ID CALR_RAT Reviewed; 416 AA. AC P18418; P10452; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 27-MAR-2024, entry version 211. DE RecName: Full=Calreticulin; DE AltName: Full=CALBP; DE AltName: Full=CRP55; DE AltName: Full=Calcium-binding protein 3; DE Short=CABP3; DE AltName: Full=Calregulin; DE AltName: Full=Endoplasmic reticulum resident protein 60; DE Short=ERp60; DE AltName: Full=HACBP; DE Flags: Precursor; GN Name=Calr; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Brain cortex; RX PubMed=2395661; DOI=10.1093/nar/18.16.4933; RA Murthy K.K., Banville D., Srikant C.B., Carrier F., Bell A., Holmes C., RA Patel Y.C.; RT "Structural homology between the rat calreticulin gene product and the RT Onchocerca volvulus antigen Ral-1."; RL Nucleic Acids Res. 18:4933-4933(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; RX PubMed=8453984; DOI=10.1006/excr.1993.1063; RA Nakamura M., Moriya M., Baba T., Michikawa Y., Yamanobe T., Arai K., RA Okinaga S., Kobayashi T.; RT "An endoplasmic reticulum protein, calreticulin, is transported into the RT acrosome of rat sperm."; RL Exp. Cell Res. 205:101-110(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX PubMed=7876339; DOI=10.1242/jcs.107.10.2705; RA Soennichsen B., Fuellekrug J., van Nguyen P., Diekmann W., Robinson D.G., RA Mieskes G.; RT "Retention and retrieval: both mechanisms cooperate to maintain RT calreticulin in the endoplasmic reticulum."; RL J. Cell Sci. 107:2705-2717(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 18-32. RC STRAIN=Sprague-Dawley; TISSUE=Testis; RX PubMed=1497655; DOI=10.1016/0006-291x(92)90798-p; RA Nakamura M., Michikawa Y., Baba T., Okinaga S., Arai K.; RT "Calreticulin is present in the acrosome of spermatids of rat testis."; RL Biochem. Biophys. Res. Commun. 186:668-673(1992). RN [6] RP PROTEIN SEQUENCE OF 18-32. RC STRAIN=LEC; TISSUE=Liver; RX PubMed=8251535; DOI=10.1016/0304-4165(93)90033-5; RA Yokoi T., Nagayama S., Kajiwara R., Kawaguchi Y., Horiuchi R., Kamataki T.; RT "Identification of protein disulfide isomerase and calreticulin as RT autoimmune antigens in LEC strain of rats."; RL Biochim. Biophys. Acta 1158:339-344(1993). RN [7] RP PROTEIN SEQUENCE OF 18-29. RX PubMed=2241926; DOI=10.1042/bj2710473; RA Treves S., de Mattei M., Lanfredi M., Villa A., Green N.M., Maclennan D.H., RA Meldolesi J., Pozzan T.; RT "Calreticulin is a candidate for a calsequestrin-like function in Ca2(+)- RT storage compartments (calciosomes) of liver and brain."; RL Biochem. J. 271:473-480(1990). RN [8] RP PROTEIN SEQUENCE OF 25-36; 88-98 AND 163-185, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; RA Lubec G., Afjehi-Sadat L., Diao W.; RL Submitted (APR-2007) to UniProtKB. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 269-361. RC STRAIN=Sprague-Dawley; RA Lone Y.-C., Bailly A., Latruffe N.; RL Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases. RN [10] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=12782144; DOI=10.1016/s0945-053x(02)00117-8; RA Somogyi E., Petersson U., Hultenby K., Wendel M.; RT "Calreticulin -- an endoplasmic reticulum protein with calcium-binding RT activity is also found in the extracellular matrix."; RL Matrix Biol. 22:179-191(2003). RN [11] RP INTERACTION WITH PDIA3. RX PubMed=11842220; DOI=10.1073/pnas.042699099; RA Frickel E.M., Riek R., Jelesarov I., Helenius A., Wuethrich K., RA Ellgaard L.; RT "TROSY-NMR reveals interaction between ERp57 and the tip of the RT calreticulin P-domain."; RL Proc. Natl. Acad. Sci. U.S.A. 99:1954-1959(2002). RN [12] RP STRUCTURE BY NMR OF 206-305. RX PubMed=11248044; DOI=10.1073/pnas.051630098; RA Ellgaard L., Riek R., Herrmann T., Guntert P., Braun D., Helenius A., RA Wuthrich K.; RT "NMR structure of the calreticulin P-domain."