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Database: UniProt
Entry: Q6Q487
LinkDB: Q6Q487
Original site: Q6Q487 
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   14-MAY-2014, entry version 81.
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.
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; NHKNPKT; -.
DR   OrthoDB; EOG73V6V4; -.
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: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   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; 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; 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
//
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