CSF1_MOUSE
ID CSF1_MOUSE Reviewed; 552 AA.
AC P07141; Q3U395; Q8R3C8;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Macrophage colony-stimulating factor 1;
DE Short=CSF-1;
DE Short=MCSF;
DE Contains:
DE RecName: Full=Processed macrophage colony-stimulating factor 1;
DE Flags: Precursor;
GN Name=Csf1; Synonyms=Csfm;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3494232; DOI=10.1093/nar/15.5.2389;
RA Delamarter J.F., Hession C., Semon D., Gough N.M., Rothenbuhler R.,
RA Mermod J.-J.;
RT "Nucleotide sequence of a cDNA encoding murine CSF-1 (Macrophage-CSF).";
RL Nucleic Acids Res. 15:2389-2390(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2457916; DOI=10.1073/pnas.85.18.6706;
RA Ladner M.B., Martin G.A., Noble J.A., Wittman V.P., Warren M.K.,
RA McGrogan M., Stanley E.R.;
RT "cDNA cloning and expression of murine macrophage colony-stimulating factor
RT from L929 cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6706-6710(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8357831; DOI=10.1016/0167-4781(93)90108-p;
RA Borycki A.G., Lenormund J., Guillier M., Leibovitch S.A.;
RT "Isolation and characterization of a cDNA clone encoding for rat CSF-1
RT gene. Post-transcriptional repression occurs in myogenic differentiation.";
RL Biochim. Biophys. Acta 1174:143-152(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell, and Neural stem cell;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-100.
RX PubMed=3493488; DOI=10.1073/pnas.84.5.1157;
RA Rajavashisth T.B., Eng R., Shadduck R.K., Waheed A., Ben-Avram C.M.,
RA Shively J.E., Lusis A.J.;
RT "Cloning and tissue-specific expression of mouse macrophage colony-
RT stimulating factor mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1157-1161(1987).
RN [8]
RP PROTEIN SEQUENCE OF 33-57.
RX PubMed=3925458; DOI=10.1073/pnas.82.13.4486;
RA Ben-Avram C.M., Shively J.E., Shadduck R.K., Waheed A., Rajavashisth T.B.,
RA Lusis A.J.;
RT "Amino-terminal amino acid sequence of murine colony-stimulating factor
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4486-4489(1985).
RN [9]
RP NUCLEOTIDE SEQUENCE OF 1-13.
RX PubMed=1874443; DOI=10.1016/0378-1119(91)90074-l;
RA Harrington M.A., Edenberg H.J., Saxman S.M., Pedigo L.M., Daub R.,
RA Broxmeyer H.E.;
RT "Cloning and characterization of the murine promoter for the colony-
RT stimulating factor-1-encoding gene.";
RL Gene 102:165-170(1991).
RN [10]
RP SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:8357831 ORIGINATES FROM MOUSE.
RX PubMed=12074592; DOI=10.1016/s0006-291x(02)00598-3;
RA Dobbins D.E., Sood R., Hashiramoto A., Hansen C.T., Wilder R.L.,
RA Remmers E.F.;
RT "Mutation of macrophage colony stimulating factor (Csf1) causes
RT osteopetrosis in the tl rat.";
RL Biochem. Biophys. Res. Commun. 294:1114-1120(2002).
RN [11]
RP SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:8357831 ORIGINATES FROM MOUSE.
RX PubMed=12379742; DOI=10.1073/pnas.202332999;
RA Van Wesenbeeck L., Odgren P.R., MacKay C.A., D'Angelo M., Safadi F.F.,
RA Popoff S.N., Van Hul W., Marks S.C. Jr.;
RT "The osteopetrotic mutation toothless (tl) is a loss-of-function frameshift
RT mutation in the rat Csf1 gene: evidence of a crucial role for CSF-1 in
RT osteoclastogenesis and endochondral ossification.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14303-14308(2002).
RN [12]
RP CHARACTERIZATION.
RX PubMed=1733926; DOI=10.1016/s0021-9258(18)45861-9;
RA Price L.K.H., Choi H.U., Rosenberg L., Stanley E.R.;
RT "The predominant form of secreted colony stimulating factor-1 is a
RT proteoglycan.";
RL J. Biol. Chem. 267:2190-2199(1992).
RN [13]
RP DISEASE.
