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{{Short description|Mammalian protein found in humans}}
'''Calnexin (CNX)''' is a [http://www.uniprot.org/uniprot/P27824 67kDa] [[integral protein]] (that appears variously as a 90kDa, 80kDa or 75kDa band on western blotting depending on the source of the antibody) of the [[endoplasmic reticulum]] (ER). It consists of a large (50 kDa) [[N-terminal]] [[calcium]]-[[Binding (molecular)|binding]] [[Lumen (anatomy)|lumenal]] [[protein domain|domain]], a single [[transmembrane helix]] and a short (90 [[Residue (chemistry)|residues]]), [[acid]]ic [[cytoplasm]]ic tail.
{{Infobox_gene}}
'''Calnexin''' ('''CNX''') is a [https://www.uniprot.org/uniprot/P27824 67kDa] [[integral protein]] (that appears variously as a 90kDa, 80kDa, or 75kDa band on western blotting depending on the source of the antibody) of the [[endoplasmic reticulum]] (ER). It consists of a large (50 kDa) [[N-terminal]] [[calcium]]-[[Binding (molecular)|binding]] [[Lumen (anatomy)|lumenal]] [[protein domain|domain]], a single [[transmembrane helix]] and a short (90 [[Residue (chemistry)|residues]]), [[acid]]ic [[cytoplasm]]ic tail.<ref name= "Wada">{{cite journal | vauthors = Wada I, Rindress D, Cameron PH, Ou WJ, Doherty JJ 2nd, Louvard D, Bell AW, Dignard D, Thomas DY, Bergeron JJ | title = SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane | journal = J Biol Chem| volume = 226 | issue = 29 | pages = 19599–610 | year = 1991 | doi = 10.1016/S0021-9258(18)55036-5 | pmid = 1918067 | doi-access = free }}</ref> In humans, calnexin is encoded by the gene ''CANX''.<ref>{{cite journal|vauthors=Paskevicius T, Farraj RA, Michalak M, Agellon LB|title=Calnexin, More Than Just a Molecular Chaperone|journal=Cells|year=2023|volume=12|issue=3|page=403 |id=Article No. 403|veditors=Lim D|doi=10.3390/cells12030403|doi-access=free|pmid=36766745|pmc=9913998}}</ref>
 
== Function ==
Calnexin is a [[Chaperone (protein)|chaperone]], characterized by assisting [[protein folding]] and quality control, ensuring that only properly folded and assembled proteins proceed further along the [[secretory pathway]].
 
Calnexin is a [[Chaperone (protein)|chaperone]], characterized by assisting [[protein folding]] and quality control, ensuring that only properly folded and assembled proteins proceed further along the [[secretory pathway]]. It specifically acts to retain unfolded or unassembled N-linked [[glycoproteins]] in the ER.<ref name= "Ou">{{cite journal | vauthors = Ou WJ, Cameron PH, Thomas DY, Bergeron JJ | title = Association of folding intermediates of glycoproteins | journal = Nature | volume = 364 | issue = 644 | pages = 771–6 | year = 1993 | pmid = 8102790 | doi = 10.1038/364771a0 | s2cid = 4340769 }}</ref>
Calnexin acts to retain unfolded or unassembled N-linked [[glycoproteins]] in the ER.
 
