ID   A6477_ARTBC             Reviewed;         231 AA.
AC   D4AQH0;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Probable cell wall protein ARB_06477 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_06477;
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: Probable component of the cell wall.
CC       {ECO:0000250|UniProtKB:P47179}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC       anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:21919205}. Secreted,
CC       cell wall.
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 SRP1/TIP1 family. {ECO:0000305}.
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DR   EMBL; ABSU01000005; EFE34714.1; -; Genomic_DNA.
DR   RefSeq; XP_003015354.1; XM_003015308.1.
DR   AlphaFoldDB; D4AQH0; -.
DR   EnsemblFungi; EFE34714; EFE34714; ARB_06477.
DR   GeneID; 9521078; -.
DR   KEGG; abe:ARB_06477; -.
DR   eggNOG; ENOG502S73X; Eukaryota.
DR   HOGENOM; CLU_065618_1_2_1; -.
DR   OMA; EPTALTW; -.
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   InterPro; IPR018466; Kre9/Knh1-like_N.
DR   Pfam; PF10342; GPI-anchored; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..203
FT                   /note="Probable cell wall protein ARB_06477"
FT                   /id="PRO_5003053910"
FT   PROPEP          204..231
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000435283"
FT   REGION          107..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           203
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   231 AA;  23800 MW;  2293813D6D87A91E CRC64;
     MRSVLYLLFT AVAAVAALEN PFLVPPGGYQ FNTREPTVLN WQPTTPGTVT LKLQMSSDIT
     PHSGLVLAAH LENTGTFTFL PPPDLMQNGL YTVQIIDDND PSKYNFTPSF MVDGATGGPT
     TGPTTSRTSM TTSEATTTSG ESTTSPSSTR PSTVSPTTTD SSDTTMSTVT SSSTPTTTDS
     TTTSESTAVS STRSSSTGMP TSSGAPDPNG AVSLALPGGL LSIVLSLMAL L