CALX_PONAB
ID CALX_PONAB Reviewed; 592 AA.
AC Q5R440; Q5R6B9; Q5R6P7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Calnexin;
DE Flags: Precursor;
GN Name=CANX;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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. Associated with partial T-cell antigen receptor
CC complexes that escape the ER of immature thymocytes, it may function as
CC a signaling complex regulating thymocyte maturation. Additionally it
CC may play a role in receptor-mediated endocytosis at the synapse (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAPK3/ERK1. Interacts with KCNH2. Associates
CC with ribosomes. Interacts with SGIP1; involved in negative regulation
CC of endocytosis. The palmitoylated form interacts with the ribosome-
CC translocon complex component SSR1, promoting efficient folding of
CC glycoproteins. Interacts with SERPINA2P/SERPINA2 and with the S and Z
CC variants of SERPINA1. Interacts with PPIB. Interacts with ZNRF4.
CC Interacts with SMIM22 (By similarity). Interacts with TMX2 (By
CC similarity). Interacts with TMEM35A/NACHO and CHRNA7 (By similarity).
CC {ECO:0000250|UniProtKB:P24643, ECO:0000250|UniProtKB:P27824,
CC ECO:0000250|UniProtKB:P35564, ECO:0000250|UniProtKB:P35565}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P27824}; Single-pass type I membrane protein
CC {ECO:0000255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P27824}.
CC Melanosome {ECO:0000250|UniProtKB:P27824}. Note=The palmitoylated form
CC preferentially localizes to the perinuclear rough ER.
CC {ECO:0000250|UniProtKB:P27824}.
CC -!- PTM: Phosphorylated at Ser-564 by MAPK3/ERK1. phosphorylation by
CC MAPK3/ERK1 increases its association with ribosomes (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Palmitoylation by DHHC6 leads to the preferential localization to
CC the perinuclear rough ER. It mediates the association of calnexin with
CC the ribosome-translocon complex (RTC) which is required for efficient
CC folding of glycosylated proteins (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation. Probably
CC ubiquitinated by ZNRF4. {ECO:0000250|UniProtKB:P27824}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR EMBL; CR860439; CAH92563.1; -; mRNA.
DR EMBL; CR860572; CAH92697.1; -; mRNA.
DR EMBL; CR861420; CAH93476.1; -; mRNA.
DR RefSeq; NP_001127039.1; NM_001133567.1.
DR AlphaFoldDB; Q5R440; -.
DR SMR; Q5R440; -.
DR Ensembl; ENSPPYT00000053633; ENSPPYP00000041212; ENSPPYG00000016126.
DR GeneID; 100174065; -.
DR KEGG; pon:100174065; -.
DR CTD; 821; -.
DR GeneTree; ENSGT00950000182915; -.
DR InParanoid; Q5R440; -.
DR OrthoDB; 775337at2759; -.
DR Proteomes; UP000001595; Chromosome 5.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
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:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB.
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; 2.
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 Acetylation; Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum;
KW Lectin; Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..592
FT /note="Calnexin"
FT /id="PRO_0000004200"
FT TOPO_DOM 21..481
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 278..290
FT /note="1-1"
FT REPEAT 295..307
FT /note="1-2"
FT REPEAT 314..326
FT /note="1-3"
FT REPEAT 333..345
FT /note="1-4"
FT REPEAT 348..358
FT /note="2-1"
FT REPEAT 367..377
FT /note="2-2"
FT REPEAT 381..391
FT /note="2-3"
FT REPEAT 395..405
FT /note="2-4"
FT REGION 260..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..409
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250"
FT REGION 278..345
FT /note="4 X approximate repeats"
FT REGION 326..359
FT /note="Interaction with PPIB"
FT /evidence="ECO:0000250"
FT REGION 348..405
FT /note="4 X approximate repeats"
FT REGION 503..592
FT /note="Sufficient to mediate interaction with SGIP1"
FT /evidence="ECO:0000250"
FT REGION 511..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..345
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..546
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 166
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 185
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 192
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 425
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 436
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27824"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27824"
FT MOD_RES 562
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27824"
FT MOD_RES 564
FT /note="Phosphoserine; by MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P27824"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27824"
FT LIPID 502
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 503
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 160..194
FT /evidence="ECO:0000250"
FT DISULFID 360..366
FT /evidence="ECO:0000250"
FT CONFLICT 83
FT /note="W -> R (in Ref. 1; CAH93476)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="T -> A (in Ref. 1; CAH92563)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="K -> R (in Ref. 1; CAH92697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 67572 MW; 31875C853C202811 CRC64;
MEGKWLLCML LVLGTAIVEA HDGHDDDVID IEDDLDDVIE EVEDSKPDTT APPSSPKVTY
KAPVPTGEVY FADSFDRGTL SGWILSKAKK DDTDDEIAKY DGKWEVDEMK ESKLPGDKGL
VLMSRAKHHA ISAKLNKPFL FDTKPLIVQY EVNFQNGIEC GGAYVKLLSK TPELNLDQFH
DKTPYTIMFG PDKCGEDYKL HFIFRHKNPK TGIYEEKHAK RPDADLKTYF TDKKTHLYTL
ILNPDNSFEI LVDQSVVNSG NLLNDMTPPV NPSREIEDPE DRKPEDWDER PKIPDPEAVK
PDDWDEDAPA KIPDEEATKP EGWLDDEPEY VPDPDAEKPE DWDEDMDGEW EAPQIANPKC
ESAPGCGVWQ RPMIDNPNYK GKWKPPMIDN PSYQGIWKPR KIPNPDFFED LEPFRMTPFS
AIGLELWSMT SDIFFDNFII CADRRIVDDW ANDGWGLKKA ADGAAEPGVV GQMIEAAEER
PWLWVVYILT VALPVFLVIL FCCSGKKQTS AMEYKKTDAP QPDVKEEEEE KEEEKDKGDE
EEEGEEKLEE KQKSDAEEDG GTVSQEEEDR KPKAEEDEIL NRSPRNRKPR RE