RX PubMed=2188141; DOI=10.1038/345442a0;
RA Yoshida H., Hayashi S., Kunisada T., Ogawa M., Nishikawa S., Okamura H.,
RA Sudo T., Shultz L.D., Nishikawa S.;
RT "The murine mutation osteopetrosis is in the coding region of the
RT macrophage colony stimulating factor gene.";
RL Nature 345:442-444(1990).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 36-180 IN COMPLEX WITH CSF1R,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=19017797; DOI=10.1073/pnas.0807762105;
RA Chen X., Liu H., Focia P.J., Shim A.H., He X.;
RT "Structure of macrophage colony stimulating factor bound to FMS: diverse
RT signaling assemblies of class III receptor tyrosine kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18267-18272(2008).
CC -!- FUNCTION: Cytokine that plays an essential role in the regulation of
CC survival, proliferation and differentiation of hematopoietic precursor
CC cells, especially mononuclear phagocytes, such as macrophages and
CC monocytes. Promotes the release of pro-inflammatory chemokines, and
CC thereby plays an important role in innate immunity and in inflammatory
CC processes. Plays an important role in the regulation of osteoclast
CC proliferation and differentiation, the regulation of bone resorption,
CC and is required for normal bone development. Required for normal male
CC and female fertility. Promotes reorganization of the actin
CC cytoskeleton, regulates formation of membrane ruffles, cell adhesion
CC and cell migration. Plays a role in lipoprotein clearance.
CC -!- SUBUNIT: Homodimer or heterodimer; disulfide-linked. Interacts with
CC CSF1R. {ECO:0000269|PubMed:19017797}.
CC -!- INTERACTION:
CC P07141; Q8C161: Aar2; NbExp=2; IntAct=EBI-777188, EBI-777252;
CC P07141; Q60771: Cldn11; NbExp=2; IntAct=EBI-777188, EBI-309095;
CC P07141; P07141: Csf1; NbExp=3; IntAct=EBI-777188, EBI-777188;
CC P07141; P09581: Csf1r; NbExp=6; IntAct=EBI-777188, EBI-6305373;
CC P07141; Q9JHU4: Dync1h1; NbExp=2; IntAct=EBI-777188, EBI-645061;
CC P07141; P05480: Src; NbExp=2; IntAct=EBI-777188, EBI-298680;
CC P07141; P03228: BARF1; Xeno; NbExp=8; IntAct=EBI-777188, EBI-16007073;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Processed macrophage colony-stimulating factor
CC 1]: Secreted, extracellular space {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P07141-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07141-2; Sequence=VSP_001189;
CC -!- PTM: N-glycosylated. The predominant soluble form is a chondroitin
CC sulfate-containing proteoglycan.
CC -!- DISEASE: Note=A defect in Csf1 is the cause of osteopetrosis.
CC Osteopetrotic mice (op/op) are severely deficient in mature macrophages
CC and osteoclasts, display failed tooth eruption, and have a restricted
CC capacity for bone remodeling. {ECO:0000269|PubMed:2188141}.
CC -!- CAUTION: The sequence reported in PubMed:8357831 was thought to
CC originate from rat, but was later shown (PubMed:12074592 and
CC PubMed:12379742) to be derived from mouse. {ECO:0000305}.
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DR EMBL; X05010; CAA28660.1; -; mRNA.
DR EMBL; M21952; AAA37481.1; -; mRNA.
DR EMBL; M21149; AAA37482.1; -; mRNA.
DR EMBL; M84361; AAA03032.1; -; mRNA.
DR EMBL; AK138489; BAE23681.1; -; mRNA.
DR EMBL; AK154872; BAE32893.1; -; mRNA.
DR EMBL; AK160995; BAE36140.1; -; mRNA.
DR EMBL; CH466607; EDL01916.1; -; Genomic_DNA.
DR EMBL; CH466607; EDL01919.1; -; Genomic_DNA.
DR EMBL; BC025593; AAH25593.1; -; mRNA.
DR EMBL; BC066187; AAH66187.1; -; mRNA.
DR EMBL; BC066200; AAH66200.1; -; mRNA.
DR EMBL; BC066205; AAH66205.1; -; mRNA.
DR EMBL; M15692; AAA37480.1; -; mRNA.
DR EMBL; M81316; AAA19866.1; -; Unassigned_DNA.
DR CCDS; CCDS17740.1; -. [P07141-1]
DR CCDS; CCDS51044.1; -. [P07141-2]
DR PIR; A31401; A31401.
