CFMA_ARTBC
ID CFMA_ARTBC Reviewed; 264 AA.
AC D4AZC5;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 2.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=GPI-anchored hemophore ARB_01545 {ECO:0000305};
DE AltName: Full=GPI-anchored CFEM domain protein ARB_01545 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_01545;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(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:0000269|PubMed:21919205}. Secreted,
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE31645.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; ABSU01000020; EFE31645.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003012285.1; XM_003012239.1.
DR AlphaFoldDB; D4AZC5; -.
DR SMR; D4AZC5; -.
DR STRING; 63400.XP_003012285.1; -.
DR EnsemblFungi; EFE31645; EFE31645; ARB_01545.
DR GeneID; 9519934; -.
DR KEGG; abe:ARB_01545; -.
DR eggNOG; ENOG502S1H2; Eukaryota.
DR HOGENOM; CLU_063084_0_1_1; -.
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.
DR SMART; SM00747; CFEM; 1.
PE 1: Evidence at protein level;
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..240
FT /note="GPI-anchored hemophore ARB_01545"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434670"
FT PROPEP 241..264
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434671"
FT REGION 21..115
FT /note="CFEM"
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT REGION 86..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48
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 240
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT DISULFID 27..70
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 31..65
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 44..51
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 53..86
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
SQ SEQUENCE 264 AA; 24819 MW; 008A5BD3A5727535 CRC64;
MKASVIVSVA LGASMCLATT LAELPACSQA CLQSMLGKAA ELGCPPHDPG CLCSHPDFTN
GLRDCTKEAC PGENIEKVVE EGQKACKDMG GAPGSSTGAP TTGTGSGTAT GTPTSGSGSE
TTAPPTSGSG SAPAPTSGGH STPYTTIPAG PTVITSGTNV ITTSRPATTL YTEVSGSQSG
SESGSSTGSG SESTSGPEPT SATSSEGGSS PSSTEGSGGS GGSGGSETSG SGNGPSPTPS
QGMAPKATGL GVAGAIGLVA LLAL