Calnexin binds only those ''N''-[[glycoprotein]]s that have GlcNAc2Man9Glc1 [[oligosaccharide]]s.<ref name= "Hammond">{{cite journal | vauthors = Hammond C, Braakman I, Helenius A | title = Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control | journal = Proc Natl Acad Sci USA | volume = 91 | issue = 3 | pages = 913–7 | year = 1984 | pmid = 8302866 | pmc = 521423 | doi = 10.1073/pnas.91.3.913 | doi-access = free }}</ref> These monoglucosylated oligosaccharides result from the trimming of two glucose residues by the sequential action of two [[glucosidase]]s, I and II. Glucosidase II can also remove the third and last glucose residue. If the glycoprotein is not properly folded, an enzyme called [[UGGT]] (for UDP-glucose:glycoprotein glucosyltransferase) will add the glucose residue back onto the oligosaccharide thus regenerating the glycoprotein's ability to bind to calnexin.<ref name= "Gañán">{{cite journal | vauthors = Gañán S, Cazzulo JJ, Parodi AJ | title = A major proportion of N-glycoproteins are transiently glucosylated in the endoplasmic reticulum | journal = Biochemistry | volume = 30 | issue = 12 | pages = 3098–104 | year = 1991 | pmid = 1826090 | doi=10.1021/bi00226a017}}</ref> The improperly-folded glycoprotein chain thus loiters in the ER and the expression of EDEM/Htm1p <ref name= "Jacob">{{cite journal | vauthors = Jacob CA, Bodmer D, Spirig U, Battig P, Marcil A, Dignard D, Bergeron JJ, Thomas DY, Aebi M | title = Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast | journal = EMBO Rep | volume = 2| issue = 5 | pages = 423–30| year = 2001 | pmid = 11375935 | pmc = 1083883 | doi = 10.1093/embo-reports/kve089 }}</ref><ref name= "Hosokawa">{{cite journal | vauthors = Hosokawa N, Wada I, Hasegawa K, Yorihuzi T, Tremblay LO, Herscovics A, Nagata K | title = A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation | journal = EMBO Rep | volume = 2| issue = 5 | pages = 415–2| year = 2001 | pmid = 11375934 | pmc = 1083879 | doi=10.1093/embo-reports/kve084}}</ref><ref name= "Lee">{{cite journal | vauthors = Lee AH, Iwakoshi NN, Glimcher LH | title = XBP-1 regulates a subset of endoplasmic reticulum chaperone genes in the unfolded protein response | journal = Mol Cell Biol | volume = 23| issue = 21 | pages = 5448–59| year = 2003 | pmid = 14559994 | pmc = 207643 | doi = 10.1128/mcb.23.21.7448-7459.2003 }}</ref> which eventually sentences the underperforming glycoprotein to [[Chemical decomposition|degradation]] by removing one of the nine [[mannose]] residues. The mannose lectin Yos-9 (OS-9 in humans) marks and sorts misfolded glycoproteins for degradation. Yos-9 recognizes mannose residues exposed after α-mannosidase removal of an outer mannose of misfolded glycoproteins.<ref name= "Quan">{{cite journal | vauthors = Quan EM, Kamiya D, Denic V, Weibezahn J, Kato K, Weissman JS | title = Defining the glycan destruction signal for endoplasmic reticulum-associated degradation | journal = Mol Cell | volume = 32| issue = 6 | pages = 870–7| year = 2008 | pmid = 19111666 | pmc = 2873636 | doi=10.1016/j.molcel.2008.11.017}}</ref>
Calnexin binds only those N-[[glycoprotein]]s that have GlcNAc2Man9Glc1 [[oligosaccharide]]s. These monoglucosylated oligosaccharides result from the trimming of two glucose residues by the sequential action of two [[glucosidase]]s, I and II. Glucosidase II can also remove the third and last glucose residue.
 
Calnexin associates with the protein folding enzyme ERp57<ref name= "Zapun">{{cite journal | vauthors = Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJ, Thomas DY | title = Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57 | journal = J Biol Chem | volume = 273 | issue = 211 | pages = 6009–12| year = 1998 | pmid = 9497314 | doi = 10.1074/jbc.273.11.6009 | doi-access = free}}</ref> to catalyze glycoprotein specific disulfide bond formation and also functions as a chaperone for the folding of [[MHC class I]] α-chain in the membrane of the ER. As newly synthesized MHC class I α-chains enter the endoplasmic reticulum, calnexin binds on to them retaining them in a partly folded state.<ref name= "Bergeron">{{cite journal | vauthors = Bergeron JJ, Brenner MB, Thomas DY, Williams DB | title = Calnexin: a membrane-bound chaperone of the endoplasmic reticulum | journal = Trends Biochem Sci | volume = 19 | issue = 3 | pages = 124–8 | year = 1994 | pmid = 8203019 | doi=10.1016/0968-0004(94)90205-4}}</ref>
If the glycoprotein is not properly folded, an enzyme called [[UGGT]] (for UDP-glucose:glycoprotein glucosyltransferase) will add the glucose residue back onto the oligosaccharide thus regenerating the glycoprotein's ability to bind to calnexin.
 
After the β2-microglobulin binds to the MHC class I peptide-loading complex (PLC), calreticulin and ERp57 take over the job of chaperoning the MHC class I protein while the tapasin links the complex to the [[transporter associated with antigen processing]] (TAP) complex. This association prepares the MHC class I for binding an antigen for presentation on the cell surface.
The improperly-folded glycoprotein chain thus loiters in the ER, risking the encounter with MNS1 ([[alpha-mannosidase]]), which eventually sentences the underperforming glycoprotein to [[Chemical decomposition|degradation]] by removing its [[mannose]] residue.
 
