CALR_ONCVO
ID CALR_ONCVO Reviewed; 388 AA.
AC P11012;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Calreticulin;
DE AltName: Full=41 kDa larval antigen;
DE AltName: Full=Protein ral-1;
DE AltName: Full=RAL1 antigen;
DE Flags: Precursor;
GN Name=crt-1; Synonyms=ral-1;
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7520419; DOI=10.1128/iai.62.9.3696-3704.1994;
RA Rokeach L.A., Zimmerman P.A., Unnasch T.R.;
RT "Epitopes of the Onchocerca volvulus RAL1 antigen, a member of the
RT calreticulin family of proteins, recognized by sera from patients with
RT onchocerciasis.";
RL Infect. Immun. 62:3696-3704(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-388.
RX PubMed=2455736; DOI=10.1172/jci113581;
RA Unnasch T.R., Gallin M.Y., Soboslay P.T., Erttmann K.D., Greene B.M.;
RT "Isolation and characterization of expression cDNA clones encoding antigens
RT of Onchocerca volvulus infective larvae.";
RL J. Clin. Invest. 82:262-269(1988).
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 -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR EMBL; M20565; AAA59056.1; -; mRNA.
DR PIR; A32507; A32507.
DR AlphaFoldDB; P11012; -.
DR SMR; P11012; -.
DR STRING; 6282.P11012; -.
DR HOGENOM; CLU_328267_0_0_1; -.
DR Proteomes; UP000024404; 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.
PE 2: Evidence at transcript level;
KW Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; Lectin;
KW Metal-binding; Reference proteome; Repeat; Signal; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..388
FT /note="Calreticulin"
FT /id="PRO_0000004196"
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 approximate repeats"
FT REGION 193..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..295
FT /note="3 X approximate repeats"
FT REGION 349..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..388
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 DISULFID 103..135
FT /evidence="ECO:0000250"
SQ SEQUENCE 388 AA; 45298 MW; 9537F298A2D31CD6 CRC64;
MQLSLLVGLV CFSAINAKIY FKEDFSDDDW EKRWIKSKHK DDFGKWEISH GKFYGDAVKD
KGLKTTQDAK FYSIGAKFDK SFSNKGKSLV IQFSVKHEQD IDCGGGYVKL MASDVNLEDS
HGETPYHIMF GPDICGPGTK KVHVIFHYKD RNHMIKKDIR CKDDVFTHLY TLIVNSDNTY
EVQIDGEKAE SGELEADWDF LPPKKIKDPD AKKPEDWDER EFIDDEDDKK PEDWDKPEHI
PDPDAKKPED WDDEMDGEWE PPMVDNPEYK GEWKPKQKKN PAYKGKWIHP EIEIPDYTPD
DNLYVYDDIG AIGFDLWQVK SGTIFDDVIV TDSVEEAKKF GEKTLKITRE GEKKKGKKTK
KQKKKEKNEK IKKEKMKKRK RANRKKKK
