ID F1C774_PERFV Unreviewed; 422 AA. AC F1C774; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 25-MAY-2022, entry version 36. DE SubName: Full=Calnexin {ECO:0000313|EMBL:ADX97134.1}; 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 -!- 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 GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of 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; 2.10.250.10; -; 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; 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}; Membrane {ECO:0000256|RuleBase:RU362126}; KW Transmembrane {ECO:0000256|RuleBase:RU362126}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362126}. 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 //