A prolonged association of calnexin with mutant misfolded [[PMP22]] known to cause [[Charcot–Marie–Tooth disease|Charcot-Marie-Tooth Disease]]<ref name= "Dickson">{{cite journal | vauthors = Dickson KM, Bergeron JJ, Shames I, Colby J, Nguyen DT, Chevet E, Thomas DY, Snipes GJ | title = Association of calnexin with mutant peripheral myelin protein-22 ex vivo: a basis for "gain-of-function" ER diseases | journal = Proc Natl Acad Sci USA | volume = 99 | issue = 15 | pages = 9852–7 | year = 2002 | pmid = 12119418 | pmc = 125041 | doi = 10.1073/pnas.152621799 | bibcode = 2002PNAS...99.9852D | doi-access = free }}</ref> leads to the sequestration, degradation and inability of PMP22 to traffic to the [[Schwann cell]] surface for [[myelination]]. After repeated rounds of calnexin binding, mutant PMP22 is modified by [[ubiquitin]] for degradation by the [[proteasome]] as well as a Golgi to ER retrieval pathway to return any misfolded PMP22 that escaped from the ER to the Golgi apparatus.<ref name= "Hara">{{cite journal | vauthors = Hara T, Hashimoto Y, Akuzawa T, Hirai R, Kobayashi H, Sato K | title = Rer1 and calnexin regulate endoplasmic reticulum retention of a peripheral myelin protein 22 mutant that causes type 1A Charcot-Marie-Tooth disease | journal = Sci Rep | volume = 4 | pages = 1–11 | year = 2014 | pmid = 25385046 | pmc = 4227013 | doi=10.1038/srep06992| bibcode = 2014NatSR...4E6992H }}</ref>
If the protein is correctly [[translation|translated]], the chance of it being correctly folded before it encounters MNS1 is high.
 
The x-ray crystal structure of calnexin revealed a globular lectin domain and a long hydrophobic arm extending out.<ref name= "Schrag">{{cite journal | vauthors = Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, Thomas DY, Cygler M | title = The structure of calnexin, an ER chaperone involved in quality control of protein folding | journal = Mol Cell | volume = 8 | issue = 3 | pages = 633–44 | year = 2001 | pmid = 11583625 | doi=10.1016/s1097-2765(01)00318-5| doi-access = free }}</ref>
Calnexin also functions as a chaperone for the folding of [[MHC class I]] alpha chain in the membrane of the ER. After folding is completed Calnexin is replaced by [[Calreticulin]], which assists in further assembly of MHC class I.
 
== Cofactors ==▼
==Uses in molecular biology==
Antibodies against calnexin can be used as markers for the ER in immmunofluorescence experiments. <ref>http://www.genetex.com/Calnexin-antibody-C3-C-term-GTX109669.html</ref>
 
[[Adenosine triphosphate|ATP]] and [[Ca++|calcium ions]] are cofactors involved in substrate binding for calnexin.<ref name= "Thomas">{{cite journal | vauthors = Ou WJ, Bergeron JJ, Li Y, Kang CY, Thomas DY | title = Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2+ | journal = J Biol Chem | volume = 270 | issue = 30 | pages = 18051–9 | year = 1995 | pmid = 7629114 | doi=10.1074/jbc.270.30.18051| doi-access = free }}</ref>
▲==Cofactors==
[[Adenosine triphosphate|ATP]] and [[Ca++|calcium ions]] are cofactors involved in substrate binding for calnexin.
 