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3133-3138(2001). RN [13] RP STRUCTURE BY NMR OF 206-278. RX PubMed=12270713; DOI=10.1016/s0022-2836(02)00812-4; RA Ellgaard L., Bettendorff P., Braun D., Herrmann T., Fiorito F., RA Jelesarov I., Guntert P., Helenius A., Wuthrich K.; RT "NMR structures of 36 and 73-residue fragments of the calreticulin P- RT domain."; RL J. Mol. Biol. 322:773-784(2002). CC -!- FUNCTION: Calcium-binding chaperone that promotes folding, oligomeric CC assembly and quality control in the endoplasmic reticulum (ER) via the CC calreticulin/calnexin cycle. This lectin interacts transiently with CC almost all of the monoglucosylated glycoproteins that are synthesized CC in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates CC its nuclear export (By similarity). Involved in maternal gene CC expression regulation. May participate in oocyte maturation via the CC regulation of calcium homeostasis (By similarity). Present in the CC cortical granules of non-activated oocytes, is exocytosed during the CC cortical reaction in response to oocyte activation and might CC participate in the block to polyspermy (By similarity). CC {ECO:0000250|UniProtKB:P27797, ECO:0000250|UniProtKB:P28491, CC ECO:0000250|UniProtKB:Q8K3H7}. CC -!- SUBUNIT: Monomer. Component of an EIF2 complex at least composed of CC CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts CC with GABARAP, NR3C1 and TRIM21. Interacts with PPIB and SPACA9. CC Interacts (via P-domain) with PDIA5 (By similarity). Interacts with CC PDIA3/ERp57 (PubMed:11842220). Interacts with CLCC1 (By similarity). CC {ECO:0000250|UniProtKB:P14211, ECO:0000250|UniProtKB:P27797, CC ECO:0000269|PubMed:11842220}. CC -!- INTERACTION: CC P18418; P30101: PDIA3; Xeno; NbExp=2; IntAct=EBI-916742, EBI-979862; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000269|PubMed:12782144}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P27797}. Secreted, extracellular space, CC extracellular matrix {ECO:0000250|UniProtKB:P27797}. Cell surface CC {ECO:0000250|UniProtKB:P27797}. Sarcoplasmic reticulum lumen CC {ECO:0000250|UniProtKB:P28491}. Cytoplasmic vesicle, secretory vesicle, CC Cortical granule {ECO:0000250|UniProtKB:Q8K3H7}. Cytolytic granule CC {ECO:0000250|UniProtKB:P27797}. Note=Also found in cell surface (T CC cells), cytosol and extracellular matrix. During oocyte maturation and CC after parthenogenetic activation accumulates in cortical granules. In CC pronuclear and early cleaved embryos localizes weakly to cytoplasm CC around nucleus and more strongly in the region near the cortex (By CC similarity). In cortical granules of non-activated oocytes, is CC exocytosed during the cortical reaction in response to oocyte CC activation (By similarity). {ECO:0000250|UniProtKB:P27797, CC ECO:0000250|UniProtKB:P28491, ECO:0000250|UniProtKB:Q8K3H7}. CC -!- TISSUE SPECIFICITY: Predentin and odontoblast. CC {ECO:0000269|PubMed:12782144}. 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 -!- DOMAIN: Associates with PDIA3 through the tip of the extended arm CC formed by the P-domain. CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}. CC -!- CAUTION: Was originally (Ref.9) thought to be D-beta-hydroxybutyrate CC dehydrogenase. {ECO:0000305}. 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; X53363; CAA37446.1; -; mRNA. DR EMBL; D78308; BAA11345.1; -; mRNA. DR EMBL; X79327; CAA55890.1; -; mRNA. DR EMBL; BC062395; AAH62395.1; -; mRNA. DR EMBL; X13702; CAA31987.1; -; mRNA. DR PIR; JH0819; JH0819. DR RefSeq; NP_071794.1; NM_022399.2. DR PDB; 1HHN; NMR; -; A=206-305. DR PDB; 1K91; NMR; -; A=238-273. DR PDB; 1K9C; NMR; -; A=206-278. DR PDBsum; 1HHN; -. DR PDBsum; 1K91; -. DR PDBsum; 1K9C; -. DR AlphaFoldDB; P18418; -. DR BMRB; P18418; -. DR SMR; P18418; -. DR BioGRID; 249008; 5. DR CORUM; P18418; -. DR IntAct; P18418; 9. DR MINT; P18418; -. DR STRING; 10116.ENSRNOP00000004091; -. DR iPTMnet; P18418; -. DR PhosphoSitePlus; P18418; -. DR SwissPalm; P18418; -. DR jPOST; P18418; -. DR PaxDb; 10116-ENSRNOP00000004091; -. DR Ensembl; ENSRNOT00000113427.1; ENSRNOP00000080548.1; ENSRNOG00000003029.7. DR