ID F1C774_PERFV Unreviewed; 422 AA. AC F1C774; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 40. DE RecName: Full=Calnexin {ECO:0000256|ARBA:ARBA00040224}; DE Flags: Fragment; GN Name=Canx {ECO:0000313|EMBL:ADX97134.1}; OS Perca flavescens (American yellow perch) (Morone flavescens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca. OX NCBI_TaxID=8167 {ECO:0000313|EMBL:ADX97134.1}; RN [1] {ECO:0000313|EMBL:ADX97134.1} RP NUCLEOTIDE SEQUENCE. RA Pierron F., Normandeau E., Campbell P.G.C., Bernatchez L., Couture P.; RT "Effects of chronic metal exposure on wild fish populations revealed by RT high-throughput cDNA sequencing."; RL Submitted (SEP-2010) 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. CC {ECO:0000256|ARBA:ARBA00037453}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004115}. Melanosome membrane CC {ECO:0000256|ARBA:ARBA00004573}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004573}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. Mitochondrion membrane CC {ECO:0000256|ARBA:ARBA00004583}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004583}. CC -!- SIMILARITY: Belongs to the calreticulin family. CC {ECO:0000256|ARBA:ARBA00010983, ECO:0000256|RuleBase:RU362126}. 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; HQ206536; ADX97134.1; -; mRNA. DR AlphaFoldDB; F1C774; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.10.250.10; Calreticulin/calnexin, P domain; 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:SF11; CALNEXIN; 1. DR PANTHER; PTHR11073; CALRETICULIN AND CALNEXIN; 1. DR Pfam; PF00262; Calreticulin; 1. DR PRINTS; PR00626; CALRETICULIN. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2. DR SUPFAM; SSF63887; P-domain of calnexin/calreticulin; 1. DR PROSITE; PS00804; CALRETICULIN_2; 1. DR PROSITE; PS00805; CALRETICULIN_REPEAT; 1. PE 2: Evidence at transcript level; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU362126}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, KW ECO:0000256|RuleBase:RU362126}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}; KW Membrane {ECO:0000256|RuleBase:RU362126}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transmembrane {ECO:0000256|RuleBase:RU362126}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362126}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}. FT TRANSMEM 377..398 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362126" FT REGION 156..221 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 237..262 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 403..422 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 180..202 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 407..422 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ADX97134.1" FT NON_TER 422 FT /evidence="ECO:0000313|EMBL:ADX97134.1" SQ SEQUENCE 422 AA; 47683 MW; 3C3A3C4C91EE8408 CRC64; VEEMKDSKLP GDKGLVLKTR AKHHAISAQL LRPFTFDTKP LIVQYEVNFQ SGIDCGGAYV KLLTQTPDLD LDQFKDKTPY TIMFGPDKCG EDYKLHFIFR HKNPKTGEYE EKHAKKPDAD LRTYYTDKKT HLYTLVLNPD NSFEVLVDQT VVNSGSLLTD MTPPVNPPAE IEDPDDQKPD DWDERPKIQD PAAAKPEDWD EDAPAQIPDE DAVKPDGWLD DEPEYIGDPD AVKPEDWDED MDGEWEAPQV PNPACETAPG CGEWKRPMID NPNHKGKWKP PMIDNPNYQG VWKPRKVPNP AFFEDLQPFR MSAFSAVGLE LWSMTSDIFF DNFFITDDRN TAERWAADGW GLKKAAEGAA DPGLATQMLN AAEERPWLWI VYVLTVALPL VLIIVFCCTG KKKSPATPAA EYKKTDEAQP DV //