CALR_SCHMA
ID CALR_SCHMA Reviewed; 393 AA.
AC Q06814; Q26562;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Calreticulin;
DE AltName: Full=Protein SM4;
DE Flags: Precursor;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Puerto Rican;
RX PubMed=8433712; DOI=10.1016/0166-6851(93)90195-4;
RA Khalife J., Trottein F., Schacht A.-M., Godin C., Pierce R.J., Capron A.;
RT "Cloning of the gene encoding a Schistosoma mansoni antigen homologous to
RT human Ro/SS-A autoantigen.";
RL Mol. Biochem. Parasitol. 57:193-202(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Puerto Rican;
RX PubMed=8139623; DOI=10.1016/0166-6851(93)90120-m;
RA Khalife J., Pierce R.J., Godin C., Capron A.;
RT "Cloning and sequencing of the gene encoding Schistosoma mansoni
RT calreticulin.";
RL Mol. Biochem. Parasitol. 62:313-315(1993).
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
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}.
CC -!- DOMAIN: The interaction with glycans occurs through a binding site in
CC the globular lectin domain. {ECO:0000250}.
CC -!- DOMAIN: The zinc binding sites are localized to the N-domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR EMBL; M93097; AAA29854.1; -; mRNA.
DR EMBL; L24159; AAA19024.1; -; Genomic_DNA.
DR PIR; A48573; A48573.
DR AlphaFoldDB; Q06814; -.
DR SMR; Q06814; -.
DR STRING; 6183.Smp_030370.1; -.
DR PRIDE; Q06814; -.
DR eggNOG; KOG0674; Eukaryota.
DR HOGENOM; CLU_018224_0_2_1; -.
DR Proteomes; UP000008854; 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; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 2: Evidence at transcript level;
KW Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Lectin; Metal-binding; Reference proteome; Repeat; Signal; Zinc.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..393
FT /note="Calreticulin"
FT /id="PRO_0000004183"
FT REPEAT 189..200
FT /note="1-1"
FT REPEAT 208..219
FT /note="1-2"
FT REPEAT 225..236
FT /note="1-3"
FT REPEAT 242..253
FT /note="1-4"
FT REPEAT 257..267
FT /note="2-1"
FT REPEAT 271..281
FT /note="2-2"
FT REPEAT 285..295
FT /note="2-3"
FT REGION 189..253
FT /note="4 X 12 AA approximate repeats"
FT REGION 194..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..295
FT /note="3 X 11 AA approximate repeats"
FT REGION 351..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 390..393
FT /note="Prevents secretion from ER"
FT BINDING 107
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 109
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 126
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 133
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 315
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..135
FT /evidence="ECO:0000250"
FT CONFLICT 89..90
FT /note="MV -> IL (in Ref. 2; AAA19024)"
FT /evidence="ECO:0000305"
FT CONFLICT 188..207
FT /note="Missing (in Ref. 2; AAA19024)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="Y -> D (in Ref. 2; AAA19024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 45398 MW; 45F59857C21940D2 CRC64;
MLSILLTLLL SKYALGHEVW FSETFPNESI ENWVQSTYNA EKQGEFKVEA GKSPVDPIED
LGLKTTQDAR FYGIARKISE PFSNRGKTMV LQFTVKFDKT VSCGGAYIKL LGSDIDPKKF
HGESPYKIMF GPDICGMATK KVHVIFNYKG KNHLIKKEIP CKDDLKTHLY TLIVNPNNKY
EVLVDNAKVE EGSLEDDWDM LPPKKIDDPN DKKPDDWVDE QFIDDPDDKK PDNWDQPKTI
PDMDAKKPDD WDDAMDGEWE RPQKDNPEYK GEWTPRRIDN PKYKGEWKPV QIDNPEYKHD
PELYVLNDIG YVGFDLWQVD SGSIFDNILI TDSPDFAKEE GERLWRKRYD AEVAKEQSSA
KDDKEEAEET KERKELPYDA KASDEPSGDH DEL
