CALR_BOMMO
ID CALR_BOMMO Reviewed; 398 AA.
AC Q7Z1E6; P82199; Q869E0;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Calreticulin;
DE Flags: Precursor;
GN Name=crt {ECO:0000312|EMBL:BAC57964.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1] {ECO:0000312|EMBL:AAP50845.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RA Kim S.R., Lee K.S., Kim I., Kang S.W., Nho S.K., Sohn H.D., Jin B.R.;
RT "Molecular cloning of a cDNA encoding putative calreticulin from the
RT silkworm, Bombyx mori.";
RL Int. J. Ind. Entomol. 6:93-97(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAP50845.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16172913; DOI=10.1007/s11033-004-5908-7;
RA Goo T.W., Park S., Jin B.R., Yun E.Y., Kim I., Nho S.-K., Kang S.-W.,
RA Kwon O.-Y.;
RT "Endoplasmic reticulum stress response of Bombyx mori calreticulin.";
RL Mol. Biol. Rep. 32:133-139(2005).
RN [3] {ECO:0000312|EMBL:BAC57964.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=p50T; TISSUE=Fat body {ECO:0000312|EMBL:BAC57964.1};
RA Takahashi T., Yamashita T.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 20-49.
RC STRAIN=Xinhang X Keming {ECO:0000269|PubMed:11280994};
RC TISSUE=Body wall {ECO:0000269|PubMed:11280994}, and
RC Fat body {ECO:0000269|PubMed:11280994};
RX PubMed=11280994;
RA Zhong B.-X.;
RT "Protein database for several tissues derived from five instar of
RT silkworm.";
RL Yi Chuan Xue Bao 28:217-224(2001).
CC -!- FUNCTION: Molecular calcium-binding chaperone promoting folding,
CC oligomeric assembly and quality control in the ER via the
CC calreticulin/calnexin cycle. This lectin may interact transiently with
CC almost all of the monoglucosylated glycoproteins that are synthesized
CC in the ER (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P27797}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- TISSUE SPECIFICITY: Expressed in fat bodies. Not expressed in midgut,
CC silk gland, ovary or testis. {ECO:0000269|PubMed:16172913,
CC ECO:0000269|Ref.1}.
CC -!- INDUCTION: Induced by disturbances in intracellular calcium levels
CC caused by the chelators BAPTA-AM and EDTA, the endoplasmic reticulum
CC calcium-ATPase inhibitor thapsigargin and by calcium. Not induced by
CC the endoplasmic reticulum stress-inducing drugs brefeldin A, DTT and
CC tunicamycin, or by heat stress and hydrogen peroxide.
CC {ECO:0000269|PubMed:16172913}.
CC -!- DOMAIN: Can be divided into a N-terminal globular domain, a proline-
CC rich P-domain forming an elongated arm-like structure and a C-terminal
CC acidic domain. The P-domain binds one molecule of calcium with high
CC affinity, whereas the acidic C-domain binds multiple calcium ions with
CC low affinity (By similarity). {ECO:0000250|UniProtKB:P27797}.
CC -!- DOMAIN: The interaction with glycans occurs through a binding site in
CC the globular lectin domain. {ECO:0000250|UniProtKB:P27797}.
CC -!- DOMAIN: The zinc binding sites are localized to the N-domain.
CC {ECO:0000250|UniProtKB:P27797}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000255}.
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DR EMBL; AY297158; AAP50845.1; -; mRNA.
DR EMBL; AB090887; BAC57964.1; -; mRNA.
DR RefSeq; NP_001037075.1; NM_001043610.1.
DR AlphaFoldDB; Q7Z1E6; -.
DR SMR; Q7Z1E6; -.
DR STRING; 7091.BGIBMGA000475-TA; -.
DR PRIDE; Q7Z1E6; -.
DR GeneID; 692629; -.
DR KEGG; bmor:692629; -.
DR CTD; 45841; -.
DR eggNOG; KOG0674; Eukaryota.
DR HOGENOM; CLU_018224_0_2_1; -.
DR InParanoid; Q7Z1E6; -.
DR OrthoDB; 822188at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; 3.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Calcium; Chaperone; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Lectin; Metal-binding; Reference proteome; Repeat;
KW Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..398
FT /note="Calreticulin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000279696"
FT REPEAT 191..202
FT /note="1-1"
FT /evidence="ECO:0000255"
FT REPEAT 210..221
FT /note="1-2"
FT /evidence="ECO:0000255"
FT REPEAT 227..238
FT /note="1-3"
FT /evidence="ECO:0000255"
FT REPEAT 244..255
FT /note="1-4"
FT /evidence="ECO:0000255"
FT REPEAT 259..269
FT /note="2-1"
FT /evidence="ECO:0000255"
FT REPEAT 273..283
FT /note="2-2"
FT /evidence="ECO:0000255"
FT REPEAT 287..297
FT /note="2-3"
FT /evidence="ECO:0000255"
FT REGION 20..197
FT /note="N-domain"
FT /evidence="ECO:0000255"
FT REGION 191..255
FT /note="4 X approximate repeats"
FT /evidence="ECO:0000255"
FT REGION 198..308
FT /note="P-domain"
FT /evidence="ECO:0000255"
FT REGION 207..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..297
FT /note="3 X approximate repeats"
FT /evidence="ECO:0000255"
FT REGION 309..398
FT /note="C-domain"
FT /evidence="ECO:0000255"
FT REGION 334..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 395..398
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT COMPBIAS 207..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..398
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 111
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 128
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 135
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 317
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT DISULFID 105..137
FT /evidence="ECO:0000250|UniProtKB:P27797"
FT CONFLICT 36
FT /note="W -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="H -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="E -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="G -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="F -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="N -> P (in Ref. 3; BAC57964)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="Y -> F (in Ref. 3; BAC57964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45802 MW; 0BC049839F5950EA CRC64;
MKAVVLVVVS LLALSSINCD VFFEEKFPDD SWESNWVYSE HPGKEFGKFK LTAGKFFSDP
EDDKGLKTSE DARFYALSRK FKPFSNEGKP LVVQFTVKHE QDIDCGGGYL KVFDCKLEQK
DMHGETPYEI MFGPDICGPG TKKVHVIFSY KGKNHLIKKD IRCKDDVYTH LYTLIVKPDN
TYEVLIDNEK VESGDLEADW DFLPNKKIKD PEAKKPEDWD DKPTIPDPED KKPEDWDKPE
HIPDPDATKP EDWDDEMDGE WEPPMIDNPD YKGVWAPKQI DNPAYKGPWV HPEIDNPEYT
PDSNLYKRDE ICAVGLDLWQ VKSGTIFDDF LITDDPAAAK ERGEVIKKRQ EGEKKMKSEQ
DEAEREKEKA EKPDDEEDDE DLDDETGDAA PVEEHDEL
