ALS1_ARTBC
ID ALS1_ARTBC Reviewed; 890 AA.
AC D4B1B1;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Agglutinin-like protein ARB_02240 {ECO:0000305};
DE AltName: Full=Adhesin ARB_02240 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_02240;
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: Cell surface adhesion protein which mediates cell
CC agglutination and host tissue adherence (By similarity).
CC {ECO:0000250|UniProtKB:Q5A8T4}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}. Cell
CC membrane {ECO:0000250|UniProtKB:Q5A8T4}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:Q5A8T4}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:Q5A8T4}.
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 ALS family. {ECO:0000305}.
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DR EMBL; ABSU01000025; EFE31046.1; -; Genomic_DNA.
DR RefSeq; XP_003011686.1; XM_003011640.1.
DR AlphaFoldDB; D4B1B1; -.
DR EnsemblFungi; EFE31046; EFE31046; ARB_02240.
DR GeneID; 9523457; -.
DR KEGG; abe:ARB_02240; -.
DR eggNOG; ENOG502S2BG; Eukaryota.
DR HOGENOM; CLU_324440_0_0_1; -.
DR OMA; KRDMSLW; -.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cell wall; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..864
FT /note="Agglutinin-like protein ARB_02240"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434673"
FT PROPEP 865..890
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434674"
FT REGION 680..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 864
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 890 AA; 93181 MW; 891B0D1351703B20 CRC64;
MRLTTSVLLW AATSVLQADA TQTYRSPTGP EAYGAYPPRY TVSYTTITST STIHSCPPRT
TTIFTSSPPP DDGCKFPGCP NQPPKPGSDV HCDIYCWAKG CSLCKNDTCP EQGGIYKRRE
DMKNIFGRST GSAEGYNYTP ETTCCCCCEP GGGKHTVTVT KTKTETKTET ASITKIITDY
VTKTVLIPTT VLEPTTIIDP TTVPTTVPTT IPTTVYNETT IHDSTTVSTT VIQPTTISDT
TTLTTTFTTV VPTYITTTTF GTVTSVVTVM VPTTITSTYV STMYTTLPGT TLTTSVTVPG
PTVTPPPVTL PPETKIITLP ASTVTKVTTL PASTMTVTST LPASTITQSG TTVTLPGSTT
VITSTIPAST ITQTYTEPGT VSTVTSTPPP ETHVITLPGS TITKVTTLPG TIMTVTQTLP
ASTVTQSGTT VTIPASTTVI TTTLPASTIT QTLTEPGKEI TVTKTNTVTT TTTSFSISLC
PTRTANPTYT PLAPLPSNYI WGCPPGQLCR PKRTPADGQC NFEVGLPSQN FVCSPDECIP
SPPRHPPQKW TPGKVEKWVV SPGYFNIDPR KFGLTFDIFS FENVTATSQG YFRRSLSALF
KRGPEIVAGE CYDECDSAAT EAEAVGADPT LCKPDSLFMK LVGQCKKCTN DRSNGTYSDF
DTVLFPEFQK WLDYCDTLPI PSGPTTRPEP GMTSSTTSSP THSTVITSMT SMTTSESSTS
MRSSSTATTS ETSSTESSRT SSESSTESST DSSTTERTRT TSTAESTETT EPTSTDASTE
STSTATHSST GSDPESTNTR HPSSTASGST TTRGGGGGHG SSSSEGPVPT SMGTATTTGG
GSIPGSGTGI PPSSSTDPVP FPGGAGSLSP STWGKVVTCI SSMALLVAFI