DR RefSeq; NP_001107001.1; NM_001113529.1. [P07141-2]
DR RefSeq; NP_001107002.1; NM_001113530.1. [P07141-1]
DR RefSeq; NP_031804.3; NM_007778.4. [P07141-1]
DR PDB; 3EJJ; X-ray; 2.40 A; A/B=36-180.
DR PDB; 3UF5; X-ray; 2.80 A; A/B=33-181.
DR PDB; 4ADQ; X-ray; 4.50 A; E/F/G/H=33-181.
DR PDBsum; 3EJJ; -.
DR PDBsum; 3UF5; -.
DR PDBsum; 4ADQ; -.
DR AlphaFoldDB; P07141; -.
DR SMR; P07141; -.
DR DIP; DIP-45278N; -.
DR IntAct; P07141; 43.
DR STRING; 10090.ENSMUSP00000014743; -.
DR BindingDB; P07141; -.
DR ChEMBL; CHEMBL3638330; -.
DR GlyGen; P07141; 3 sites.
DR iPTMnet; P07141; -.
DR PhosphoSitePlus; P07141; -.
DR SwissPalm; P07141; -.
DR CPTAC; non-CPTAC-3701; -.
DR jPOST; P07141; -.
DR MaxQB; P07141; -.
DR PaxDb; P07141; -.
DR PeptideAtlas; P07141; -.
DR PRIDE; P07141; -.
DR ProteomicsDB; 285344; -. [P07141-1]
DR ProteomicsDB; 285345; -. [P07141-2]
DR Antibodypedia; 20082; 902 antibodies from 43 providers.
DR DNASU; 12977; -.
DR Ensembl; ENSMUST00000014743; ENSMUSP00000014743; ENSMUSG00000014599. [P07141-1]
DR Ensembl; ENSMUST00000118593; ENSMUSP00000113136; ENSMUSG00000014599. [P07141-2]
DR Ensembl; ENSMUST00000120243; ENSMUSP00000113617; ENSMUSG00000014599. [P07141-1]
DR GeneID; 12977; -.
DR KEGG; mmu:12977; -.
DR UCSC; uc008qxk.2; mouse. [P07141-1]
DR UCSC; uc008qxl.2; mouse. [P07141-2]
DR CTD; 1435; -.
DR MGI; MGI:1339753; Csf1.
DR VEuPathDB; HostDB:ENSMUSG00000014599; -.
DR eggNOG; ENOG502S271; Eukaryota.
DR GeneTree; ENSGT00390000015805; -.
DR HOGENOM; CLU_095000_0_0_1; -.
DR InParanoid; P07141; -.
DR OMA; CQIAYEF; -.
DR OrthoDB; 715874at2759; -.
DR PhylomeDB; P07141; -.
DR TreeFam; TF337718; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-449836; Other interleukin signaling.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 12977; 1 hit in 71 CRISPR screens.
DR EvolutionaryTrace; P07141; -.
DR PRO; PR:P07141; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P07141; protein.
DR Bgee; ENSMUSG00000014599; Expressed in stroma of bone marrow and 235 other tissues.
DR ExpressionAtlas; P07141; baseline and differential.
DR Genevisible; P07141; MM.
DR GO; GO:1990682; C:CSF1-CSF1R complex; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005157; F:macrophage colony-stimulating factor receptor binding; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0003006; P:developmental process involved in reproduction; IMP:BHF-UCL.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0038145; P:macrophage colony-stimulating factor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0030225; P:macrophage differentiation; IMP:MGI.
DR GO; GO:0061519; P:macrophage homeostasis; IMP:MGI.
DR GO; GO:0060763; P:mammary duct terminal end bud growth; IMP:MGI.
DR GO; GO:0060611; P:mammary gland fat development; IMP:MGI.
DR GO; GO:0061518; P:microglial cell proliferation; IGI:ARUK-UCL.
DR GO; GO:0030224; P:monocyte differentiation; IMP:MGI.
DR GO; GO:0035702; P:monocyte homeostasis; IMP:MGI.
DR GO; GO:0097529; P:myeloid leukocyte migration; IGI:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0001780; P:neutrophil homeostasis; IMP:MGI.
DR GO; GO:0042476; P:odontogenesis; ISO:MGI.
