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 24-JAN-2024, entry version 188. 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, RC Pancreas, 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}. 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; 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. 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; 12. DR IntAct; O08795; 1. DR STRING; 10090.ENSMUSP00000110987; -. DR GlyConnect; 2337; 2 N-Linked glycans (1 site). DR GlyCosmos; O08795; 2 sites, 2 glycans. DR GlyGen; O08795; 4 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (2 sites). 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; 10090-ENSMUSP00000110987; -. DR PeptideAtlas; O08795; -. DR ProteomicsDB; 271398; -. [O08795-1] DR ProteomicsDB; 271399; -. [O08795-2] DR Pumba; O08795; -. DR Antibodypedia; 3848; 356 antibodies from 33 providers. DR DNASU; 19089; -. DR Ensembl; ENSMUST00000003493.9; ENSMUSP00000003493.8; ENSMUSG00000003402.15. [O08795-1] DR Ensembl; ENSMUST00000115331.10; ENSMUSP00000110987.3; ENSMUSG00000003402.15. [O08795-2] DR Ensembl; ENSMUST00000216344.2; ENSMUSP00000149936.2; ENSMUSG00000003402.15. [O08795-1] DR GeneID; 19089; -. DR KEGG; mmu:19089; -. DR UCSC; uc009oni.2; mouse. [O08795-1] DR UCSC; uc009onk.2; mouse. [O08795-2] DR AGR; MGI:107877; -. 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; YENGQHC; -. DR OrthoDB; 103990at2759; -. 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; 14 hits in 78 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 274 other cell types or tissues. DR ExpressionAtlas; O08795; baseline and differential. 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; 1.10.238.10; EF-hand; 1. DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1. DR Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 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:SF1; GLUCOSIDASE 2 SUBUNIT BETA; 1. DR PANTHER; PTHR12630; N-LINKED OLIGOSACCHARIDE PROCESSING; 1. DR Pfam; PF13202; EF-hand_5; 2. DR Pfam; PF12999; PRKCSH-like; 1. DR Pfam; PF13015; PRKCSH_1; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF57424; LDL receptor-like module; 1. DR SUPFAM; SSF50911; Mannose 6-phosphate receptor domain; 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. DR Genevisible; O08795; MM. 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 //