ECM33_ARTBC
ID ECM33_ARTBC Reviewed; 387 AA.
AC D4AZK9;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Cell surface GPI-anchored protein ARB_01627 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_01627;
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: Required for proper cell wall integrity and for the correct
CC assembly of the mannoprotein outer layer of the cell wall.
CC {ECO:0000250|UniProtKB:P38248}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P38248};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P38248}. Secreted
CC {ECO:0000269|PubMed:21919205}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:P38248}. Note=Identified as GPI-anchored plasma
CC membrane protein (GPI-PMP) as well as covalently-linked GPI-modified
CC cell wall protein (GPI-CWP) in the outer cell wall layer.
CC {ECO:0000250|UniProtKB:P38248}.
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 SPS2 family. {ECO:0000305}.
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DR EMBL; ABSU01000021; EFE31479.1; -; Genomic_DNA.
DR RefSeq; XP_003012119.1; XM_003012073.1.
DR AlphaFoldDB; D4AZK9; -.
DR SMR; D4AZK9; -.
DR STRING; 663331.D4AZK9; -.
DR EnsemblFungi; EFE31479; EFE31479; ARB_01627.
DR GeneID; 9519687; -.
DR KEGG; abe:ARB_01627; -.
DR eggNOG; ENOG502QUZC; Eukaryota.
DR HOGENOM; CLU_035846_0_1_1; -.
DR OMA; GGFQIAR; -.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..364
FT /note="Cell surface GPI-anchored protein ARB_01627"
FT /id="PRO_0000434928"
FT PROPEP 365..387
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434929"
FT REGION 338..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 364
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 387 AA; 41257 MW; 90E4AAF6655E1BAB CRC64;
MAITKYLVSA LAVAGLAFAK DCAGDLTIEN QQDVSTLSSC EKWDGDIVIS EVVKSSISLT
GVKQITGSLK AKNSSITELS APNLNSIGDA LSLSTCTALR SLDLSSLTKV KTLSLEALPK
LQALGFTRTV SQATSILITN TDLTSLQGLD LETVGDFMVT NNPHLMEINV NKMTNITGYL
NFAANNKQLS VKFPNLEGAH NMTFRNVSDA SLPSLHKMDG LLGFYSNFFM NISAPNLTAT
GDLVFTSNSA VMNISMPKLE TVKGGLQLAN NSLLEDIEGF PALKLITGAL DITGKFKTVK
LPSLKEVRGD ANLQSTETFG CDPWQKLKDS DVIRGKLTCR ERQEKPKTGD DHSGGDEEGH
KGAAAAFAKA PAAALLIAFV GALQFFL
