GLU2B_MOUSE
ID GLU2B_MOUSE Reviewed; 521 AA.
AC O08795; Q921X2;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Glucosidase 2 subunit beta;
DE AltName: Full=80K-H protein;
DE AltName: Full=Glucosidase II subunit beta {ECO:0000303|PubMed:9148925};
DE AltName: Full=Protein kinase C substrate 60.1 kDa protein heavy chain;
DE Short=PKCSH;
DE Flags: Precursor;
GN Name=Prkcsh {ECO:0000312|MGI:MGI:107877};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 15-49 AND
RP 462-466, FUNCTION, AND INTERACTION WITH GANAB AND PTPRC.
RC TISSUE=T-cell lymphoma;
RX PubMed=9148925; DOI=10.1074/jbc.272.20.13117;
RA Arendt C.W., Ostergaard H.L.;
RT "Identification of the CD45-associated 116-kDa and 80-kDa proteins as the
RT alpha- and beta-subunits of alpha-glucosidase II.";
RL J. Biol. Chem. 272:13117-13125(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=21685914; DOI=10.1038/ng.860;
RA Fedeles S.V., Tian X., Gallagher A.R., Mitobe M., Nishio S., Lee S.H.,
RA Cai Y., Geng L., Crews C.M., Somlo S.;
RT "A genetic interaction network of five genes for human polycystic kidney
RT and liver diseases defines polycystin-1 as the central determinant of cyst
RT formation.";
RL Nat. Genet. 43:639-647(2011).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-166, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6] {ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O, ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR, ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE, ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 30-117 IN COMPLEX WITH CALCIUM
RP AND D-GLUCAL, FUNCTION, PATHWAY, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=27462106; DOI=10.1073/pnas.1604463113;
RA Caputo A.T., Alonzi D.S., Marti L., Reca I.B., Kiappes J.L., Struwe W.B.,
RA Cross A., Basu S., Lowe E.D., Darlot B., Santino A., Roversi P.,
RA Zitzmann N.;
RT "Structures of mammalian ER alpha-glucosidase II capture the binding modes
RT of broad-spectrum iminosugar antivirals.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E4630-E4638(2016).
CC -!- FUNCTION: Regulatory subunit of glucosidase II that cleaves
CC sequentially the 2 innermost alpha-1,3-linked glucose residues from the
CC Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature
CC glycoproteins (PubMed:27462106, PubMed:9148925). Required for efficient
CC PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of
CC the primary cilia (PubMed:21685914). {ECO:0000269|PubMed:21685914,
CC ECO:0000269|PubMed:27462106, ECO:0000269|PubMed:9148925}.
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC {ECO:0000269|PubMed:27462106}.
CC -!- SUBUNIT: Heterodimer of a catalytic alpha subunit (GANAB) and a beta
CC subunit (PRKCSH) (PubMed:9148925, PubMed:27462106). Binds glycosylated
CC PTPRC (PubMed:9148925). {ECO:0000269|PubMed:27462106,
CC ECO:0000269|PubMed:9148925}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O08795-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O08795-2; Sequence=VSP_010672;
CC -!- TISSUE SPECIFICITY: Expressed in kidney (at protein level).
CC {ECO:0000269|PubMed:21685914}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice exhibit early embryonic lethality
CC by 11.5 dpc. Conditional ubiquitous or kidney-specific knockdown
CC results in polycystic liver and kidney phenotypes, respectively.
CC {ECO:0000269|PubMed:21685914}.
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DR EMBL; U92794; AAC53183.1; -; mRNA.
DR EMBL; BC009816; AAH09816.1; -; mRNA.
DR CCDS; CCDS22918.1; -. [O08795-1]
DR CCDS; CCDS80967.1; -. [O08795-2]
DR RefSeq; NP_001280579.1; NM_001293650.1. [O08795-2]
DR RefSeq; NP_001280580.1; NM_001293651.1. [O08795-1]
DR RefSeq; NP_032951.1; NM_008925.2. [O08795-1]
DR RefSeq; XP_006510158.1; XM_006510095.3. [O08795-2]
DR RefSeq; XP_006510159.1; XM_006510096.2. [O08795-2]
DR PDB; 5F0E; X-ray; 1.74 A; B=30-117.
