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-APR-2013, entry version 76.
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; Trichocomaceae;
OC mitosporic Trichocomaceae; Aspergillus.
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.,
RA Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
RA Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
RA Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
RA Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
RA Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
RA Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
RA Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA 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.,
RA Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
RA Machida M., Hall N., 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 glycoproteins in the
CC endoplasmic reticulum. It may act in assisting protein assembly
CC and/or in the retention within the ER of unassembled protein
CC subunits. It seems to play a major role in the quality control
CC apparatus of the ER by the retention of incorrectly folded
CC proteins (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein (By similarity).
CC -!- SIMILARITY: Belongs to the calreticulin family.
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DR EMBL; AY560606; AAS68033.1; -; mRNA.
DR EMBL; AAHF01000005; EAL89509.1; -; Genomic_DNA.
DR RefSeq; XP_751547.1; XM_746454.1.
DR ProteinModelPortal; Q6Q487; -.
DR SMR; Q6Q487; 47-434.
DR PRIDE; Q6Q487; -.
DR EnsemblFungi; CADAFUAT00008238; CADAFUAP00008238; CADAFUAG00008238.
DR GeneID; 3509033; -.
DR KEGG; afm:AFUA_4G12850; -.
DR eggNOG; NOG305105; -.
DR HOGENOM; HOG000192435; -.
DR KO; K08054; -.
DR OMA; FEIWTMQ; -.
DR OrthoDB; EOG4J14J7; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 2.10.250.10; -; 2.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR001580; Calret/calnex.
DR InterPro; IPR018124; Calret/calnex_CS.
DR InterPro; IPR009033; Calreticulin/calnexin_P_dom.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR PANTHER; PTHR11073; PTHR11073; 1.
DR Pfam; PF00262; Calreticulin; 1.
DR PRINTS; PR00626; CALRETICULIN.
DR SUPFAM; SSF63887; Calret_calnex_P; 1.
DR SUPFAM; SSF49899; ConA_like_lec_gl; 2.
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; Complete proteome; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Lectin; Membrane; Metal-binding; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 23 Potential.
FT CHAIN 24 563 Calnexin homolog.
FT /FTId=PRO_0000043348.
FT TOPO_DOM 24 493 Lumenal (Potential).
FT TRANSMEM 494 514 Helical; (Potential).
FT TOPO_DOM 515 563 Cytoplasmic (Potential).
FT REGION 253 386 P domain (Extended arm) (By similarity).
FT METAL 98 98 Calcium; via carbonyl oxygen (By
FT similarity).
FT METAL 413 413 Calcium (By similarity).
FT BINDING 145 145 Carbohydrate (By similarity).
FT BINDING 147 147 Carbohydrate (By similarity).
FT BINDING 166 166 Carbohydrate (By similarity).
FT BINDING 197 197 Carbohydrate (By similarity).
FT CARBOHYD 236 236 N-linked (GlcNAc...) (Potential).
FT DISULFID 141 175 By similarity.
FT DISULFID 337 343 By similarity.
FT CONFLICT 332 332 V -> G (in Ref. 1; AAS68033).
FT CONFLICT 446 446 S -> P (in Ref. 1; AAS68033).
FT CONFLICT 527 527 G -> D (in Ref. 1; AAS68033).
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
//
