ID   A0A140ZYV0_TACFU        Unreviewed;       418 AA.
AC   A0A140ZYV0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Calreticulin {ECO:0000256|PIRNR:PIRNR002356};
GN   Name=CRT {ECO:0000313|EMBL:AJS13455.1};
OS   Tachysurus fulvidraco (Yellow catfish) (Pimelodus fulvidraco).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Bagridae; Tachysurus.
OX   NCBI_TaxID=1234273 {ECO:0000313|EMBL:AJS13455.1};
RN   [1] {ECO:0000313|EMBL:AJS13455.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Huang C.;
RT   "Molecular cloning and mRNA tissue expression of grp78 and calreticulin in
RT   yellow catfish Pelteobagrus fulvidraco and Javelin goby Synechogobius
RT   hasta.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319, ECO:0000256|PIRNR:PIRNR002356}.
CC   -!- SIMILARITY: Belongs to the calreticulin family.
CC       {ECO:0000256|ARBA:ARBA00010983, ECO:0000256|PIRNR:PIRNR002356,
CC       ECO:0000256|RuleBase:RU362126}.
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DR   EMBL; KM114875; AJS13455.1; -; mRNA.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
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; IPR009169; Calreticulin.
DR   InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   PANTHER; PTHR11073; PTHR11073; 1.
DR   Pfam; PF00262; Calreticulin; 2.
DR   PIRSF; PIRSF002356; Calreticulin; 1.
DR   PRINTS; PR00626; CALRETICULIN.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF63887; SSF63887; 1.
DR   PROSITE; PS00803; CALRETICULIN_1; 1.
DR   PROSITE; PS00804; CALRETICULIN_2; 1.
DR   PROSITE; PS00805; CALRETICULIN_REPEAT; 1.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|PIRSR:PIRSR002356-2};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PIRNR:PIRNR002356};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|PIRNR:PIRNR002356};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR002356-2};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU362126}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU362126"
FT   CHAIN           19..418
FT                   /note="Calreticulin"
FT                   /evidence="ECO:0000256|RuleBase:RU362126"
FT                   /id="PRO_5007356956"
FT   REGION          196..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..418
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002356-2"
FT   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002356-2"
FT   BINDING         65
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002356-2"
FT   BINDING         110
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002356-1"
FT   BINDING         112
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002356-1"
FT   BINDING         129
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002356-1"
FT   BINDING         136
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002356-1"
FT   BINDING         318
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002356-1"
FT   BINDING         329
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002356-2"
FT   DISULFID        106..138
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002356-3"
SQ   SEQUENCE   418 AA;  48458 MW;  0C8500360C09B051 CRC64;
     MTTLCLLFMS LSLALVAAEP TVYFREQFED GDAWKSRWLE STHKSDYGKF VLSAGKFYGD
     AEKDKGLQTS QDAHFYAISS RFEDFSNKDQ PLVVQFTAKH EQSIDCGGGY IKLFPSSIKQ
     EEMHGESTYN IMFGPDICGP GTKKVHVIFN YKGKNHLINK DIRCKDDEYT HLYTLIVNPD
     NTYEVKIDNK KVESGSLEDD WDFLPPKKIK DPEAKKPEDW DEQEKIDDPD DKKPEDWDEP
     ETIPDPDAKK PDDWDEEMDG EWEPPMVTNP DYKGEWKPKQ IDNPAYKGKW VHPEIDNPEY
     TPDAEIYKYS SNGVIGLDLW QVKSGTIFDN FLITNDPKLA EKIADESWGA TKDAEKKMKE
     SQEEEERKKR EEEDKKRSEE AKDEADEEKD EEEEEEEEDD DEDEDDEEGT DSNLKDEL
//