DR PDB; 5H9O; X-ray; 2.37 A; B/D=30-117.
DR PDB; 5HJO; X-ray; 2.29 A; B/D=35-117.
DR PDB; 5HJR; X-ray; 2.40 A; B/D=35-117.
DR PDB; 5IED; X-ray; 1.81 A; B=30-117.
DR PDB; 5IEE; X-ray; 1.92 A; B=30-117.
DR PDB; 5IEF; X-ray; 2.38 A; B=30-117.
DR PDB; 5IEG; X-ray; 1.82 A; B=30-117.
DR PDB; 7JTY; X-ray; 2.21 A; B/D=15-517.
DR PDB; 7K9N; X-ray; 2.07 A; B/D=15-517.
DR PDB; 7K9O; X-ray; 2.30 A; B/D=15-517.
DR PDB; 7K9Q; X-ray; 2.30 A; B/D=15-517.
DR PDB; 7K9T; X-ray; 2.10 A; B/D=15-517.
DR PDB; 7KAD; X-ray; 2.51 A; B/D=15-517.
DR PDB; 7KB6; X-ray; 2.20 A; B/D=15-517.
DR PDB; 7KB8; X-ray; 2.38 A; B/D=15-517.
DR PDB; 7KBJ; X-ray; 2.21 A; B/D=15-117.
DR PDB; 7KBR; X-ray; 2.09 A; B/D=15-117.
DR PDB; 7KRY; X-ray; 2.55 A; B/D=15-517.
DR PDB; 7L9E; X-ray; 2.29 A; B/D=15-117.
DR PDBsum; 5F0E; -.
DR PDBsum; 5H9O; -.
DR PDBsum; 5HJO; -.
DR PDBsum; 5HJR; -.
DR PDBsum; 5IED; -.
DR PDBsum; 5IEE; -.
DR PDBsum; 5IEF; -.
DR PDBsum; 5IEG; -.
DR PDBsum; 7JTY; -.
DR PDBsum; 7K9N; -.
DR PDBsum; 7K9O; -.
DR PDBsum; 7K9Q; -.
DR PDBsum; 7K9T; -.
DR PDBsum; 7KAD; -.
DR PDBsum; 7KB6; -.
DR PDBsum; 7KB8; -.
DR PDBsum; 7KBJ; -.
DR PDBsum; 7KBR; -.
DR PDBsum; 7KRY; -.
DR PDBsum; 7L9E; -.
DR AlphaFoldDB; O08795; -.
DR SMR; O08795; -.
DR BioGRID; 202370; 11.
DR IntAct; O08795; 1.
DR STRING; 10090.ENSMUSP00000110987; -.
DR GlyConnect; 2337; 2 N-Linked glycans (1 site).
DR GlyGen; O08795; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; O08795; -.
DR PhosphoSitePlus; O08795; -.
DR SwissPalm; O08795; -.
DR CPTAC; non-CPTAC-3580; -.
DR EPD; O08795; -.
DR jPOST; O08795; -.
DR MaxQB; O08795; -.
DR PaxDb; O08795; -.
DR PeptideAtlas; O08795; -.
DR PRIDE; O08795; -.
DR ProteomicsDB; 271398; -. [O08795-1]
DR ProteomicsDB; 271399; -. [O08795-2]
DR Antibodypedia; 3848; 316 antibodies from 33 providers.
DR DNASU; 19089; -.
DR Ensembl; ENSMUST00000003493; ENSMUSP00000003493; ENSMUSG00000003402. [O08795-1]
DR Ensembl; ENSMUST00000115331; ENSMUSP00000110987; ENSMUSG00000003402. [O08795-2]
DR Ensembl; ENSMUST00000216344; ENSMUSP00000149936; ENSMUSG00000003402. [O08795-1]
DR GeneID; 19089; -.
DR KEGG; mmu:19089; -.
DR UCSC; uc009oni.2; mouse. [O08795-1]
DR UCSC; uc009onk.2; mouse. [O08795-2]
DR CTD; 5589; -.
