ID   CNE1_USTMA              Reviewed;         523 AA.
AC   A0A0D1C6P2;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Calnexin {ECO:0000303|PubMed:24280385};
DE   Flags: Fragment;
GN   Name=CNE1 {ECO:0000303|PubMed:24280385}; ORFNames=UMAG_10287;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   REVIEW ON FUNCTION.
RX   PubMed=16467570; DOI=10.1242/jcs.02856;
RA   Williams D.B.;
RT   "Beyond lectins: the calnexin/calreticulin chaperone system of the
RT   endoplasmic reticulum.";
RL   J. Cell Sci. 119:615-623(2006).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24280385; DOI=10.1105/tpc.113.115691;
RA   Fernandez-Alvarez A., Elias-Villalobos A., Jimenez-Martin A.,
RA   Marin-Menguiano M., Ibeas J.I.;
RT   "Endoplasmic reticulum glucosidases and protein quality control factors
RT   cooperate to establish biotrophy in Ustilago maydis.";
RL   Plant Cell 25:4676-4690(2013).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP   BIP1, INDUCTION, AND DOMAIN.
RX   PubMed=26487566; DOI=10.1111/nph.13703;
RA   Lo Presti L., Lopez Diaz C., Turra D., Di Pietro A., Hampel M., Heimel K.,
RA   Kahmann R.;
RT   "A conserved co-chaperone is required for virulence in fungal plant
RT   pathogens.";
RL   New Phytol. 209:1135-1148(2016).
CC   -!- FUNCTION: Endoplasmic reticulum (ER) chaperone that functions to
CC       stabilize non-native glycoproteins and retain them in the ER until they
CC       are properly folded or targeted for ER associated degradation (ERAD)
CC       (Probable). Is essential for avoiding plant defense responses in cells
CC       with defective N-glycoproteins processing (PubMed:24280385). With co-
CC       chaperone DNJ1, coordinately functions during the tunicamycin-induced
CC       unfolded protein response (UPR) (PubMed:26487566). During biotrophic
CC       development, the UPR-associated function of DNJ1 appears to be more
CC       important than that of CNE1 (PubMed:26487566).
CC       {ECO:0000269|PubMed:24280385, ECO:0000269|PubMed:26487566,
CC       ECO:0000305|PubMed:16467570}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:26487566}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Expression is increased in the absence of DNJ1.
CC       {ECO:0000269|PubMed:26487566}.
CC   -!- DISRUPTION PHENOTYPE: Leads only to slight reduction of virulence
CC       (PubMed:24280385, PubMed:26487566). Severely affects growth and
CC       displays an altered morphology, when the calnexin DNJ1 is also deleted
CC       (PubMed:26487566). {ECO:0000269|PubMed:24280385,
CC       ECO:0000269|PubMed:26487566}.
CC   -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR   EMBL; CM003145; KIS69272.1; -; Genomic_DNA.
DR   RefSeq; XP_011389173.1; XM_011390871.1.
DR   STRING; 237631.A0A0D1C6P2; -.
DR   EnsemblFungi; KIS69272; KIS69272; UMAG_10287.
DR   GeneID; 23566338; -.
DR   KEGG; uma:UMAG_10287; -.
DR   VEuPathDB; FungiDB:UMAG_10287; -.
DR   OrthoDB; 775337at2759; -.
DR   Proteomes; UP000000561; Chromosome 6.
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:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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; 1.
DR   SUPFAM; SSF63887; SSF63887; 1.
DR   PROSITE; PS00803; CALRETICULIN_1; 1.
DR   PROSITE; PS00804; CALRETICULIN_2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           <1..523
FT                   /note="Calnexin"
FT                   /id="PRO_0000454650"
FT   TOPO_DOM        1..440
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        462..523
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          191..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   523 AA;  57409 MW;  A63D5772ED62498C CRC64;
     IEQFTSDWSE RWSTSQASKF QREDDTEAFK YDGVWSVEEP EVFPGLAGDA GLVLKSKAKQ
     HAISHLFDSP IDPKGKPLVV QYEVKLQKGL SCGGAYIKLL SATEAGVTPD EFSDKTPYTI
     MFGPDKCGQT NKVHFIFRHK NPKTGEFEEK HVKYPAYPKL AKTSTLYTLV VQPDQSFEIF
     INNESKKKGS LLEDFEPPVN PPTEIDDPED EKPADWVDQA RIFDPKATKP EDWDEDAPLE
     IPDQDAVKPD GWLEDEPLTI PDPDAQKPEE WDDDEDGEWF APSIPNPKCE AAAGCGEWVR
     PVIRNPAYKG KWTAPLIDNP EYKGVWEPRT IANPNYFEDK SPADFNPIGG VGFELWTMDE
     DILFDNIYIG HDPSQAKAFA AETFDQKIKI EQRQEDKETA AKAAEDGAGF VGQVRSHVNT
     FIGRARQDPI GAIKEMPQVA GGLGAAFAGL LGLVGLVGGV LGGGSKVKVT TKDGKKVDAP
     TAAKGKAKEV TEKVKATGVQ AKDAVTKRTN AAAAKVDDAA NDE