ID   CNE1_CRYNH              Reviewed;         551 AA.
AC   J9VLH0;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Calnexin {ECO:0000303|PubMed:34566931};
DE   Flags: Precursor;
GN   Name=CNE1 {ECO:0000303|PubMed:34566931}; ORFNames=CNAG_02500;
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA   Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA   Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA   Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA   Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA   Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA   Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
RN   [2]
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   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=34566931; DOI=10.3389/fmicb.2021.727039;
RA   Horianopoulos L.C., Lee C.W.J., Hu G., Caza M., Kronstad J.W.;
RT   "Dnj1 promotes virulence in Cryptococcus neoformans by maintaining robust
RT   endoplasmic reticulum homeostasis under temperature stress.";
RL   Front. Microbiol. 12:727039-727039(2021).
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). With co-chaperone DNJ1, coordinately maintains ER
CC       homeostasis and contributes to maintenance of cell wall architecture
CC       (PubMed:34566931). {ECO:0000269|PubMed:34566931,
CC       ECO:0000305|PubMed:16467570}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:34566931}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Leads to a slight growth defect at 30 degrees
CC       Celsius and marked defect at 37 degrees Celsius (PubMed:34566931).
CC       Leads to abnormal cell morphology of enlarged cells with collapsed cell
CC       walls and increased chitin within the cell walls, as well as strong
CC       growth defects at both 30 and 37 degrees Celsius when both DNJ1 and
CC       CNE1 are deleted (PubMed:34566931). {ECO:0000269|PubMed:34566931}.
CC   -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR   EMBL; CP003825; AFR95332.1; -; Genomic_DNA.
DR   RefSeq; XP_012050186.1; XM_012194796.1.
DR   EnsemblFungi; AFR95332; AFR95332; CNAG_02500.
DR   GeneID; 23886116; -.
DR   VEuPathDB; FungiDB:CNAG_02500; -.
DR   HOGENOM; CLU_018224_1_2_1; -.
DR   Proteomes; UP000010091; Chromosome 6.
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; 1.
DR   SUPFAM; SSF63887; SSF63887; 1.
DR   PROSITE; PS00803; CALRETICULIN_1; 1.
DR   PROSITE; PS00804; CALRETICULIN_2; 1.
DR   PROSITE; PS00805; CALRETICULIN_REPEAT; 1.
PE   3: Inferred from homology;
KW   Chaperone; Endoplasmic reticulum; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..551
FT                   /note="Calnexin"
FT                   /id="PRO_5005137169"
FT   TOPO_DOM        24..477
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        478..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        499..551
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          293..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..315
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  61005 MW;  1BC0D3A249528823 CRC64;
     MRPQNVAGVA GTGALIMAAG ALADQTVFHP TSLTAPFIEQ FIESIPDSRW TVSRATKQTP
     VGDEIFSYVG QWEVEEPEVY PGIPGDKGLV LKTKAAHHAI STLFTEPIDP KGKSLVVQYE
     VKLQKGLECG GAYIKLLTDQ QDEGLRAGED YTDKTPFTIM FGPDKCGSTN KVHFIFRHKN
     PLTGEWEEKH LKNPPSPKIT KTTALYTLIT NPDQTFEILI NDESVRKGSL LEDFDPAVNP
     PKEIDDPEDF KPETWVDEAE IEDITATKPD DWDEDAPMMI TDTAAVKPVD WLEEEPETIP
     DPEAEKPEEW DDEEDGDWIP PMVPNPKCED VSGCGPWTAP KIRNPDYKGK WTVPRIPNPD
     YKGPWAPRKI ANPAFFEDLH PSDFTKIGGV GIELWTMTED ILFDNLYIGH DAAQAKKFAE
     ETYHVKKPIE KEAEGSNEDE LEEPSSLVEK VQLKVYEFLH LATFDIAQAI KQMPEVAAGL
     AAAVFTLLGM LLALFGFIGS APTKVKQTTV KTKAVAPVAP AGEEEKKALD QAGVEIPAEG
     SKKRVTRSTK E