Ensembl; ENSRNOT00055012941; ENSRNOP00055010325; ENSRNOG00055007731. DR Ensembl; ENSRNOT00060021445; ENSRNOP00060016944; ENSRNOG00060012624. DR Ensembl; ENSRNOT00065016763; ENSRNOP00065012805; ENSRNOG00065010365. DR GeneID; 64202; -. DR KEGG; rno:64202; -. DR AGR; RGD:620288; -. DR CTD; 811; -. DR RGD; 620288; Calr. DR eggNOG; KOG0674; Eukaryota. DR GeneTree; ENSGT00950000182915; -. DR HOGENOM; CLU_018224_0_2_1; -. DR InParanoid; P18418; -. DR OMA; NWVYSEH; -. DR OrthoDB; 5489154at2759; -. DR PhylomeDB; P18418; -. DR TreeFam; TF338438; -. DR Reactome; R-RNO-1236974; ER-Phagosome pathway. DR Reactome; R-RNO-3000480; Scavenging by Class A Receptors. DR Reactome; R-RNO-901042; Calnexin/calreticulin cycle. DR Reactome; R-RNO-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR EvolutionaryTrace; P18418; -. DR PRO; PR:P18418; -. DR Proteomes; UP000002494; Chromosome 19. DR Bgee; ENSRNOG00000003029; Expressed in ovary and 20 other cell types or tissues. DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD. DR GO; GO:0009986; C:cell surface; IDA:RGD. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD. DR GO; GO:0060473; C:cortical granule; ISS:UniProtKB. DR GO; GO:0044194; C:cytolytic granule; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:RGD. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; ISO:RGD. DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD. DR GO; GO:0005615; C:extracellular space; IDA:RGD. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0042824; C:MHC class I peptide loading complex; ISO:RGD. DR GO; GO:0005635; C:nuclear envelope; IDA:RGD. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD. DR GO; GO:0005844; C:polysome; ISO:RGD. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0005840; C:ribosome; IEA:Ensembl. DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD. DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IDA:RGD. DR GO; GO:0030246; F:carbohydrate binding; ISO:RGD. DR GO; GO:0001849; F:complement component C1q complex binding; ISO:RGD. DR GO; GO:0042562; F:hormone binding; IPI:RGD. DR GO; GO:0005178; F:integrin binding; ISO:RGD. DR GO; GO:0005506; F:iron ion binding; IDA:RGD. DR GO; GO:0140313; F:molecular sequestering activity; IEA:Ensembl. DR GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL. DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:RGD. DR GO; GO:0005049; F:nuclear export signal receptor activity; ISO:RGD. DR GO; GO:0042277; F:peptide binding; IDA:RGD. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. DR GO; GO:0055007; P:cardiac muscle cell differentiation; IEP:RGD. DR GO; GO:0071257; P:cellular response to electrical stimulus; IEP:RGD. DR GO; GO:0071285; P:cellular response to lithium ion; IEP:RGD. DR GO; GO:0071310; P:cellular response to organic substance; IEP:RGD. DR GO; GO:0098586; P:cellular response to virus; IEP:RGD. DR GO; GO:0090398; P:cellular senescence; ISO:RGD. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:RGD. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; ISO:RGD. DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD. DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; ISO:RGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0017148; P:negative regulation of translation; ISO:RGD. DR GO; GO:1901164; P:negative regulation of trophoblast cell migration; ISO:RGD. DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; ISO:RGD. DR GO; GO:0045787; P:positive regulation of cell cycle; ISO:RGD. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD. DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; ISO:RGD. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; ISO:RGD. DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD. DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:RGD. DR GO; GO:0006611; P:protein export from nucleus; ISO:RGD. