CFMB_ARTBC
ID CFMB_ARTBC Reviewed; 186 AA.
AC D4B2Q8;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=GPI-anchored hemophore ARB_02741 {ECO:0000305};
DE AltName: Full=GPI-anchored CFEM domain protein ARB_02741 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_02741;
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}.
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DR EMBL; ABSU01000030; EFE30369.1; -; Genomic_DNA.
DR RefSeq; XP_003011009.1; XM_003010963.1.
DR AlphaFoldDB; D4B2Q8; -.
DR SMR; D4B2Q8; -.
DR EnsemblFungi; EFE30369; EFE30369; ARB_02741.
DR GeneID; 9525126; -.
DR KEGG; abe:ARB_02741; -.
DR eggNOG; ENOG502SD7M; Eukaryota.
DR HOGENOM; CLU_063084_2_1_1; -.
DR OMA; PCVQKAC; -.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..163
FT /note="GPI-anchored hemophore ARB_02741"
FT /id="PRO_5003054633"
FT PROPEP 164..186
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434906"
FT REGION 20..85
FT /note="CFEM"
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT REGION 89..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..159
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 163
FT /note="GPI-anchor amidated glycine"
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 186 AA; 18266 MW; 324FEB28B595568C CRC64;
MKFSQAVIAL AAATVVSAQL PDVPQCSLPC FLDALTTDGC SELTDFKCHC SKPELPAKIT
PCVKSKCPVA EQVSVSNAVV KQCSEAGAPV SIPPVEESSS KPSEPSTSEA PTASPTESTP
APTTPAPTGT GSPSGTGAPG GPSGTGTFTN TGVPTQSTPI YTGAASGLSA NIGGMGAAIL
AIAAYL
