CALX_ASPFU
ID CALX_ASPFU Reviewed; 563 AA.
AC Q6Q487; Q4WQH5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Calnexin homolog;
DE Flags: Precursor;
GN ORFNames=AFUA_4G12850;
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 [MRNA].
RC STRAIN=YJ-407;
RA Zhang L., Jin C.;
RT "Calnexin from Aspergillus fumigatus YJ-407.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
CC -!- FUNCTION: Interacts with newly synthesized monoglucosylated
CC glycoproteins in the endoplasmic reticulum. It may act in assisting
CC protein assembly and/or in the retention within the ER of unassembled
CC protein subunits. It seems to play a major role in the quality control
CC apparatus of the ER by the retention of incorrectly folded proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY560606; AAS68033.1; -; mRNA.
DR EMBL; AAHF01000005; EAL89509.1; -; Genomic_DNA.
DR RefSeq; XP_751547.1; XM_746454.1.
DR AlphaFoldDB; Q6Q487; -.
DR SMR; Q6Q487; -.
DR STRING; 746128.CADAFUBP00006796; -.
DR EnsemblFungi; EAL89509; EAL89509; AFUA_4G12850.
DR GeneID; 3509033; -.
DR KEGG; afm:AFUA_4G12850; -.
DR VEuPathDB; FungiDB:Afu4g12850; -.
DR eggNOG; KOG0675; Eukaryota.
DR HOGENOM; CLU_018224_1_2_1; -.
DR InParanoid; Q6Q487; -.
DR OMA; SGCGKWE; -.
DR OrthoDB; 775337at2759; -.
DR PHI-base; PHI:2306; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0034605; P:cellular response to heat; IMP:AspGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:AspGD.
DR GO; GO:0006457; P:protein folding; IMP:AspGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 2.10.250.10; -; 1.
DR InterPro; IPR001580; Calret/calnex.
DR InterPro; IPR018124; Calret/calnex_CS.
DR InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR11073; PTHR11073; 1.
DR Pfam; PF00262; Calreticulin; 1.
DR PRINTS; PR00626; CALRETICULIN.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF63887; SSF63887; 1.
DR PROSITE; PS00803; CALRETICULIN_1; 1.
DR PROSITE; PS00804; CALRETICULIN_2; 1.
DR PROSITE; PS00805; CALRETICULIN_REPEAT; 2.
PE 2: Evidence at transcript level;
KW Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..563
FT /note="Calnexin homolog"
FT /id="PRO_0000043348"
FT TOPO_DOM 24..493
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 241..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..386
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250"
FT REGION 521..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..307
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 147
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 166
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 173
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 402
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 141..175
FT /evidence="ECO:0000250"
FT DISULFID 337..343
FT /evidence="ECO:0000250"
FT CONFLICT 332
FT /note="V -> G (in Ref. 1; AAS68033)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="S -> P (in Ref. 1; AAS68033)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="G -> D (in Ref. 1; AAS68033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 563 AA; 61854 MW; 9D4E5020A7E53F84 CRC64;
MRFNAAITGA LVSSATLMGQ AHAEETEKKA DATSLVEKPT FTPTTIEAPF LEQFTADWDS
RWTPSHAKKE DSKSEEDWAY VGEWAVEEPT VLNGMVGDKG LVVKNVAAHH AISAKFPKKI
DNKGKTLVVQ YEVKPQNSLV CGGAYMKLLQ ENKKLHAEEF SNATPYVIMF GPDKCGATNK
VHFIFRHKNP KTGEYEEKHM TAPPAARTTK LTTLYTLIVK PDQSFQILID GEAVKNGTLL
EDFAPPVNPE KEIDDPKDKK PADWVDEAKI PDPEAKKPDD WDEDAPYEIV DEEATMPEDW
LEDEPTSIPD PEAEKPEDWD DEEDGDWIPP TVPNPKCNEV SGCGPWTPPM KKNPAYKGKW
TAPLIDNPAY KGIWKPRKIP NPAYFEDKTP SNFEPMGAVG FEIWTMQNDI LFDNIYIGHS
IEDAEKLRKE TFDLKHPVEV ALEEASKPKL EEKAATPSVS FKEAPVTYVR EKVDYFVGLA
KQDPINAVKQ VPEVAGGLGA LLLTMILVIV GAVGASSPAP AAAAKKGKEA ASAAKEKASE
AVSSAADTAK GAATKRNTRS SAQ
