ID   A0A140ZYV0_TACFU        Unreviewed;       418 AA.
AC   A0A140ZYV0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
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}.
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; KM114875; AJS13455.1; -; mRNA.
DR   AlphaFoldDB; A0A140ZYV0; -.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0060473; C:cortical granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0033018; C:sarcoplasmic 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; 2.60.120.200; -; 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; IPR009169; Calreticulin.
DR   InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   PANTHER; PTHR11073:SF59; CALRETICULIN; 1.
DR   PANTHER; PTHR11073; CALRETICULIN AND CALNEXIN; 1.
DR   Pfam; PF00262; Calreticulin; 2.
DR   PIRSF; PIRSF002356; Calreticulin; 1.
DR   PRINTS; PR00626; CALRETICULIN.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF63887; P-domain of calnexin/calreticulin; 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   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PIRNR:PIRNR002356};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR002356-3};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|PIRNR:PIRNR002356}; 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   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
//