CFMC_ASPFU
ID CFMC_ASPFU Reviewed; 198 AA.
AC Q4WNE1;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=GPI-anchored hemophore cfmC {ECO:0000305};
DE AltName: Full=GPI anchored CFEM domain protein C {ECO:0000303|PubMed:24361821};
DE Flags: Precursor;
GN Name=cfmC {ECO:0000303|PubMed:24361821}; ORFNames=AFUA_6G06690;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAHF01000006; EAL88523.1; -; Genomic_DNA.
DR RefSeq; XP_750561.1; XM_745468.1.
DR AlphaFoldDB; Q4WNE1; -.
DR SMR; Q4WNE1; -.
DR EnsemblFungi; EAL88523; EAL88523; AFUA_6G06690.
DR GeneID; 3508768; -.
DR KEGG; afm:AFUA_6G06690; -.
DR eggNOG; ENOG502SD7M; Eukaryota.
DR HOGENOM; CLU_063084_1_1_1; -.
DR InParanoid; Q4WNE1; -.
DR OMA; DVACCIA; -.
DR OrthoDB; 1627841at2759; -.
DR PHI-base; PHI:4017; -.
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.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..172
FT /note="GPI-anchored hemophore cfmC"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431739"
FT PROPEP 173..198
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431740"
FT REGION 22..92
FT /note="CFEM"
FT REGION 99..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
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 172
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 28..66
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 32..61
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 41..47
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 49..91
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
SQ SEQUENCE 198 AA; 19454 MW; 40D7A3234969CD7E CRC64;
MKFFSVSLAL AACLSMAAAQ GLDGLPDCAK SCATNSIPAS CGLDVKCICT DSSFISGISC
CVLQSCGPDQ QQEDAHPFFP TAAVEFANRI CKTAGVTNMP QSPSCANTTQ SATGTASKSS
TATSGSSTES NASQTAATAT TSTTPPTSPT SPTSTTGSTT SSAASTTNTT TGAAVTQHKD
IGLIALAGAA LAAFGLLA
