CFMA_ASPFU
ID CFMA_ASPFU Reviewed; 305 AA.
AC Q4WLB9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=GPI-anchored hemophore cfmA {ECO:0000305};
DE AltName: Full=GPI-anchored CFEM domain protein A {ECO:0000303|PubMed:24361821};
DE Flags: Precursor;
GN Name=cfmA {ECO:0000303|PubMed:24361821}; ORFNames=AFUA_6G14090;
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 PROTEIN SEQUENCE OF 49-61, GPI-ANCHOR, AND SUBCELLULAR LOCATION.
RX PubMed=11545413;
RX DOI=10.1002/1522-2683(200108)22:13<2812::aid-elps2812>3.0.co;2-q;
RA Bruneau J.-M., Magnin T., Tagat E., Legrand R., Bernard M., Diaquin M.,
RA Fudali C., Latge J.-P.;
RT "Proteome analysis of Aspergillus fumigatus identifies
RT glycosylphosphatidylinositol-anchored proteins associated to the cell wall
RT biosynthesis.";
RL Electrophoresis 22:2812-2823(2001).
RN [3]
RP STRUCTURE OF GPI-ANCHOR.
RX PubMed=12626404; DOI=10.1093/glycob/cwg004;
RA Fontaine T., Magnin T., Melhert A., Lamont D., Latge J.-P.,
RA Ferguson M.A.J.;
RT "Structures of the glycosylphosphatidylinositol membrane anchors from
RT Aspergillus fumigatus membrane proteins.";
RL Glycobiology 13:169-177(2003).
RN [4]
RP 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:0000269|PubMed:11545413}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:11545413, ECO:0000269|PubMed:12626404}. Note=Found
CC anchored in the cell membrane as well as a covalently-linked GPI-
CC modified cell wall protein (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-like anchor contains a phosphoceramide lipid group.
CC {ECO:0000269|PubMed:12626404}.
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; EAL89245.1; -; Genomic_DNA.
DR RefSeq; XP_751283.1; XM_746190.1.
DR AlphaFoldDB; Q4WLB9; -.
DR STRING; 746128.CADAFUBP00000066; -.
DR EnsemblFungi; EAL89245; EAL89245; AFUA_6G14090.
DR GeneID; 3508600; -.
DR KEGG; afm:AFUA_6G14090; -.
DR VEuPathDB; FungiDB:Afu6g14090; -.
DR eggNOG; ENOG502S1H2; Eukaryota.
DR HOGENOM; CLU_063084_0_0_1; -.
DR InParanoid; Q4WLB9; -.
DR OMA; MISIVAD; -.
DR OrthoDB; 1576685at2759; -.
DR PHI-base; PHI:4015; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:AspGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR008427; Extracellular_membr_CFEM_dom.
DR Pfam; PF05730; CFEM; 1.
DR SMART; SM00747; CFEM; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; GPI-anchor; Heme; Iron; Lipoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..276
FT /note="GPI-anchored hemophore cfmA"
FT /id="PRO_0000245562"
FT PROPEP 277..305
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000245563"
FT REGION 19..95
FT /note="CFEM"
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT REGION 92..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
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 276
FT /note="GPI-like-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..68
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 29..63
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 42..49
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 51..84
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
SQ SEQUENCE 305 AA; 26811 MW; 7020D67C59D4DC07 CRC64;
MKASVSLLLL SAASMASAAM SVSQCAQMCL SNMKAKAGEL GCSAGDDKCL CSQANYGYGI
RDCTTEACPD DDAIAVLSSA LSSCPSDSAA VTATGAGGSS SGSGSGSDSG SGSGSGSGSG
SGSGSGSGSS SGSGSGSGSG SGSGSGSNSG SGSASSTATG TATGTATGTA TGTATGTATG
SENSTTGGAG AGAGAGASST GTNASGTGAT TSGANPSNTG ATTTDTTLTT TTTSSENGSS
TGNSSSETGA GSGSSTATGS GSGSGAGSAS TTAPNSSSTG NVAPRGAVVG SGAVGALALA
ALIIL