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD. DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB. DR GO; GO:0040020; P:regulation of meiotic nuclear division; ISO:RGD. DR GO; GO:0032355; P:response to estradiol; IEP:RGD. DR GO; GO:1903416; P:response to glycoside; IEP:RGD. DR GO; GO:0010033; P:response to organic substance; IEP:RGD. DR GO; GO:0033574; P:response to testosterone; IEP:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0007283; P:spermatogenesis; IEP:RGD. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.10.250.10; Calreticulin/calnexin, P domain; 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:SF16; CALRETICULIN; 1. DR PANTHER; PTHR11073; CALRETICULIN AND CALNEXIN; 1. DR Pfam; PF00262; Calreticulin; 2. DR PIRSF; PIRSF002356; Calreticulin; 1. DR PRINTS; PR00626; CALRETICULIN. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF63887; P-domain of calnexin/calreticulin; 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. DR World-2DPAGE; 0004:P18418; -. DR Genevisible; P18418; RN. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Calcium; Chaperone; Cytoplasm; KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; KW Endoplasmic reticulum; Extracellular matrix; Hydroxylation; Lectin; KW Lysosome; Metal-binding; Reference proteome; Repeat; KW Sarcoplasmic reticulum; Secreted; Signal; Zinc. FT SIGNAL 1..17 FT /evidence="ECO:0000269|PubMed:1497655, FT ECO:0000269|PubMed:2241926, ECO:0000269|PubMed:8251535" FT CHAIN 18..416 FT /note="Calreticulin" FT /id="PRO_0000004177" FT REPEAT 191..202 FT /note="1-1" FT REPEAT 210..221 FT /note="1-2" FT REPEAT 227..238 FT /note="1-3" FT REPEAT 244..255 FT /note="1-4" FT REPEAT 259..269 FT /note="2-1" FT REPEAT 273..283 FT /note="2-2" FT REPEAT 287..297 FT /note="2-3" FT REGION 18..197 FT /note="N-domain" FT REGION 191..255 FT /note="4 X approximate repeats" FT REGION 193..278 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 198..308 FT /note="P-domain" FT REGION 237..270 FT /note="Interaction with PPIB" FT /evidence="ECO:0000250" FT REGION 259..297 FT /note="3 X approximate repeats" FT REGION 309..416 FT /note="C-domain" FT REGION 350..416 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 413..416 FT /note="Prevents secretion from ER" FT COMPBIAS 199..254 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 352..381 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 382..416 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 26 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 62 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 64 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" 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 BINDING 328 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT MOD_RES 48 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P27797" FT MOD_RES 64 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P27797" FT MOD_RES 159 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P27797" FT MOD_RES 209 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P27797" FT DISULFID 105..137 FT /evidence="ECO:0000250" FT CONFLICT 269 FT /note="P -> R (in Ref. 9; CAA31987)" FT /evidence="ECO:0000305" FT CONFLICT 359..361 FT /note="DKQ -> AAG (in Ref. 9; CAA31987)" FT /evidence="ECO:0000305" FT TURN 220..222 FT /evidence="ECO:0007829|PDB:1K9C" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:1HHN" FT TURN 234..236 FT /evidence="ECO:0007829|PDB:1K9C" FT STRAND 240..243 FT /evidence="ECO:0007829|PDB:1HHN" FT HELIX 255..258 FT /evidence="ECO:0007829|PDB:1HHN" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:1HHN" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:1HHN" SQ SEQUENCE 416 AA; 47995 MW; 2E6713CED31A2970 CRC64; MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV LSSGKFYGDQ EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPGGLDQK DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDAAKPEDWD ERAKIDDPTD SKPEDWDKPE HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK QDEEQRLKEE EEDKKRKEEE EAEDKEDEDD RDEDEDEEDE KEEDEEDATG QAKDEL //