CALX2_ARATH
ID CALX2_ARATH Reviewed; 532 AA.
AC Q38798; Q9LY26;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Calnexin homolog 2;
DE Flags: Precursor;
GN OrderedLocusNames=At5g07340; ORFNames=T2I1_50;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=7846171; DOI=10.1104/pp.106.4.1691;
RA Boyce J.M., Coates D., Fricker M.D., Evans D.E.;
RT "Genomic sequence of a calnexin homolog from Arabidopsis thaliana.";
RL Plant Physiol. 106:1691-1691(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q38798-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17742.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U08315; AAA17742.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL163912; CAB87923.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91138.1; -; Genomic_DNA.
DR EMBL; BT001999; AAN72010.1; -; mRNA.
DR EMBL; BT010385; AAQ56828.1; -; mRNA.
DR PIR; T49873; T49873.
DR RefSeq; NP_196351.1; NM_120816.3. [Q38798-1]
DR AlphaFoldDB; Q38798; -.
DR SMR; Q38798; -.
DR BioGRID; 15904; 48.
DR IntAct; Q38798; 19.
DR STRING; 3702.AT5G07340.2; -.
DR SwissPalm; Q38798; -.
DR PaxDb; Q38798; -.
DR PRIDE; Q38798; -.
DR ProteomicsDB; 239190; -. [Q38798-1]
DR EnsemblPlants; AT5G07340.1; AT5G07340.1; AT5G07340. [Q38798-1]
DR GeneID; 830625; -.
DR Gramene; AT5G07340.1; AT5G07340.1; AT5G07340. [Q38798-1]
DR KEGG; ath:AT5G07340; -.
DR Araport; AT5G07340; -.
DR eggNOG; KOG0675; Eukaryota.
DR HOGENOM; CLU_018224_1_0_1; -.
DR InParanoid; Q38798; -.
DR OMA; MRRERIF; -.
DR PhylomeDB; Q38798; -.
DR PRO; PR:Q38798; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38798; baseline and differential.
DR Genevisible; Q38798; AT.
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; 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 Alternative splicing; Calcium; Chaperone; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Lectin; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..532
FT /note="Calnexin homolog 2"
FT /id="PRO_0000004203"
FT TOPO_DOM 26..468
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 227..238
FT /note="1-1"
FT REPEAT 244..255
FT /note="1-2"
FT REPEAT 263..274
FT /note="1-3"
FT REPEAT 282..293
FT /note="1-4"
FT REPEAT 297..307
FT /note="2-1"
FT REPEAT 316..326
FT /note="2-2"
FT REPEAT 330..340
FT /note="2-3"
FT REPEAT 344..354
FT /note="2-4"
FT REGION 208..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..358
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250"
FT REGION 227..293
FT /note="4 X approximate repeats"
FT REGION 297..354
FT /note="4 X approximate repeats"
FT REGION 493..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..299
FT /note="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 114
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 116
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 136
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 373
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..145
FT /evidence="ECO:0000250"
FT DISULFID 309..315
FT /evidence="ECO:0000250"
FT CONFLICT 30
FT /note="I -> V (in Ref. 1; AAA17742)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="M -> K (in Ref. 1; AAA17742)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 60490 MW; 2283669E7A5C6D1C CRC64;
MRERIITFVS LLLVALLSFP SVSYCDDQTI LYESFDEPFD GRWVVSEKAE YQGVWKHEKS
EGHDDYGLLV SEKAKKYGIV KELDVDEPLN LNEGTVVLQY EARFQEGLEC GGAYLKYLRP
QEAGWVPQGF DNDSPYSIMF GPDKCGATNK VHFILKHKNP KSGEFVEHHL KFPPSVPFDM
LSHVYTAVLK SDNEVRILVD GEEKKKGNLL SAEDFEPPLI PSKTIPDPED KKPEDWDERA
KIPDPNAVKP DDWDEDAPME IEDEEAEKPE GWLDDEPVEV EDPEASKPED WDDEEDGEWE
APKVSNTKCE AAPGCGEWKR PMKRNPAYKG KWSSPLIDNP AYKGIWKPRD IPNPDYFELE
RPNLEPIAAI GIEIWTMQDG ILFDNILISK DEKVAETYRQ STWKPKFDVE KEKQKAEDEA
AGEADGLKSY QKKVFDLLYK VADISFLSAY KSKIMELIEK AETQPNLTIG VLISIVIVFL
SLFFKLIFGG AKAKVEKKKP ETAAETSTSE AKTEEKAEAV AAPRKRQTRR ES
