ID   CFMC_ARTBC              Reviewed;         188 AA.
AC   D4AXU8;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=GPI-anchored hemophore ARB_01017 {ECO:0000305};
DE   AltName: Full=GPI-anchored CFEM domain protein ARB_01017 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_01017;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: GPI-anchored cell wall protein involved in stabilizing the
CC       cell wall (By similarity). {ECO:0000250|UniProtKB:Q4WLB9}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:D4AZC5}.
CC       Secreted, cell wall {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   -!- SIMILARITY: Belongs to the RBT5 family. {ECO:0000305}.
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DR   EMBL; ABSU01000017; EFE32126.1; -; Genomic_DNA.
DR   RefSeq; XP_003012766.1; XM_003012720.1.
DR   AlphaFoldDB; D4AXU8; -.
DR   SMR; D4AXU8; -.
DR   EnsemblFungi; EFE32126; EFE32126; ARB_01017.
DR   GeneID; 9522844; -.
DR   KEGG; abe:ARB_01017; -.
DR   eggNOG; ENOG502SD7M; Eukaryota.
DR   HOGENOM; CLU_063084_1_1_1; -.
DR   OMA; DVACCIA; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..165
FT                   /note="GPI-anchored hemophore ARB_01017"
FT                   /id="PRO_5003053753"
FT   PROPEP          166..188
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434926"
FT   REGION          20..81
FT                   /note="CFEM"
FT                   /evidence="ECO:0000305"
FT   REGION          95..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42
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           165
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..64
FT                   /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT   DISULFID        30..59
FT                   /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT   DISULFID        39..45
FT                   /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT   DISULFID        47..80
FT                   /evidence="ECO:0000250|UniProtKB:Q5A0X8"
SQ   SEQUENCE   188 AA;  17726 MW;  97FF7F197ADF347D CRC64;
     MKLSVVALAA LVSVAAAQGV SELPKCAQDC ASKGFPSSCG ADVKCVCTSN SFLDAITCCV
     ATTCTAEEQK KTIQFAKGIC GGVGVNVPDS AVCPTGGSSS SGSASSTPTS SGGSSSETGS
     VTGTAITGTN SPTPTSRRPS GSSTAHSSGS GSPATSTGAP TQTGNAAASV NANGGLLAAI
     AALVIAVA