CFMB_ASPFU
ID CFMB_ASPFU Reviewed; 202 AA.
AC Q4WMA6;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=GPI-anchored hemophore cfmB {ECO:0000305};
DE AltName: Full=GPI-anchored CFEM domain protein B {ECO:0000303|PubMed:24361821};
DE Flags: Precursor;
GN Name=cfmB {ECO:0000303|PubMed:24361821}; ORFNames=AFUA_6G10580;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP DOMAIN, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=24361821; DOI=10.1016/j.fgb.2013.12.005;
RA Vaknin Y., Shadkchan Y., Levdansky E., Morozov M., Romano J., Osherov N.;
RT "The three Aspergillus fumigatus CFEM-domain GPI-anchored proteins (CfmA-C)
RT affect cell-wall stability but do not play a role in fungal virulence.";
RL Fungal Genet. Biol. 63:55-64(2014).
CC -!- FUNCTION: GPI-anchored cell wall protein involved in stabilizing the
CC cell wall. Not implicated in virulence, heme uptake and biofilm
CC formation. {ECO:0000269|PubMed:24361821}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:Q59UT4}. Cell membrane
CC {ECO:0000250|UniProtKB:Q4WLB9}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:Q4WLB9}. Note=Found anchored in the cell
CC membrane as well as a covalently-linked GPI-modified cell wall protein
CC (GPI-CWP). {ECO:0000250|UniProtKB:Q59UT4}.
CC -!- DOMAIN: The CFEM domain is involved in heme-binding and contains 8
CC cysteines and is found in proteins from several pathogenic fungi,
CC including both human and plant pathogens (By similarity). The CFEM
CC domain adopts a novel helical-basket fold that consists of six alpha-
CC helices, and is uniquely stabilized by four disulfide bonds formed by
CC its 8 signature cysteines (By similarity).
CC {ECO:0000250|UniProtKB:Q5A0X8}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Increases susceptibility towards the chitin/beta-
CC glucan-microfibril destabilizing compounds Congo red and calcofluor
CC white. {ECO:0000269|PubMed:24361821}.
CC -!- SIMILARITY: Belongs to the RBT5 family. {ECO:0000305}.
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DR EMBL; AAHF01000006; EAL88908.1; -; Genomic_DNA.
DR RefSeq; XP_750946.1; XM_745853.1.
DR AlphaFoldDB; Q4WMA6; -.
DR SMR; Q4WMA6; -.
DR EnsemblFungi; EAL88908; EAL88908; AFUA_6G10580.
DR GeneID; 3508251; -.
DR KEGG; afm:AFUA_6G10580; -.
DR VEuPathDB; FungiDB:Afu6g10580; -.
DR eggNOG; ENOG502SFDE; Eukaryota.
DR HOGENOM; CLU_063084_2_0_1; -.
DR InParanoid; Q4WMA6; -.
DR OMA; PCVQKAC; -.
DR OrthoDB; 1627841at2759; -.
DR PHI-base; PHI:4016; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR InterPro; IPR008427; Extracellular_membr_CFEM_dom.
DR Pfam; PF05730; CFEM; 1.
DR SMART; SM00747; CFEM; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall; Disulfide bond; Glycoprotein; GPI-anchor; Heme;
KW Iron; Lipoprotein; Membrane; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..180
FT /note="GPI-anchored hemophore cfmB"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431737"
FT PROPEP 181..202
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431738"
FT REGION 20..85
FT /note="CFEM"
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT REGION 94..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT LIPID 180
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..67
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 30..62
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 40..48
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 50..83
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
SQ SEQUENCE 202 AA; 19683 MW; A9A43B089C200477 CRC64;
MHFSRTSLIL FAAGLASAQL PNVPGCSLDC FVAALSADGC SSLTDFACHC QKPELVSNIT
PCVQSACNIA DQSSVSVAVV SQCSAAGHPI SVPPVGAAST TASETATTTE SSTQTTTGTS
STASKTSSSA ASSTPSSSSA SSSHHHSSSS ALTTRTLTST EPSSQSTSAS AAATTTLSGN
AGSEKANVAG VVAVAAAALY LL