==External links==▼
* {{MeshName|Calnexin}}▼
 
== References ==
{{reflist}}
 
▲== External links ==
==Further reading==▼
▲* {{MeshName|Calnexin}}
 
▲== Further reading ==
{{refbegin | 2}}
* {{cite book | vauthors = Benyair R, Ron E, Lederkremer GZ | title = Protein quality control, retention, and degradation at the endoplasmic reticulum | volume = 292 | pages = 197–280 | year = 2011 | pmid = 22078962 | doi = 10.1016/B978-0-12-386033-0.00005-0 | series = International Review of Cell and Molecular Biology | isbn = 9780123860330 }}
{{PBB_Further_reading
* {{cite journal | vauthors = Del Bem LE | title = The evolutionary history of calreticulin and calnexin genes in green plants | journal = Genetica | volume = 139 | issue = 2 | pages = 225–9 | date = Feb 2011 | pmid = 21222018 | doi = 10.1007/s10709-010-9544-y | s2cid = 9228786 }}
| citations =
* {{cite journal | authorvauthors =Del BemKleizen B, Braakman I LEV| title =The evolutionaryProtein history of calreticulinfolding and calnexinquality genescontrol in greenthe plants.endoplasmic reticulum | journal =Genetica Current Opinion in Cell Biology | volume =139 16 | issue = 24 | pages = 225–9343–9 |year date = 2011Aug 2004 | pmid = 2122201815261665 | doi = 10.10071016/s10709j.ceb.2004.06.012 | hdl = 1874/5106 | hdl-010-9544-yaccess = free }}
* {{cite journal | authorvauthors =Kleizen Rasmussen HH, van Damme J, Puype M, Gesser B, BraakmanCelis IJE, Vandekerckhove J | title =Protein foldingMicrosequences andof quality145 controlproteins recorded in the endoplasmictwo-dimensional reticulum.gel protein database of normal human epidermal keratinocytes | journal =Curr. Opin. Cell Biol.Electrophoresis | volume =16 13 | issue = 412 | pages = 343–9960–9 |year date = 2005Dec 1992 | pmid = 152616651286667 | doi = 10.10161002/jelps.ceb.2004.06.01211501301199 | s2cid = 41855774 }}
* {{cite journal | authorvauthors =Rasmussen HHGalvin K, vanKrishna S, DammePonchel JF, PuypeFrohlich M, ''etCummings al.''DE, Carlson R, Wands JR, Isselbacher KJ, Pillai S, Ozturk M | title =Microsequences ofThe 145major proteinshistocompatibility recordedcomplex inclass theI twoantigen-dimensional gelbinding protein databasep88 ofis normalthe humanproduct epidermalof keratinocytes.the calnexin gene | journal =Electrophoresis Proceedings of the National Academy of Sciences of the United States of America | volume =13 89 | issue = 1218 | pages = 960–98452–6 |year date = 1993Sep 1992 | pmid = 12866671326756 | pmc = 49938 | doi = 10.10021073/elpspnas.1150130119989.18.8452 | bibcode = 1992PNAS...89.8452G | doi-access = free }}
* {{cite journal | authorvauthors =Galvin K, KrishnaPind S, PonchelRiordan FJR, ''etWilliams al.''DB | title =The majorParticipation histocompatibilityof complexthe classendoplasmic Ireticulum antigen-bindingchaperone proteincalnexin (p88, isIP90) in the productbiogenesis of the calnexincystic genefibrosis transmembrane conductance regulator | journal =Proc. Natl.The Acad.Journal Sci.of U.S.A.Biological Chemistry | volume =89 269 | issue = 1817 | pages = 8452–612784–8 |year= 1992date |pmid= 1326756Apr 1994 | doi = 10.10731016/pnas.89.S0021-9258(18.8452)99944-8 | pmid = 7513695 | pmcdoi-access =49938 free }}
* {{cite journal | authorvauthors =Pind SHonoré B, RiordanRasmussen JRHH, WilliamsCelis DBA, Leffers H, Madsen P, Celis JE | title =Participation ofThe themolecular endoplasmicchaperones reticulumHSP28, GRP78, endoplasmin, chaperoneand calnexin (p88,exhibit IP90)strikingly different levels in thequiescent biogenesiskeratinocytes ofas thecompared cysticto fibrosistheir transmembraneproliferating conductancenormal regulatorand transformed counterparts: cDNA cloning and expression of calnexin | journal =J. Biol. Chem.Electrophoresis | volume =269 15 | issue = 173–4 | pages = 12784–8482–90 | year = 19941992 | pmid = 75136958055875 | doi = 10.1002/elps.1150150166 | s2cid = 22393279 }}
