ID   FLA_ARTBC               Reviewed;         421 AA.
AC   D4B388;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Fasciclin-like arabinogalactan protein ARB_02922 {ECO:0000250|UniProtKB:O22126};
DE   Flags: Precursor;
GN   ORFNames=ARB_02922;
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: May be a cell surface adhesion protein.
CC       {ECO:0000250|UniProtKB:O22126}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC       anchor {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the fasciclin-like AGP family. {ECO:0000305}.
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DR   EMBL; ABSU01000032; EFE30243.1; -; Genomic_DNA.
DR   RefSeq; XP_003010883.1; XM_003010837.1.
DR   AlphaFoldDB; D4B388; -.
DR   SMR; D4B388; -.
DR   STRING; 663331.D4B388; -.
DR   EnsemblFungi; EFE30243; EFE30243; ARB_02922.
DR   GeneID; 9524998; -.
DR   KEGG; abe:ARB_02922; -.
DR   eggNOG; KOG1437; Eukaryota.
DR   HOGENOM; CLU_031281_2_3_1; -.
DR   OMA; IANYHIV; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.30.180.10; -; 2.
DR   InterPro; IPR036378; FAS1_dom_sf.
DR   InterPro; IPR000782; FAS1_domain.
DR   Pfam; PF02469; Fasciclin; 2.
DR   SMART; SM00554; FAS1; 2.
DR   SUPFAM; SSF82153; SSF82153; 2.
DR   PROSITE; PS50213; FAS1; 2.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..397
FT                   /note="Fasciclin-like arabinogalactan protein ARB_02922"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434496"
FT   PROPEP          398..421
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434497"
FT   DOMAIN          18..167
FT                   /note="FAS1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   DOMAIN          169..296
FT                   /note="FAS1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   REGION          300..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..319
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           397
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   421 AA;  43547 MW;  3A848F3CF43C1AE4 CRC64;
     MLLYYILVAL WATVTYAKSF SEDISEMPEL SEMSSYLNQT PEAKDVLDQQ KNVTLLALEN
     SAFRDFVGQG EGNDNQSSSN SSLLRGIFSY QLVKGLHNSE QITTTPQFSP TELNDAGFTN
     VSSGQIVQLV EKDGKDYAIS GLNDNSTIIK PGVDVENGVI HVIDRPLTLP QSVTATLQAA
     NLTSFQGALQ RGNAVSNAND PKDITLFAPR NLGFQRIGTA FENISAEDLG QIANYHIVKG
     KVLYSPDLTD ADHPTYADKD LHISTVDGRS YVNSARVEST NLLVNNGVIH VISDVLNPNN
     DTAKPVPNAD PPPPAFENAN PVSTDPLTDG IPSPTSVIPL PGITSGGEGG GGGGGESTAP
     PSPTATVTET QSGGGGGGGG GAGGGPGPTA TNTPQPGAAA TERAKAGLAA VVGLGVVLIN
     A