DR GO; GO:0001503; P:ossification; ISO:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; IDA:MGI.
DR GO; GO:0002158; P:osteoclast proliferation; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IGI:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IGI:MGI.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISO:MGI.
DR GO; GO:1902228; P:positive regulation of macrophage colony-stimulating factor signaling pathway; ISO:MGI.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:MGI.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; IMP:MGI.
DR GO; GO:1905523; P:positive regulation of macrophage migration; ISO:MGI.
DR GO; GO:1904141; P:positive regulation of microglial cell migration; ISO:MGI.
DR GO; GO:0045657; P:positive regulation of monocyte differentiation; IMP:MGI.
DR GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; ISO:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0042488; P:positive regulation of odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IGI:MGI.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:MGI.
DR GO; GO:0030278; P:regulation of ossification; IMP:MGI.
DR GO; GO:0002931; P:response to ischemia; ISO:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:MGI.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR008001; MCSF-1.
DR PANTHER; PTHR10058; PTHR10058; 1.
DR Pfam; PF05337; CSF-1; 1.
DR PIRSF; PIRSF001948; MCSF-1; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytokine;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Growth factor;
KW Immunity; Inflammatory response; Innate immunity; Membrane; Proteoglycan;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:3925458"
FT CHAIN 33..552
FT /note="Macrophage colony-stimulating factor 1"
FT /id="PRO_0000005858"
FT CHAIN 33..447
FT /note="Processed macrophage colony-stimulating factor 1"
FT /evidence="ECO:0000250|UniProtKB:Q8JZQ0"
FT /id="PRO_0000296232"
FT TOPO_DOM 33..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 197..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..122
FT /evidence="ECO:0000269|PubMed:19017797"
FT DISULFID 63
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:19017797"
FT DISULFID 80..171
FT /evidence="ECO:0000269|PubMed:19017797"
FT DISULFID 134..178
FT /evidence="ECO:0000269|PubMed:19017797"
FT DISULFID 189
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 191
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 182..476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001189"
FT VARIANT 292
FT /note="D -> G"
FT VARIANT 345
FT /note="S -> P"
FT CONFLICT 3
FT /note="Missing (in Ref. 7; AAA37480)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="A -> R (in Ref. 7; AAA37480)"
FT /evidence="ECO:0000305"
FT CONFLICT 7..8
FT /note="AG -> PR (in Ref. 7; AAA37480)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="P -> A (in Ref. 1; CAA28660)"
FT /evidence="ECO:0000305"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:3EJJ"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:3EJJ"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:3EJJ"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:3EJJ"
FT HELIX 78..95
FT /evidence="ECO:0007829|PDB:3EJJ"
FT HELIX 104..118
FT /evidence="ECO:0007829|PDB:3EJJ"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3EJJ"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:3EJJ"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:3EJJ"
FT HELIX 142..162
FT /evidence="ECO:0007829|PDB:3EJJ"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:3EJJ"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:3EJJ"
SQ SEQUENCE 552 AA; 60649 MW; 3886D72D70E770AF CRC64;
MTARGAAGRC PSSTWLGSRL LLVCLLMSRS IAKEVSEHCS HMIGNGHLKV LQQLIDSQME
TSCQIAFEFV DQEQLDDPVC YLKKAFFLVQ DIIDETMRFK DNTPNANATE RLQELSNNLN
SCFTKDYEEQ NKACVRTFHE TPLQLLEKIK NFFNETKNLL EKDWNIFTKN CNNSFAKCSS
RDVVTKPDCN CLYPKATPSS DPASASPHQP PAPSMAPLAG LAWDDSQRTE GSSLLPSELP
LRIEDPGSAK QRPPRSTCQT LESTEQPNHG DRLTEDSQPH PSAGGPVPGV EDILESSLGT
NWVLEEASGE ASEGFLTQEA KFSPSTPVGG SIQAETDRPR ALSASPFPKS TEDQKPVDIT
DRPLTEVNPM RPIGQTQNNT PEKTDGTSTL REDHQEPGSP HIATPNPQRV SNSATPVAQL
LLPKSHSWGI VLPLGELEGK RSTRDRRSPA ELEGGSASEG AARPVARFNS IPLTDTGHVE
QHEGSSDPQI PESVFHLLVP GIILVLLTVG GLLFYKWKWR SHRDPQTLDS SVGRPEDSSL
TQDEDRQVEL PV
