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P07141 UniProtKB Transmembrane 493 515 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P07141 UniProtKB Topological domain 516 552 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P07141 UniProtKB Region 197 293 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P07141 UniProtKB Region 321 412 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P07141 UniProtKB Region 439 465 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P07141 UniProtKB Region 525 552 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P07141 UniProtKB Compositional bias 252 267 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P07141 UniProtKB Compositional bias 370 385 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P07141 UniProtKB Compositional bias 538 552 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P07141 UniProtKB Glycosylation 107 107 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P07141 UniProtKB Glycosylation 154 154 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P07141 UniProtKB Glycosylation 172 172 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P07141 UniProtKB Glycosylation 308 308 . . . Note=O-linked (Xyl...) (chondroitin sulfate) serine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09603 P07141 UniProtKB Glycosylation 360 360 . . . Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09603 P07141 UniProtKB Disulfide bond 39 122 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19017797;Dbxref=PMID:19017797 P07141 UniProtKB Disulfide bond 63 63 . . . Note=Interchain;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19017797;Dbxref=PMID:19017797 P07141 UniProtKB Disulfide bond 80 171 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19017797;Dbxref=PMID:19017797 P07141 UniProtKB Disulfide bond 134 178 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19017797;Dbxref=PMID:19017797 P07141 UniProtKB Disulfide bond 189 189 . . . Note=Interchain;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07141 UniProtKB Disulfide bond 191 191 . . . Note=Interchain;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07141 UniProtKB Alternative sequence 182 476 . . . ID=VSP_001189;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P07141 UniProtKB Natural variant 292 292 . . . Note=D->G P07141 UniProtKB Natural variant 345 345 . . . Note=S->P P07141 UniProtKB Sequence conflict 3 3 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P07141 UniProtKB Sequence conflict 6 6 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P07141 UniProtKB Sequence conflict 7 8 . . . Note=AG->PR;Ontology_term=ECO:0000305;evidence=ECO:0000305 P07141 UniProtKB Sequence conflict 246 246 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P07141 UniProtKB Helix 37 41 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ P07141 UniProtKB Helix 45 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ P07141 UniProtKB Beta strand 65 70 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ P07141 UniProtKB Turn 72 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ P07141 UniProtKB Helix 78 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ P07141 UniProtKB Helix 104 118 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ P07141 UniProtKB Helix 119 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ P07141 UniProtKB Turn 131 134 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ P07141 UniProtKB Beta strand 135 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ P07141 UniProtKB Helix 142 162 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ P07141 UniProtKB Turn 164 167 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ P07141 UniProtKB Helix 172 177 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3EJJ