ID   A0A140ZYV0_TACFU        Unreviewed;       418 AA.
AC   A0A140ZYV0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   16-OCT-2019, entry version 13.
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
RT   calreticulin in yellow catfish Pelteobagrus fulvidraco and Javelin
RT   goby Synechogobius hasta.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|PIRNR:PIRNR002356}.
CC   -!- SIMILARITY: Belongs to the calreticulin family.
CC       {ECO:0000256|PIRNR:PIRNR002356, ECO:0000256|RuleBase:RU362126,
CC       ECO:0000256|SAAS:SAAS00583791}.
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   GO; GO:0005783; C:endoplasmic reticulum; 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|PIRNR:PIRNR002356,
KW   ECO:0000256|RuleBase:RU362126, ECO:0000256|SAAS:SAAS00030830};
KW   Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR002356,
KW   ECO:0000256|RuleBase:RU362126};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR002356-2};
KW   Signal {ECO:0000256|RuleBase:RU362126}.
FT   SIGNAL        1     18       {ECO:0000256|RuleBase:RU362126}.
FT   CHAIN        19    418       Calreticulin. {ECO:0000256|RuleBase:
FT                                RU362126}.
FT                                /FTId=PRO_5007356956.
FT   REGION      196    280       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      344    418       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    196    255       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    344    383       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    384    418       Acidic. {ECO:0000256|SAM:MobiDB-lite}.
FT   METAL        27     27       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR002356-2}.
FT   METAL        63     63       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR002356-2}.
FT   METAL        65     65       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR002356-2}.
FT   METAL       329    329       Calcium. {ECO:0000256|PIRSR:PIRSR002356-
FT                                2}.
FT   BINDING     110    110       Carbohydrate. {ECO:0000256|PIRSR:
FT                                PIRSR002356-1}.
FT   BINDING     112    112       Carbohydrate. {ECO:0000256|PIRSR:
FT                                PIRSR002356-1}.
FT   BINDING     129    129       Carbohydrate. {ECO:0000256|PIRSR:
FT                                PIRSR002356-1}.
FT   BINDING     136    136       Carbohydrate. {ECO:0000256|PIRSR:
FT                                PIRSR002356-1}.
FT   BINDING     318    318       Carbohydrate. {ECO:0000256|PIRSR:
FT                                PIRSR002356-1}.
FT   DISULFID    106    138       {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
//