CALX_SCHPO
ID CALX_SCHPO Reviewed; 560 AA.
AC P36581;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Calnexin homolog;
DE Flags: Precursor;
GN Name=cal1; Synonyms=cnx1; ORFNames=SPAC3C7.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7621821; DOI=10.1002/j.1460-2075.1995.tb07309.x;
RA Parlati F., Dignard D., Bergeron J.J.M., Thomas D.Y.;
RT "The calnexin homologue cnx1+ in Schizosaccharomyces pombe, is an essential
RT gene which can be complemented by its soluble ER domain.";
RL EMBO J. 14:3064-3072(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7876257; DOI=10.1074/jbc.270.9.4845;
RA Jannatipour M., Rokeach L.A.;
RT "The Schizosaccharomyces pombe homologue of the chaperone calnexin is
RT essential for viability.";
RL J. Biol. Chem. 270:4845-4853(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551; SER-553 AND THR-555, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR EMBL; M98799; AAA79757.1; -; Genomic_DNA.
DR EMBL; U13389; AAA68631.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16741.1; -; Genomic_DNA.
DR PIR; S56142; S56142.
DR RefSeq; NP_593612.1; NM_001019043.2.
DR AlphaFoldDB; P36581; -.
DR SMR; P36581; -.
DR BioGRID; 279476; 6.
DR STRING; 4896.SPAC3C7.11c.1; -.
DR iPTMnet; P36581; -.
DR MaxQB; P36581; -.
DR PaxDb; P36581; -.
DR PRIDE; P36581; -.
DR EnsemblFungi; SPAC3C7.11c.1; SPAC3C7.11c.1:pep; SPAC3C7.11c.
DR PomBase; SPAC3C7.11c; -.
DR VEuPathDB; FungiDB:SPAC3C7.11c; -.
DR eggNOG; KOG0675; Eukaryota.
DR HOGENOM; CLU_018224_1_2_1; -.
DR InParanoid; P36581; -.
DR OMA; SGCGKWE; -.
DR PhylomeDB; P36581; -.
DR Reactome; R-SPO-901042; Calnexin/calreticulin cycle.
DR PRO; PR:P36581; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IDA:PomBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:PomBase.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; ISO:PomBase.
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 1: Evidence at protein level;
KW Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Lectin; Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..560
FT /note="Calnexin homolog"
FT /id="PRO_0000004209"
FT TOPO_DOM 23..489
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 244..255
FT /note="1-1"
FT REPEAT 261..272
FT /note="1-2"
FT REPEAT 280..291
FT /note="1-3"
FT REPEAT 299..310
FT /note="1-4"
FT REPEAT 314..324
FT /note="2-1"
FT REPEAT 333..343
FT /note="2-2"
FT REPEAT 347..357
FT /note="2-3"
FT REPEAT 361..371
FT /note="2-4"
FT REGION 242..375
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250"
FT REGION 244..310
FT /note="4 X approximate repeats"
FT REGION 253..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..371
FT /note="4 X approximate repeats"
FT REGION 517..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 138
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 154
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 161
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 391
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT MOD_RES 551
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 555
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 132..163
FT /evidence="ECO:0000250"
FT DISULFID 326..332
FT /evidence="ECO:0000250"
SQ SEQUENCE 560 AA; 63466 MW; E3B20877333E9123 CRC64;
MKYGKVSFLA LLCSLYVRGS LADPESEQEP LVFNPTEVKA PLVEQFQGAW SERWIPSHAK
RFVNGIEEMS YVGEWTVEES SGPGALKGEA GLVMKDEAAH HAISYEFDEP INEPEKDLVV
QYEVNPEEGL NCGGAYLKLL AEPTHGEMSN SIDYRIMFGP DKCGVNDRVH FIFKHKNPLT
GEYSEKHLDS RPASLLKPGI TNLYTLIVKP DQTFEVRING DVVRQGSLFY DFIPPVLPPV
EIYDPEDIKP ADWVDEPEIP DPNAVKPDDW DEDAPRMIPD PDAVKPEDWL EDEPLYIPDP
EAQKPEDWDD EEDGDWIPSE IINPKCIEGA GCGEWKPPMI RNPNYRGPWS PPMIPNPEFI
GEWYPRKIPN PDYFDDDHPS HFGPLYGVGF ELWTMQPNIR FSNIYVGHSI EDAERLGNET
FLPKLKAERE LLSKQESMEK QSMHVDEESN QILEKFLDVY DIIKAKLPPN VAEKVDYYVE
TIIETPEIGI AIVAVLGSLT AVILTCYFYF FASSSPASLS TGTTEAEKEQ QEKFKQETET
EKIDVSYAPE TESPTAKNED
