CALR3_BOVIN
ID CALR3_BOVIN Reviewed; 384 AA.
AC Q2TBR8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Calreticulin-3;
DE AltName: Full=Calsperin;
DE Flags: Precursor;
GN Name=CALR3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: During spermatogenesis, may act as a lectin-independent
CC chaperone for specific client proteins such as ADAM3. CALR3 capacity
CC for calcium-binding may be absent or much lower than that of CALR.
CC Required for sperm fertility (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of an EIF2 complex at least composed of
CC CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
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; BC109750; AAI09751.1; -; mRNA.
DR RefSeq; NP_001033603.1; NM_001038514.2.
DR AlphaFoldDB; Q2TBR8; -.
DR SMR; Q2TBR8; -.
DR STRING; 9913.ENSBTAP00000013175; -.
DR PaxDb; Q2TBR8; -.
DR PRIDE; Q2TBR8; -.
DR GeneID; 508555; -.
DR KEGG; bta:508555; -.
DR CTD; 125972; -.
DR eggNOG; KOG0674; Eukaryota.
DR InParanoid; Q2TBR8; -.
DR OrthoDB; 822188at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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.
PE 2: Evidence at transcript level;
KW Chaperone; Differentiation; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Lectin; Metal-binding; Reference proteome; Repeat; Signal;
KW Spermatogenesis; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..384
FT /note="Calreticulin-3"
FT /id="PRO_0000282867"
FT REPEAT 191..202
FT /note="1-1"
FT REPEAT 209..220
FT /note="1-2"
FT REPEAT 222..231
FT /note="1-3"
FT REPEAT 235..246
FT /note="1-4"
FT REPEAT 250..260
FT /note="2-1"
FT REPEAT 264..272
FT /note="2-2"
FT REPEAT 274..284
FT /note="2-3"
FT REGION 20..197
FT /note="N-domain"
FT REGION 191..246
FT /note="4 X approximate repeats"
FT REGION 198..294
FT /note="P-domain"
FT REGION 250..284
FT /note="3 X approximate repeats"
FT REGION 295..384
FT /note="C-domain"
FT MOTIF 381..384
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
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 303
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..137
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 44512 MW; BAE01C8F353718C2 CRC64;
MAAARVPLWA ICVRRVALAT VYFQEEFLDG ERWRNRWVHS TNDSQFGHFR LSSGNFYGHK
EKDKGLQTTQ NSRFYAISAR FKPFSNKGKT LIIQYTVKHE QKMDCGGGYI KLFPADVDQK
NLNGKSQYYI MFGPDICGFD IKTVHVILHF KNQYHANKKS IRCKVDSFTH LYTLVLRPDL
TYEVKIDGQS IESGSIEYDW QLTSLKKMEK ASAEAEGWDQ AAKDKSQDWE KHFLDASASK
PSDWKGELDG DWQAAMLQKP PYQDGLKPEG IDKDVWLHQK MKNSYLTEYD LSEFENIGAV
GLELWQVRSG TIFDNFLITD DEEYAENFGK ATWGETKGPE KEMDAIQAKE EVKKAQEEDE
DDMLMGRFRG RENSFKGFHR RNEF
