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 01-JUN-1994 (REL. 29, 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; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RM 93252832 RA DAVID V., HOCHSTENBACH F., RAJAGOPALAN S., BRENNER M.B.; RL J. BIOL. CHEM. 268:9585-9592(1993). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA TJOELKER L.W., SEYFRIED C.E., EDDY R.L. JR., SHOWS T.B. JR., RA CALDERON J., SCHREIBER R.B., GRAY P.W.; RL SUBMITTED (XXX-1993) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [3] RP SEQUENCE FROM N.A. RA HONORE B., LEFFERS H., MADSEN P., CELIS J.E.; RL SUBMITTED (JUN-1992) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [4] RP SEQUENCE OF 237-592 FROM N.A. RM 92409534 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.; RL PROC. NATL. ACAD. SCI. U.S.A. 89:8452-8456(1992). RN [5] RP PARTIAL SEQUENCE OF 275-286; 293-313; 383-398 AND 516-523. RC TISSUE=KERATINOCYTES; RM 93162043 RA RASMUSSEN H.H., VAN DAMME J., PUYPE M., GESSER B., CELIS J.E., RA VANDEKERCKHOVE J.; 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; HSIP90. DR EMBL; L18887; HSCALNEXI. DR EMBL; M94859; HSCALIEF. DR EMBL; M98452; HSCLNXN. DR AARHUS/GHENT-2DPAGE; 9702; IEF. DR MIM; 114217; 11TH EDITION. DR PIR; A46673; A46673. DR PROSITE; PS00803; CALRETICULIN_1. DR PROSITE; PS00804; CALRETICULIN_2. DR PROSITE; PS00805; CALRETICULIN_REPEAT. KW CALCIUM-BINDING; ENDOPLASMIC RETICULUM; TRANSMEMBRANE; SIGNAL; KW REPEAT; CHAPERONE. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 592 CALNEXIN. FT DOMAIN 21 462 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. 4). FT CONFLICT 480 480 R -> L (IN REF. 4). SQ SEQUENCE 592 AA; 67568 MW; 1712680 CN; 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 //