ECM33_ASPFU
ID ECM33_ASPFU Reviewed; 398 AA.
AC Q4WNS8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Protein ecm33;
DE Flags: Precursor;
GN Name=ecm33; ORFNames=AFUA_4G06820;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP PROTEIN SEQUENCE OF 275-283 AND 288-298, AND GPI-ANCHOR.
RX PubMed=11545413;
RX DOI=10.1002/1522-2683(200108)22:13<2812::aid-elps2812>3.0.co;2-q;
RA Bruneau J.-M., Magnin T., Tagat E., Legrand R., Bernard M., Diaquin M.,
RA Fudali C., Latge J.-P.;
RT "Proteome analysis of Aspergillus fumigatus identifies
RT glycosylphosphatidylinositol-anchored proteins associated to the cell wall
RT biosynthesis.";
RL Electrophoresis 22:2812-2823(2001).
RN [3]
RP PROTEIN SEQUENCE OF 235-249, AND STRUCTURE OF GPI-ANCHOR.
RX PubMed=12626404; DOI=10.1093/glycob/cwg004;
RA Fontaine T., Magnin T., Melhert A., Lamont D., Latge J.-P.,
RA Ferguson M.A.J.;
RT "Structures of the glycosylphosphatidylinositol membrane anchors from
RT Aspergillus fumigatus membrane proteins.";
RL Glycobiology 13:169-177(2003).
RN [4]
RP FUNCTION.
RX PubMed=16672465; DOI=10.1128/aem.72.5.3259-3267.2006;
RA Chabane S., Sarfati J., Ibrahim-Granet O., Du C., Schmidt C., Mouyna I.,
RA Prevost M.-C., Calderone R., Latge J.-P.;
RT "Glycosylphosphatidylinositol-anchored Ecm33p influences conidial cell wall
RT biosynthesis in Aspergillus fumigatus.";
RL Appl. Environ. Microbiol. 72:3259-3267(2006).
CC -!- FUNCTION: Involved in conidial and mycelial cell wall biogenesis.
CC {ECO:0000269|PubMed:16672465}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- PTM: The GPI-like anchor contains a phosphoceramide lipid group. The
CC anchor position has not been determined.
CC -!- SIMILARITY: Belongs to the SPS2 family. {ECO:0000305}.
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DR EMBL; AAHF01000005; EAL90106.1; -; Genomic_DNA.
DR RefSeq; XP_752144.1; XM_747051.1.
DR AlphaFoldDB; Q4WNS8; -.
DR SMR; Q4WNS8; -.
DR STRING; 746128.CADAFUBP00006215; -.
DR EnsemblFungi; EAL90106; EAL90106; AFUA_4G06820.
DR GeneID; 3509473; -.
DR KEGG; afm:AFUA_4G06820; -.
DR VEuPathDB; FungiDB:Afu4g06820; -.
DR eggNOG; ENOG502QUZC; Eukaryota.
DR HOGENOM; CLU_035846_0_1_1; -.
DR InParanoid; Q4WNS8; -.
DR OMA; GGFQIAR; -.
DR OrthoDB; 1342410at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:AspGD.
DR GO; GO:0005886; C:plasma membrane; IDA:AspGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..372
FT /note="Protein ecm33"
FT /id="PRO_0000245545"
FT PROPEP 373..398
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000245546"
FT REGION 344..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 372
FT /note="GPI-like-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 244
FT /note="T -> TT (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 41505 MW; 6209DFC64391D1C4 CRC64;
MAFLKYALPA LAAAQAVLAA NCGKTDETIT ISSQSDADGY SSCSTIKGTI EIDEHLSGAI
TFNNVKQIDG TLSCTGGANI SSIAAPMLNS IADTFKLDGL TTLTTLSFPS LTSVGSIQWT
ALPQLQSLDF TKGVNEAGDV TITNTGLANL NGISLNTVGK FDITENTQLK SININNLKNA
TGLINFAGNL NSLEVELPNL SSGTNMTFRN VSAVSVPSLH NLTGQLGFWG DTFKSFSAPN
LTETGDLVFN SNSKLTNISM PALETVNGGF LITRNDELSS IDLPSLKVVT GAVDFSGKFD
EVSMPKLENV KGQFNLQSTG NFSCDTFDKA HNDKVIRGTY KCKAAEPNPT TKDGSSGTTT
SSGSSASASK SNAADLNAAN LPALGFAAVF GALVQYVL
