CALX_HELTU
ID CALX_HELTU Reviewed; 540 AA.
AC Q39994;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Calnexin homolog;
DE Flags: Precursor;
OS Helianthus tuberosus (Jerusalem artichoke) (Helianthus tomentosus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4233;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Blanc commun; TISSUE=Tuber;
RA Hasenfratz M., Jeltsch J., Lesot A., Michalak M., Durst F.;
RT "Cloning and characterization of a cDNA encoding an analog of the calnexin
RT chaperone from Jerusalem artichoke.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
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; Z35108; CAA84491.1; -; mRNA.
DR PIR; T10892; T10892.
DR AlphaFoldDB; Q39994; -.
DR SMR; Q39994; -.
DR PRIDE; Q39994; -.
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: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; 3.
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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..540
FT /note="Calnexin homolog"
FT /id="PRO_0000004204"
FT TOPO_DOM 30..469
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 229..240
FT /note="1-1"
FT REPEAT 246..257
FT /note="1-2"
FT REPEAT 265..276
FT /note="1-3"
FT REPEAT 284..295
FT /note="1-4"
FT REPEAT 299..309
FT /note="2-1"
FT REPEAT 318..328
FT /note="2-2"
FT REPEAT 332..342
FT /note="2-3"
FT REPEAT 346..356
FT /note="2-4"
FT REGION 221..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..360
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250"
FT REGION 229..295
FT /note="4 X approximate repeats"
FT REGION 299..356
FT /note="4 X approximate repeats"
FT REGION 499..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..301
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 118
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 145
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 375
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..147
FT /evidence="ECO:0000250"
FT DISULFID 311..317
FT /evidence="ECO:0000250"
SQ SEQUENCE 540 AA; 61274 MW; F9A5C4E2DE4A7124 CRC64;
MELSRRKMCC YIQFCCFVLI GCFISQICAS SDAIFYESFD ESFEGSWIVS EKEDYPGEWK
HSKSEGHDDY GLLVSDKARK YAIVKELEKP VELKDGTIVL QYEVRLQNGL ECGGAYLKYL
RPQDAGWTAK GFDNESPYSI MFGPDKCGAT NKVHFILKHK NPKSGDYVEH HLKFPPSVPS
DKLTHVYTAV IKPDNELVIL IDGEEKKKAN FLSSEDFEPA LIPTKTIPDP DDKKPEDWDE
RAKIPDPEAT KPDDWDEDAP MEILDEEAEK PEGWLDDEPE EIDDPEAVKP EDWDDEEDGE
WEAPQIENPK CESAPGCGEW RRPLKRNPAY KGKWHAPLID NPAYKGIWKP REIPNPDYFE
LEKPNFEPIA AIGIEDLDQQ DGILFDNILI ASDEKTAAKS GILLGSRSLR WKKRNRRLKK
NQPLLDGLKG IQKAVFDVLY KIADLPFLGD HKVKVLELIE KAETQPNITI GVIVSIIVVI
FSILLKLLFG GKKAAPKVNV VPKKKEEPEA SNTAEVREGE EEKTEGEVAA APRRRPRRDT
