CALR_RAT
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 03-AUG-2022, entry version 202.
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}.
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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; 8.
DR MINT; P18418; -.
DR STRING; 10116.ENSRNOP00000004091; -.
DR UniLectin; P18418; -.
DR iPTMnet; P18418; -.
DR PhosphoSitePlus; P18418; -.
DR SwissPalm; P18418; -.
DR World-2DPAGE; 0004:P18418; -.
DR jPOST; P18418; -.
DR PaxDb; P18418; -.
DR PRIDE; P18418; -.
DR Ensembl; ENSRNOT00000113427; ENSRNOP00000080548; ENSRNOG00000003029.
DR GeneID; 64202; -.
DR KEGG; rno:64202; -.
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; MMWCKTV; -.
DR OrthoDB; 822188at2759; -.
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 tissues.
DR Genevisible; P18418; RN.
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; IDA: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:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; 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; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005844; C:polysome; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
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: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:0003729; F:mRNA binding; IDA:BHF-UCL.
DR GO; GO:0050681; F:nuclear androgen receptor binding; 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: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:0045892; P:negative regulation of transcription, DNA-templated; 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 NIK/NF-kappaB signaling; 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; 2.10.250.10; -; 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 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