* {{cite journal | authorvauthors =Honoré BTjoelker LW, RasmussenSeyfried HHCE, CelisEddy ARL, ''etByers al.''MG, |title=TheShows molecularTB, chaperonesCalderon HSP28J, GRP78,Schreiber endoplasminRB, andGray calnexinPW exhibit| strikinglytitle different= levelsHuman, inmouse, quiescentand keratinocytesrat ascalnexin comparedcDNA tocloning: theiridentification proliferatingof normalpotential andcalcium transformedbinding counterparts:motifs cDNAand cloninggene andlocalization expressionto ofhuman calnexinchromosome 5 | journal =Electrophoresis Biochemistry | volume =15 33 | issue = 3–411 | pages = 482–903229–36 |year date = Mar 1994 | pmid = 80558758136357 | doi = 10.10021021/elps.1150150166 bi00177a013 }}
* {{cite journal | authorvauthors =Tjoelker LW,Lenter Seyfried CEM, EddyVestweber RL, ''et al.''D | title =Human, mouse,The andintegrin ratchains calnexinbeta cDNA1 cloning:and identificationalpha of6 potentialassociate calciumwith bindingthe motifschaperone andcalnexin gene localizationprior to humanintegrin chromosomeassembly 5| |journal =Biochemistry The Journal of Biological Chemistry | volume =33 269 | issue = 1116 | pages = 3229–3612263–8 |year date = Apr 1994 | doi = 10.1016/S0021-9258(17)32710-2 | pmid = 81363578163531 | doi-access =10.1021/bi00177a013 free }}
* {{cite journal | authorvauthors =Lenter MRajagopalan S, VestweberXu DY, Brenner MB | title =The integrinRetention chainsof betaunassembled 1components andof alphaintegral 6membrane associateproteins with the chaperoneby calnexin prior to integrin assembly | journal =J. Biol. Chem.Science | volume =269 263 | issue = 165145 | pages = 12263–8387–90 |year date = Jan 1994 | pmid = 81635318278814 | doi = 10.1126/science.8278814 | bibcode = 1994Sci...263..387R }}
* {{cite journal | authorvauthors =Rajagopalan SDavid V, XuHochstenbach YF, Rajagopalan S, Brenner MB | title =Retention ofInteraction unassembledwith componentsnewly ofsynthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane proteinsprotein byIP90 (calnexin) | journal =Science The Journal of Biological Chemistry | volume =263 268 | issue = 514513 | pages = 387–909585–92 |year= 1994date |pmid= 8278814May 1993 | doi = 10.11261016/science.8278814S0021-9258(18)98391-2 | pmid = 8486646 | doi-access = free }}
* {{cite journal | authorvauthors =David VBellovino D, HochstenbachMorimoto FT, RajagopalanTosetti SF, BrennerGaetani MBS | title =Interaction withRetinol newlybinding synthesizedprotein and retainedtransthyretin proteinsare secreted as a complex formed in the endoplasmic reticulum suggestsin a chaperone function forHepG2 human integral membrane protein IP90hepatocarcinoma (calnexin)cells | journal =J. Biol.Experimental Chem.Cell Research | volume =268 222 | issue = 131 | pages = 9585–9277–83 |year date = 1993Jan 1996 | pmid = 84866468549676 | doi = 10.1006/excr.1996.0010 | doi-access = free }}
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* {{cite journal | authorvauthors =Otteken ADevergne O, MossHummel BM, |title=CalreticulinKoeppen interactsH, withLe newlyBeau synthesizedMM, humanNathanson immunodeficiencyEC, virusKieff typeE, 1Birkenbach envelopeM glycoprotein,| suggestingtitle a= chaperoneA functionnovel similarinterleukin-12 top40-related thatprotein ofinduced calnexinby latent Epstein-Barr virus infection in B lymphocytes | journal =J. Biol.Journal Chem.of Virology | volume =271 70 | issue = 12 | pages = 97–1031143–53 |year date = Feb 1996 | pmid = 85506328551575 | pmc = 189923 | doi = 10.10741128/jbcJVI.27170.12.97 1143-1153.1996}}
* {{cite journal | authorvauthors =Devergne OAndersson B, HummelWentland MMA, KoeppenRicafrente HJY, ''etLiu al.''W, |title=AGibbs novelRA interleukin-12| p40-relatedtitle protein= inducedA by"double latentadaptor" Epstein-Barrmethod virusfor infectionimproved inshotgun Blibrary lymphocytesconstruction | journal =J. Virol.Analytical Biochemistry | volume =70 236 | issue = 21 | pages = 1143–53107–13 |year date = Apr 1996 | pmid= 8551575 |doi= 8619474 | pmcdoi =189923 10.1006/abio.1996.0138 }}
