CALX_PEA
ID CALX_PEA Reviewed; 551 AA.
AC O82709;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Calnexin homolog;
DE Flags: Precursor;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=10595399; DOI=10.1089/104454999314854;
RA Ehtesham N.Z., Phan T.N., Gaikwad A., Sopory S.K., Tuteja N.;
RT "Calnexin from Pisum sativum: cloning of the cDNA and characterization of
RT the encoded protein.";
RL DNA Cell Biol. 18:853-862(1999).
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 -!- TISSUE SPECIFICITY: In vegetative and flowering tissues.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR EMBL; Y17329; CAA76741.1; -; mRNA.
DR AlphaFoldDB; O82709; -.
DR SMR; O82709; -.
DR PRIDE; O82709; -.
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; TAS:AgBase.
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; 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; 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; 2.
PE 2: Evidence at transcript level;
KW Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Lectin; Membrane; Metal-binding; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..551
FT /note="Calnexin homolog"
FT /id="PRO_0000004205"
FT TOPO_DOM 27..480
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 235..246
FT /note="1-1"
FT REPEAT 252..263
FT /note="1-2"
FT REPEAT 271..282
FT /note="1-3"
FT REPEAT 289..299
FT /note="1-4"
FT REPEAT 303..313
FT /note="2-1"
FT REPEAT 322..332
FT /note="2-2"
FT REPEAT 336..346
FT /note="2-3"
FT REPEAT 350..360
FT /note="2-4"
FT REGION 226..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..364
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250"
FT REGION 235..299
FT /note="4 X approximate repeats"
FT REGION 303..360
FT /note="4 X approximate repeats"
FT REGION 510..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 124
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 144
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 151
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 379
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..153
FT /evidence="ECO:0000250"
FT DISULFID 315..321
FT /evidence="ECO:0000250"
SQ SEQUENCE 551 AA; 62532 MW; 25A5F5F13B989365 CRC64;
MVDRKEIPLA MGLLAVLLFF VASSSSFHLV RASDEVDDAI FYESFDEDFD NRWIVSGKEE
YNGVWKHSKS EGHDDFGLLV SEPARKYAIV KELDAPVSLK DGTVVLQFET RLQNGLECGG
AYIKYLQTQE SGWKPKGFDN ESGYSIMFGP DRCGATNKVH FIFRHKNPKT GKHVEHHLKF
PPSVPSDKLS HVYTAVLKDD NEVSILIDGE EKKKANFLSS EDFEPALIPS KTIPDPDDKK
PEDWDERAKI PDPEAVKPED WDEDAPREII DEEAEKPEPW LDHEPEVDDP EAKPEDWDDE
EDGEWEAPKI ENPKCEAAPG CGEWKRPTKS NPAYKGKWSA PYIDNPNYKG IWKPQEIPNP
EYFELEKPDF EPIAAIGIEI WTMQDGILFD NVLIAKDDKI AESYRETTWK PKFNIEKEKQ
KHEEEAAAAA AARSESEGIA GIQKKAFDLL YKIADIAFLS GQKEKIIEII EKGEKQPNLT
IGIIVSVVIV FVSIFFRLIF GGKKPANVEA NVEKKKTNTE TTSKQDGGEK EDNKEKEETA
NPPRRRPKRD N
