CALX1_ARATH
ID CALX1_ARATH Reviewed; 530 AA.
AC P29402;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Calnexin homolog 1;
DE Flags: Precursor;
GN Name=CNX1; OrderedLocusNames=At5g61790; ORFNames=MAC9.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8454626; DOI=10.1016/s0021-9258(18)53287-7;
RA Huang L., Franklin A.E., Hoffman N.E.;
RT "Primary structure and characterization of an Arabidopsis thaliana
RT calnexin-like protein.";
RL J. Biol. Chem. 268:6560-6566(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR EMBL; Z18242; CAA79144.1; -; mRNA.
DR EMBL; AB010069; BAB10079.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97518.1; -; Genomic_DNA.
DR EMBL; AY059880; AAL24362.1; -; mRNA.
DR EMBL; AY114669; AAM47988.1; -; mRNA.
DR EMBL; AY086864; AAM63911.1; -; mRNA.
DR PIR; JN0597; JN0597.
DR RefSeq; NP_200987.1; NM_125573.4.
DR AlphaFoldDB; P29402; -.
DR SMR; P29402; -.
DR BioGRID; 21545; 26.
DR STRING; 3702.AT5G61790.1; -.
DR iPTMnet; P29402; -.
DR SwissPalm; P29402; -.
DR PaxDb; P29402; -.
DR PRIDE; P29402; -.
DR ProteomicsDB; 239178; -.
DR EnsemblPlants; AT5G61790.1; AT5G61790.1; AT5G61790.
DR GeneID; 836301; -.
DR Gramene; AT5G61790.1; AT5G61790.1; AT5G61790.
DR KEGG; ath:AT5G61790; -.
DR Araport; AT5G61790; -.
DR TAIR; locus:2159223; AT5G61790.
DR eggNOG; KOG0675; Eukaryota.
DR HOGENOM; CLU_018224_1_0_1; -.
DR OMA; SGCGKWE; -.
DR OrthoDB; 775337at2759; -.
DR PhylomeDB; P29402; -.
DR PRO; PR:P29402; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P29402; baseline and differential.
DR Genevisible; P29402; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
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:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
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; 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; 2.
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; 3.
PE 1: Evidence at protein level;
KW Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Lectin; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..530
FT /note="Calnexin homolog 1"
FT /id="PRO_0000004202"
FT TOPO_DOM 21..466
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 225..236
FT /note="1-1"
FT REPEAT 242..253
FT /note="1-2"
FT REPEAT 261..272
FT /note="1-3"
FT REPEAT 280..291
FT /note="1-4"
FT REPEAT 295..305
FT /note="2-1"
FT REPEAT 314..324
FT /note="2-2"
FT REPEAT 328..338
FT /note="2-3"
FT REPEAT 342..352
FT /note="2-4"
FT REGION 216..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..356
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250"
FT REGION 225..291
FT /note="4 X approximate repeats"
FT REGION 295..352
FT /note="4 X approximate repeats"
FT REGION 490..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..297
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 114
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 134
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 141
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 371
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..143
FT /evidence="ECO:0000250"
FT DISULFID 307..313
FT /evidence="ECO:0000250"
SQ SEQUENCE 530 AA; 60486 MW; 583F81DCF4EF67A9 CRC64;
MRQRQLFSVF LLLLAFVSFQ KLCYCDDQTV LYESFDEPFD GRWIVSKNSD YEGVWKHAKS
EGHEDYGLLV SEKARKYGIV KELDEPLNLK EGTVVLQYEV RFQEGLECGG AYLKYLRPQE
AGWTPQGFDS ESPYSIMFGP DKCGGTNKVH FILKHKNPKS GEYVEHHLKF PPSVPYDKLS
HVYTAILKPD NEVRILVDGE EKKKANLLSG EDFEPALIPA KTIPDPEDKK PEDWDERAKI
PDPNAVKPED WDEDAPMEIE DEEAEKPEGW LDDEPEEVDD PEATKPEDWD DEEDGMWEAP
KIDNPKCEAA PGCGEWKRPM KRNPAYKGKW SSPLIDNPAY KGIWKPRDIP NPDYFELDRP
DYEPIAAIGI EIWTMQDGIL FDNILIAKDE KVAETYRQTT WKPKFDVEKE KQKAEEEAAG
SADGLKSYQK VVFDLLNKVA DLSFLSAYKS KITELIEKAE QQPNLTIGVL VAIVVVFFSL
FLKLIFGGKK AAAPVEKKKP EVAESSKSGD EAEKKEETAA PRKRQPRRDN