* {{cite journal | authorvauthors =Andersson B,van WentlandLeeuwen MAJE, RicafrenteKearse JY,KP ''et| al.''title |title=A "doubleCalnexin adaptor"associates methodexclusively forwith improvedindividual shotgunCD3 librarydelta constructionand T cell antigen receptor (TCR) alpha proteins containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexes | journal =Anal. Biochem.The Journal of Biological Chemistry | volume =236 271 | issue = 116 | pages = 107–139660–5 |year date = Apr 1996 | pmid = 86194748621641 | doi = 10.10061074/abiojbc.1996271.013816.9660 | doi-access = free }}
* {{cite journal | authorvauthors =van LeeuwenOliver JEJD, KearseHresko KPRC, |title=CalnexinMueckler associatesM, exclusivelyHigh withS individual| CD3title delta= andThe Tglut cell1 antigenglucose receptortransporter (TCR)interacts alphawith proteinscalnexin containingand incompletelycalreticulin trimmed| glycansjournal that are= notThe assembledJournal intoof multisubunitBiological TCR complexesChemistry |journal=J. Biol. Chem. |volume = 271 | issue = 1623 | pages = 9660–513691–6 |year date = Jun 1996 | pmid = 86216418662691 | doi = 10.1074/jbc.271.1623.966013691 | doi-access = free }}
* {{cite journal | authorvauthors =Oliver JDLi Y, HreskoBergeron RCJJ, MuecklerLuo ML, HighOu SWJ, Thomas DY, Kang CY | title =The glutEffects of inefficient cleavage of the signal sequence of HIV-1 glucosegp transporter120 interactson its association with calnexin, folding, and calreticulinintracellular transport | journal =J. Biol.Proceedings Chem.of the National Academy of Sciences of the United States of America | volume =271 93 | issue = 2318 | pages = 13691–69606–11 |year date = Sep 1996 | pmid = 86626918790377 | pmc = 38475 | doi = 10.10741073/jbcpnas.27193.2318.136919606 | bibcode = 1996PNAS...93.9606L | doi-access = free }}
* {{cite journal | authorvauthors =Li Y, BergeronTrombetta JJES, LuoSimons LJF, ''etHelenius al.''A | title =Effects ofEndoplasmic inefficientreticulum cleavageglucosidase ofII theis signal sequencecomposed of HIV-1a gpcatalytic 120subunit, onconserved itsfrom associationyeast with calnexin,to foldingmammals, and intracellulara transporttightly bound noncatalytic HDEL-containing subunit | journal =Proc. Natl.The Acad.Journal Sci.of U.S.A.Biological Chemistry | volume =93 271 | issue = 1844 | pages = 9606–1127509–16 |year date = Nov 1996 | pmid = 87903778910335 | doi = 10.10731074/pnasjbc.93271.1844.9606 27509 | pmcdoi-access =38475 free }}
* {{cite journal | authorvauthors =Trombetta ES,Tatu Simons JFU, Helenius A | title =Endoplasmic reticulumInteractions glucosidasebetween IInewly issynthesized composedglycoproteins, ofcalnexin and a catalyticnetwork subunit,of conservedresident fromchaperones yeastin tothe mammals,endoplasmic andreticulum a| tightlyjournal bound= noncatalyticThe HDEL-containingJournal subunitof |journal=J.Cell Biol. Chem.Biology | volume =271 136 | issue = 443 | pages = 27509–16555–65 |year date = 1996Feb 1997 | pmid = 89103359024687 | pmc = 2134297 | doi = 10.10741083/jbcjcb.271136.443.27509 555 }}
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* {{cite journal | authorvauthors =Wiest DLYu W, BhandoolaAndersson AB, PuntWorley JKC, ''etMuzny al.''DM, |title=IncompleteDing endoplasmicY, reticulumLiu (ER)W, retentionRicafrente inJY, immatureWentland thymocytesMA, asLennon revealedG, byGibbs surfaceRA expression| oftitle "ER= Large-resident"scale molecularconcatenation chaperonescDNA sequencing | journal =Proc. Natl.Genome Acad.Research Sci.| U.S.A.volume |volume=94 7 | issue = 54 | pages = 1884–9353–8 |year date = Apr 1997 | pmid = 90508749110174 | pmc = 139146 | doi = 10.10731101/pnasgr.947.54.1884 | pmc=20012 353 }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-Scale Concatenation cDNA Sequencing |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi= 10.1101/gr.7.4.353| pmc=139146 }}
}}
{{refend}}
 
{{PDB Gallery|geneid=821}}
 
{{Calcium-binding proteins}}
{{Lectins}}
{{Membrane proteins}}
 
{{membrane-protein-stub}}
 
[[Category:Integral membrane proteins]]
[[Category:C-type lectins]]
[[Category:Molecular chaperones]]
 
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