PRY1_ARTBC
ID PRY1_ARTBC Reviewed; 309 AA.
AC D4B327;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Probable pathogenesis-related protein ARB_02861 {ECO:0000305};
DE AltName: Full=Wasp ves v 5 allergen homolog {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_02861;
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: Secreted protein required for efficient export of lipids such
CC as acetylated sterols. Acts in detoxification of hydrophobic compounds.
CC {ECO:0000250|UniProtKB:P47032}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P47032}.
CC -!- DOMAIN: The SCP domain is necessary and sufficient for lipid export and
CC sterol-binding. {ECO:0000250|UniProtKB:P47032}.
CC -!- ALLERGEN: May cause an allergic reaction in human. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE30323.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; ABSU01000031; EFE30323.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003010963.1; XM_003010917.1.
DR AlphaFoldDB; D4B327; -.
DR SMR; D4B327; -.
DR STRING; 663331.D4B327; -.
DR EnsemblFungi; EFE30323; EFE30323; ARB_02861.
DR GeneID; 9525080; -.
DR KEGG; abe:ARB_02861; -.
DR eggNOG; KOG3017; Eukaryota.
DR HOGENOM; CLU_035730_5_0_1; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.33.10; -; 1.
DR InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR InterPro; IPR014044; CAP_domain.
DR InterPro; IPR035940; CAP_sf.
DR InterPro; IPR001283; CRISP-related.
DR PANTHER; PTHR10334; PTHR10334; 1.
DR Pfam; PF00188; CAP; 1.
DR PRINTS; PR00837; V5TPXLIKE.
DR SMART; SM00198; SCP; 1.
DR SUPFAM; SSF55797; SSF55797; 1.
DR PROSITE; PS01009; CRISP_1; 1.
PE 3: Inferred from homology;
KW Allergen; Glycoprotein; Lipid transport; Lipid-binding; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..309
FT /note="Probable pathogenesis-related protein ARB_02861"
FT /id="PRO_0000434918"
FT DOMAIN 154..284
FT /note="SCP"
FT /evidence="ECO:0000250|UniProtKB:P47032"
FT REGION 47..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 309 AA; 32027 MW; 262BE27DBF0305FB CRC64;
MKSSVLMTAL CVAGSLAAEQ ISPPNEVVVT AKKVVVVTTT VTTTIPCPTV IPTTSYKPEP
TSKPPVIPPV PTSSAEPLPP PPVEPSTIPC PEPGTSTYAP PPPPPPPTSA PAPPAPPPPP
PSSAPAPPAP PPSQPSQGPA PPPPPPGKDY KEVAGYHHNV HRSNHSAPAL TWSSALESSA
RKLAESCNYG HDTSIDGGGY GQNIGYQSGY NNVAALLTEQ MYNEEAILFE GNYGNNNPSN
FHSWGHFTQM VWIGTTHVGC FTAHCSNLGG QGSGGDAYYT VCNYSPPGNV LGQYAENVKP
PKGQPVVTV