CALX_SOYBN
ID CALX_SOYBN Reviewed; 546 AA.
AC Q39817;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Calnexin homolog;
DE Flags: Precursor;
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Roanoke; TISSUE=Seed;
RA Goode J.H., Settlage S.B., Wilson R.F., Dewey R.E.;
RT "Isolation of a calnexin homolog from developing soybean seeds.";
RL (er) Plant Gene Register PGR95-005(1995).
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; U20502; AAA80588.1; -; mRNA.
DR PIR; T06415; T06415.
DR RefSeq; NP_001235116.1; NM_001248187.2.
DR AlphaFoldDB; Q39817; -.
DR SMR; Q39817; -.
DR STRING; 3847.GLYMA06G17060.1; -.
DR PRIDE; Q39817; -.
DR EnsemblPlants; KRH54057; KRH54057; GLYMA_06G162600.
DR GeneID; 547851; -.
DR Gramene; KRH54057; KRH54057; GLYMA_06G162600.
DR KEGG; gmx:547851; -.
DR eggNOG; KOG0675; Eukaryota.
DR InParanoid; Q39817; -.
DR OrthoDB; 775337at2759; -.
DR Proteomes; UP000008827; Chromosome 6.
DR Genevisible; Q39817; GM.
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: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; 1.
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; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..546
FT /note="Calnexin homolog"
FT /id="PRO_0000004206"
FT TOPO_DOM 26..475
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 234..245
FT /note="1-1"
FT REPEAT 251..262
FT /note="1-2"
FT REPEAT 270..281
FT /note="1-3"
FT REPEAT 289..300
FT /note="1-4"
FT REPEAT 304..314
FT /note="2-1"
FT REPEAT 323..333
FT /note="2-2"
FT REPEAT 337..347
FT /note="2-3"
FT REPEAT 351..361
FT /note="2-4"
FT REGION 217..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..365
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250"
FT REGION 234..300
FT /note="4 X approximate repeats"
FT REGION 304..361
FT /note="4 X approximate repeats"
FT REGION 501..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..307
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 123
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 143
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 150
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 380
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..152
FT /evidence="ECO:0000250"
FT DISULFID 316..322
FT /evidence="ECO:0000250"
SQ SEQUENCE 546 AA; 62081 MW; E5E8BF5D1E68C85F CRC64;
MGERKGIPMA LGLLAMILFF IASSSSHLVR ASDDADDAIF YESFDEDFDG RWIVSDKEDY
NGVWKHAKSD GHDDYGLLVS EQARKYAIVK ELAESVSLKD GTVVLQFETR LQNGLECGGA
YIKYLRPQES GWKPKEFDNE SPYSIMFGPD KCGATNKVHF IFKHKNPKSG EYVEHHLKYP
PSVPSDKLTH VYTAILKPDN ELQILIDGEE KKKANFLSSE DFEPPLIPSK TIPDPDDKKP
EDWDERAKIP DPSAVKPDDW DEDAPMEILD EEAEKPEGWL DDEPEEIDDP EATKPEDWDD
EEDGEWEAPK IENPKCEAAP GCGEWKRPTK RNPAYKGKWS APYIDNPSYK GIWKPREIPN
PEYFELAKPD FEPIAAIGIE IWTMQDGILF DNVLIANDDK VAESYRETTW KPKFTVEKDK
LKAEEEAATG SDGISGFQKK VFDLLYKIAD IPFLSEHKSK IFDLIEKAEK QPNLTIGILV
AVVVVFVSIF FRLIFGGKKP AKVEKKPERT EASNNQGSGE NEENKEKEKQ KEEASNAARR
RPRRET
