ID CALX_HUMAN STANDARD; PRT; 592 AA. AC P27824; DT 01-AUG-1992 (Rel. 23, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Calnexin precursor (Major histocompatibility complex class I DE antigen-binding protein p88) (p90) (IP90). GN CANX. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93252832; PubMed=8486646; RA David V., Hochstenbach F., Rajagopalan S., Brenner M.B.; RT "Interaction with newly synthesized and retained proteins in the RT endoplasmic reticulum suggests a chaperone function for human RT integral membrane protein IP90 (calnexin)."; RL J. Biol. Chem. 268:9585-9592(1993). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Placenta; RX MEDLINE=94183823; PubMed=8136357; RA Tjoelker L.W., Seyfried C.E., Eddy R.L. Jr., Shows T.B. Jr., RA Calderon J., Schreiber R.B., Gray P.W.; RT "Human, mouse, and rat calnexin cDNA cloning: identification of RT potential calcium binding motifs and gene localization to human RT chromosome 5."; RL Biochemistry 33:3229-3236(1994). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Keratinocytes; RX MEDLINE=94333293; PubMed=8055875; RA Honore B., Rasmussen H.H., Celis A., Leffers H., Madsen P., RA Celis J.E.; RT "The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin RT exhibit strikingly different levels in quiescent keratinocytes as RT compared to their proliferating normal and transformed counterparts: RT cDNA cloning and expression of calnexin."; RL Electrophoresis 15:482-490(1994). RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Fibroblast; RA Hansen J.J., Jorgensen M.M., Bolund L., Gregersen N.; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC TISSUE=Placenta; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP SEQUENCE OF 237-592 FROM N.A. RX MEDLINE=92409534; PubMed=1326756; RA Galvin K., Krishna S., Ponchel F., Frohlich M., Cummings D.E., RA Carlson R., Wands J.R., Isselbacher K.J., Pillai S., Ozturk M.; RT "The major histocompatibility complex class I antigen-binding protein RT p88 is the product of the calnexin gene."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8452-8456(1992). RN [7] RP PARTIAL SEQUENCE OF 275-286; 293-313; 383-398 AND 516-523. RC TISSUE=Keratinocytes; RX MEDLINE=93162043; PubMed=1286667; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). CC -!- FUNCTION: CALCIUM-BINDING PROTEIN THAT INTERACTS WITH NEWLY CC SYNTHESIZED GLYCOPROTEINS IN THE ENDOPLASMIC RETICULUM. IT MAY ACT CC IN ASSISTING PROTEIN ASSEMBLY AND/OR IN THE RETENTION WITHIN THE CC ER OF UNASSEMBLED PROTEIN SUBUNITS. IT SEEMS TO PLAY A MAJOR ROLE CC IN THE QUALITY CONTROL APPARATUS OF THE ER BY THE RETENTION OF CC INCORRECTLY FOLDED PROTEINS. CC -!- SUBCELLULAR LOCATION: Type I membrane protein. Endoplasmic CC reticulum. CC -!- SIMILARITY: BELONGS TO THE CALRETICULIN FAMILY. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L10284; AAA36125.1; -. DR EMBL; L18887; AAA21013.1; -. DR EMBL; M94859; AAA21749.1; -. DR EMBL; M98452; AAA35696.1; -. DR EMBL; BC003552; AAH03552.1; -. DR EMBL; AJ271880; CAB72137.1; -. DR PIR; A46673; A46673. DR Aarhus/Ghent-2DPAGE; 9702; IEF. DR Genew; HGNC:1473; CANX. DR MIM; 114217; -. DR GO; GO:0009306; P:protein secretion; TAS. DR InterPro; IPR001580; Calreticulin. DR Pfam; PF00262; calreticulin; 1. DR PRINTS; PR00626; CALRETICULIN. DR ProDom; PD001866; Calreticulin; 1. DR PROSITE; PS00803; CALRETICULIN_1; 1. DR PROSITE; PS00804; CALRETICULIN_2; 1. DR PROSITE; PS00805; CALRETICULIN_REPEAT; 3. KW Calcium-binding; Endoplasmic reticulum; Transmembrane; Signal; KW Repeat; Chaperone. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 592 CALNEXIN. FT DOMAIN 21 481 LUMENAL (POTENTIAL). FT TRANSMEM 482 502 POTENTIAL. FT DOMAIN 503 592 CYTOPLASMIC (POTENTIAL). FT DOMAIN 278 345 4 X APPROXIMATE REPEATS. FT REPEAT 278 290 1-1. FT REPEAT 295 307 1-2. FT REPEAT 314 326 1-3. FT REPEAT 333 345 1-4. FT DOMAIN 348 405 4 X APPROXIMATE REPEATS. FT REPEAT 348 358 2-1. FT REPEAT 367 377 2-2. FT REPEAT 381 391 2-3. FT REPEAT 395 405 2-4. FT CONFLICT 179 179 F -> L (IN REF. 2). FT CONFLICT 431 433 SDI -> LTF (IN REF. 6). FT CONFLICT 480 480 R -> L (IN REF. 4). SQ SEQUENCE 592 AA; 67568 MW; EDE094D9B82261EE CRC64; MEGKWLLCML LVLGTAIVEA HDGHDDDVID IEDDLDDVIE EVEDSKPDTT APPSSPKVTY KAPVPTGEVY FADSFDRGTL SGWILSKAKK DDTDDEIAKY DGKWEVEEMK ESKLPGDKGL VLMSRAKHHA ISAKLNKPFL FDTKPLIVQY EVNFQNGIEC GGAYVKLLSK TPELNLDQFH DKTPYTIMFG PDKCGEDYKL HFIFRHKNPK TGIYEEKHAK RPDADLKTYF TDKKTHLYTL ILNPDNSFEI LVDQSVVNSG NLLNDMTPPV NPSREIEDPE DRKPEDWDER PKIPDPEAVK PDDWDEDAPA KIPDEEATKP EGWLDDEPEY VPDPDAEKPE DWDEDMDGEW EAPQIANPRC ESAPGCGVWQ RPVIDNPNYK GKWKPPMIDN PSYQGIWKPR KIPNPDFFED LEPFRMTPFS AIGLELWSMT SDIFFDNFII CADRRIVDDW ANDGWGLKKA ADGAAEPGVV GQMIEAAEER PWLWVVYILT VALPVFLVIL FCCSGKKQTS GMEYKKTDAP QPDVKEEEEE KEEEKDKGDE EEEGEEKLEE KQKSDAEEDG GTVSQEEEDR KPKAEEDEIL NRSPRNRKPR RE //