DR MGI; MGI:107877; Prkcsh.
DR VEuPathDB; HostDB:ENSMUSG00000003402; -.
DR eggNOG; KOG2397; Eukaryota.
DR GeneTree; ENSGT00510000047770; -.
DR HOGENOM; CLU_016834_1_0_1; -.
DR InParanoid; O08795; -.
DR OMA; KCVYRME; -.
DR OrthoDB; 632472at2759; -.
DR PhylomeDB; O08795; -.
DR TreeFam; TF329550; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR UniPathway; UPA00957; -.
DR BioGRID-ORCS; 19089; 12 hits in 73 CRISPR screens.
DR ChiTaRS; Prkcsh; mouse.
DR PRO; PR:O08795; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O08795; protein.
DR Bgee; ENSMUSG00000003402; Expressed in choroid plexus of fourth ventricle and 270 other tissues.
DR ExpressionAtlas; O08795; baseline and differential.
DR Genevisible; O08795; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0017177; C:glucosidase II complex; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001889; P:liver development; IGI:MGI.
DR GO; GO:0006491; P:N-glycan processing; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:MGI.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IGI:MGI.
DR Gene3D; 2.70.130.10; -; 1.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR039794; Gtb1-like.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR036607; PRKCSH.
DR InterPro; IPR028146; PRKCSH_N.
DR PANTHER; PTHR12630; PTHR12630; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF12999; PRKCSH-like; 1.
DR Pfam; PF13015; PRKCSH_1; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR SUPFAM; SSF57424; SSF57424; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51914; MRH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000269|PubMed:9148925"
FT CHAIN 15..521
FT /note="Glucosidase 2 subunit beta"
FT /id="PRO_0000004144"
FT DOMAIN 37..71
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 69..113
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 209..244
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 245..290
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 406..507
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 226..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 518..521
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 306..332
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49
FT /ligand="substrate"
FT /ligand_note="ligand shared with catalytic subunit"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5HJO"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 53
FT /ligand="substrate"
FT /ligand_note="ligand shared with catalytic subunit"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5HJO"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14314"
FT MOD_RES 89
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 166
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14314"
FT MOD_RES 376
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 383
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 427
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..58
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT DISULFID 56..70
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT DISULFID 77..99
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT DISULFID 97..112
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT DISULFID 100..116
FT /evidence="ECO:0000269|PubMed:27462106,
FT ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O,
FT ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR,
FT ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE,
FT ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG"
FT DISULFID 408..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 464..493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 478..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT VAR_SEQ 329
FT /note="E -> EVQGEQPK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010672"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:7K9T"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:7K9T"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:5F0E"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5F0E"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:5F0E"
SQ SEQUENCE 521 AA; 58793 MW; BD070319898B4A38 CRC64;
MLLLLLLLLP LCWAVEVKRP RGVSLSNHHF YEESKPFTCL DGTATIPFDQ VNDDYCDCKD
GSDEPGTAAC PNGSFHCTNT GYKPLYILSS RVNDGVCDCC DGTDEYNSGT VCENTCREKG
RKEKESLQQL AEVTREGFRL KKILIEEWKT AREEKQSKLL ELQAGKKSLE DQVETLRAAK
EEAERPEKEA KDQHRKLWEE QQAAAKARRE QERAASAFQE LDDNMDGMVS LAELQTHPEL
DTDGDGALSE EEAQALLSGD TQTDTTSFYD RVWAAIRDKY RSEVPPTDIP VPEETEPKEE
KPPVLPPTEE EEEEEEEPEE EEEEEEEEEE APPPLQPPQP PSPTEDEKMP PYDEETQAII
DAAQEARSKF EEVERSLKEM EESIRSLEQE ISFDFGPSGE FAYLYSQCYE LTTNEYVYRL
CPFKLVSQKP KHGGSPTSLG TWGSWAGPDH DKFSAMKYEQ GTGCWQGPNR STTVRLLCGK
ETVVTSTTEP SRCEYLMELM TPAACPEPPP EAPSDGDHDE L
