CALX_ARTBC
ID CALX_ARTBC Reviewed; 563 AA.
AC D4AVD4;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Calnexin homolog ARB_00147 {ECO:0000305};
DE AltName: Full=Allergen Pen ch 31 homolog {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_00147;
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: Calcium-binding protein that interacts with newly synthesized
CC monoglucosylated glycoproteins in the endoplasmic reticulum. It may act
CC in assisting protein assembly and/or in the retention within the ER of
CC unassembled protein subunits. It seems to play a major role in the
CC quality control apparatus of the ER by the retention of incorrectly
CC folded proteins. {ECO:0000250|UniProtKB:P27824}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P27824}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P27824}.
CC -!- ALLERGEN: May cause an allergic reaction in human. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR EMBL; ABSU01000012; EFE33056.1; -; Genomic_DNA.
DR RefSeq; XP_003013696.1; XM_003013650.1.
DR AlphaFoldDB; D4AVD4; -.
DR SMR; D4AVD4; -.
DR STRING; 663331.D4AVD4; -.
DR PRIDE; D4AVD4; -.
DR EnsemblFungi; EFE33056; EFE33056; ARB_00147.
DR GeneID; 9520141; -.
DR KEGG; abe:ARB_00147; -.
DR eggNOG; KOG0675; Eukaryota.
DR HOGENOM; CLU_018224_1_2_1; -.
DR OMA; SGCGKWE; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
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 3: Inferred from homology;
KW Allergen; Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..563
FT /note="Calnexin homolog ARB_00147"
FT /id="PRO_0000434932"
FT TOPO_DOM 24..496
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 240..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P27797"
FT BINDING 147
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 149
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 168
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 175
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 404
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P27797"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 143..177
FT /evidence="ECO:0000250|UniProtKB:P27797"
SQ SEQUENCE 563 AA; 62270 MW; AA531D3B0DAB517B CRC64;
MRLNAQLASL LLSSIVLVGS AHGADEEPVA EKKEASSIER PTFVPTTIKA PFVEQFTDKW
DSRWSVSHAK KEDAKSDEEW AYVGEWSVEE PTVFKGIEGD KGLVVKNPAA HHAISAKFPK
KIDNKGKTLV VQYEVKLQNS LSCGGAYMKL LQENKKLHSE EFSNASPYVI MFGPDRCGAT
NKVHFIFKHK NPKTGEYEEK HLKAPPAIKV TKLTSLYTLI VNPDQTFQIR IDGEPLKNGT
LLEDFTPPVN PPKEIDDEKD TKPADWVDEE KIPDPEAKKP EDWDEDAPFE IVDTEATKPA
DWLDDEPTTI PDPEAVKPED WDDEEDGDWI APTVPNPKCE EGSGCGKWEP PMIRNPAYKG
KWSAPLIDNP AYKGVWAPRK IPNPNYFEDK TPSNFEPMGA IGFEIWTMQN DILFDNIYIG
HSIEDAEKFK AETYDIKRPI EEAEEEASKP KLSPQIDDET DISFTQDPIG YVRAKIDRFI
SLAQDDPIAA LQAVPEVGGA IGAILASLLI IIGMFGLSSP APPAKSTGKT AEKTEKEKTT
EAVTASGADS GQGEAKKRAA KSG
