CBP1_AJECG
ID CBP1_AJECG Reviewed; 110 AA.
AC O42720; C0NRM0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Calcium-binding protein;
DE Short=CBP;
DE Flags: Precursor;
GN Name=CBP1; ORFNames=HCBG_05800;
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 33-64.
RX PubMed=9489665; DOI=10.1046/j.1365-2958.1998.00697.x;
RA Batanghari J.W., Deepe G.S. Jr., Di Cera E., Goldman W.E.;
RT "Histoplasma acquisition of calcium and expression of CBP1 during
RT intracellular parasitism.";
RL Mol. Microbiol. 27:531-539(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION, AND MASS SPECTROMETRY.
RX PubMed=9393824; DOI=10.1128/iai.65.12.5257-5261.1997;
RA Batanghari J.W., Goldman W.E.;
RT "Calcium dependence and binding in cultures of Histoplasma capsulatum.";
RL Infect. Immun. 65:5257-5261(1997).
RN [4]
RP INDUCTION.
RX PubMed=11207606; DOI=10.1046/j.1462-5822.2000.00078.x;
RA Kuegler S., Young B., Miller V.L., Goldman W.E.;
RT "Monitoring phase-specific gene expression in Histoplasma capsulatum with
RT telomeric GFP fusion plasmids.";
RL Cell. Microbiol. 2:537-547(2000).
RN [5]
RP FUNCTION.
RX PubMed=11082066; DOI=10.1126/science.290.5495.1368;
RA Sebghati T.S., Engle J.T., Goldman W.E.;
RT "Intracellular parasitism by Histoplasma capsulatum: fungal virulence and
RT calcium dependence.";
RL Science 290:1368-1372(2000).
RN [6]
RP SUBUNIT, DISULFIDE BONDS, MASS SPECTROMETRY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=18361504; DOI=10.1021/bi701495v;
RA Beck M.R., DeKoster G.T., Hambly D.M., Gross M.L., Cistola D.P.,
RA Goldman W.E.;
RT "Structural features responsible for the biological stability of
RT Histoplasma's virulence factor CBP.";
RL Biochemistry 47:4427-4438(2008).
RN [7]
RP STRUCTURE BY NMR OF 33-110, DISULFIDE BONDS, AND FUNCTION.
RX PubMed=19298372; DOI=10.1111/j.1365-2958.2009.06647.x;
RA Beck M.R., Dekoster G.T., Cistola D.P., Goldman W.E.;
RT "NMR structure of a fungal virulence factor reveals structural homology
RT with mammalian saposin B.";
RL Mol. Microbiol. 72:344-353(2009).
CC -!- FUNCTION: Involved in calcium binding and uptake in yeast phase.
CC Required for growth in limiting calcium conditions and for yeast
CC survival in host macrophages. Is able to bind a variety of lipids.
CC {ECO:0000269|PubMed:11082066, ECO:0000269|PubMed:19298372}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per monomer.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable up to 53 degrees Celsius. {ECO:0000269|PubMed:18361504};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18361504}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- DEVELOPMENTAL STAGE: Expressed in the yeast phase during infection, and
CC not in mycelia.
CC -!- INDUCTION: Most abundant protein released by H.capsulatum. Its
CC production continues as the yeast multiplies inside host cells.
CC {ECO:0000269|PubMed:11207606}.
CC -!- PTM: May be glycosylated.
CC -!- MASS SPECTROMETRY: Mass=7858.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9393824};
CC -!- MASS SPECTROMETRY: Mass=7855.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18361504};
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DR EMBL; AF006209; AAC39354.1; -; Genomic_DNA.
DR EMBL; GG663370; EEH05536.1; -; Genomic_DNA.
DR PDB; 2JV7; NMR; -; A/B=33-110.
DR PDBsum; 2JV7; -.
DR AlphaFoldDB; O42720; -.
DR SMR; O42720; -.
DR EnsemblFungi; EEH05536; EEH05536; HCBG_05800.
DR VEuPathDB; FungiDB:HCBG_05800; -.
DR HOGENOM; CLU_2170308_0_0_1; -.
DR OrthoDB; 1866936at2759; -.
DR EvolutionaryTrace; O42720; -.
DR PHI-base; PHI:163; -.
DR PHI-base; PHI:5046; -.
DR PHI-base; PHI:7602; -.
DR Proteomes; UP000001631; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR InterPro; IPR022013; CBP.
DR Pfam; PF12192; CBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:9489665"
FT CHAIN 33..110
FT /note="Calcium-binding protein"
FT /id="PRO_0000020844"
FT DISULFID 60..108
FT DISULFID 65..105
FT DISULFID 76..93
FT HELIX 37..58
FT /evidence="ECO:0007829|PDB:2JV7"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:2JV7"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:2JV7"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2JV7"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:2JV7"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:2JV7"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2JV7"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2JV7"
SQ SEQUENCE 110 AA; 11014 MW; BD98F2FA1B4C77CE CRC64;
MLFSKVIAPA FILLGAASAA PGGLAPENAS KRDQPSVGDA FDKYNEAVRV FTQLSSAANC
DWAACLSSLS ASSAACIAAV GELGLDVPLD LACAATATSS ATEACKGCLW
