ID GLU2B_HUMAN Reviewed; 528 AA. AC P14314; A8K318; Q96BU9; Q96D06; Q9P0W9; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 231. DE RecName: Full=Glucosidase 2 subunit beta; DE AltName: Full=80K-H protein {ECO:0000303|PubMed:2793184}; DE AltName: Full=Glucosidase II subunit beta; DE AltName: Full=Protein kinase C substrate 60.1 kDa protein heavy chain; DE Short=PKCSH; DE Flags: Precursor; GN Name=PRKCSH {ECO:0000303|PubMed:28375157, ECO:0000312|HGNC:HGNC:9411}; GN Synonyms=G19P1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RX PubMed=2793184; DOI=10.1016/0888-7543(89)90063-3; RA Sakai K., Masamichi H., Minoshima S., Kudoh J., Fukuyama R., Shimizu N.; RT "Isolation of cDNAs encoding a substrate for protein kinase C: nucleotide RT sequence and chromosomal mapping of the gene for a human 80K protein."; RL Genomics 5:309-315(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9043864; RA Ophoff R.A., Terwindt G.M., Vergouwe M.N., van Eijk R., Mohrenweiser H., RA Litt M., Hofker M.H., Haan J., Ferrari M.D., Frants R.R.; RT "A 3-Mb region for the familial hemiplegic migraine locus on 19p13.1-p13.2: RT exclusion of PRKCSH as a candidate gene."; RL Eur. J. Hum. Genet. 4:321-328(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PATHWAY, INTERACTION WITH RP GANAB, AND SUBCELLULAR LOCATION. RC TISSUE=Lymphocyte; RX PubMed=10929008; DOI=10.1093/glycob/10.8.815; RA Pelletier M.F., Marcil A., Sevigny G., Jakob C.A., Tessier D.C., Chevet E., RA Menard R., Bergeron J.J.M., Thomas D.Y.; RT "The heterodimeric structure of glucosidase II is required for its RT activity, solubility, and localization in vivo."; RL Glycobiology 10:815-827(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-528 (ISOFORM 1), AND VARIANT RP THR-291. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-528 (ISOFORM 2), AND VARIANT RP THR-291. RC TISSUE=Lung; 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 [8] RP PROTEIN SEQUENCE OF 15-21. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [9] RP INVOLVEMENT IN PCLD1. RX PubMed=12529853; DOI=10.1086/368295; RA Li A., Davila S., Furu L., Qian Q., Tian X., Kamath P.S., King B.F., RA Torres V.E., Somlo S.; RT "Mutations in PRKCSH cause isolated autosomal dominant polycystic liver RT disease."; RL Am. J. Hum. Genet. 72:691-703(2003). RN [10] RP INVOLVEMENT IN PCLD1. RX PubMed=12577059; DOI=10.1038/ng1104; RA Drenth J.P.H., te Morsche R.H.M., Smink R., Bonifacino J.S., RA Jansen J.B.M.J.; RT "Germline mutations in PRKCSH are associated with autosomal dominant RT polycystic liver disease."; RL Nat. Genet. 33:345-347(2003). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP PHOSPHORYLATION AT SER-24 AND SER-168. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted phosphoproteome."; RL Cell 161:1619-1632(2015). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [15] RP INVOLVEMENT IN PCLD1, AND VARIANTS PCLD1 18-LYS--LEU-528 DEL; RP 156-GLN--LEU-528 DEL; 198-TRP--LEU-528 DEL; 414-GLN--LEU-528 DEL AND RP 423-TYR--LEU-528 DEL. RX PubMed=28375157; DOI=10.1172/jci90129; RA Besse W., Dong K., Choi J., Punia S., Fedeles S.V., Choi M., RA Gallagher A.R., Huang E.B., Gulati A., Knight J., Mane S., Tahvanainen E., RA Tahvanainen P., Sanna-Cherchi S., Lifton R.P., Watnick T., Pei Y.P., RA Torres V.E., Somlo S.; RT "Isolated polycystic liver disease genes define effectors of polycystin-1 RT function."; RL J. Clin. Invest. 127:1772-1785(2017). 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:10929008). Required for efficient CC PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of CC the primary cilia (By similarity). {ECO:0000250|UniProtKB:O08795, CC ECO:0000269|PubMed:10929008}. CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism. CC {ECO:0000269|PubMed:10929008}. CC -!- SUBUNIT: Heterodimer of a catalytic alpha subunit (GANAB) and a beta CC subunit (PRKCSH) (PubMed:10929008). Binds glycosylated PTPRC (By CC similarity). {ECO:0000250|UniProtKB:O08795, CC ECO:0000269|PubMed:10929008}. CC -!- INTERACTION: CC P14314; Q14697-1: GANAB; NbExp=3; IntAct=EBI-716953, EBI-11614043; CC P14314; Q14697-2: GANAB; NbExp=2; IntAct=EBI-716953, EBI-16399534; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE- CC ProRule:PRU10138, ECO:0000305|PubMed:10929008}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P14314-1; Sequence=Displayed; CC Name=2; CC IsoId=P14314-2; Sequence=VSP_043749; CC -!- DISEASE: Polycystic liver disease 1 with or without kidney cysts CC (PCLD1) [MIM:174050]: An autosomal dominant hepatobiliary disease CC characterized by overgrowth of biliary epithelium and supportive CC connective tissue, resulting in multiple liver cysts. A subset of CC patients may develop kidney cysts that usually do not result in CC clinically significant renal disease. {ECO:0000269|PubMed:12529853, CC ECO:0000269|PubMed:12577059, ECO:0000269|PubMed:28375157}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAH15154.1; Type=Erroneous initiation; Evidence={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; J03075; AAA52493.1; -; mRNA. DR EMBL; U50326; AAA98668.1; -; Genomic_DNA. DR EMBL; U50317; AAA98668.1; JOINED; Genomic_DNA. DR EMBL; U50318; AAA98668.1; JOINED; Genomic_DNA. DR EMBL; U50319; AAA98668.1; JOINED; Genomic_DNA. DR EMBL; U50320; AAA98668.1; JOINED; Genomic_DNA. DR EMBL; U50321; AAA98668.1; JOINED; Genomic_DNA. DR EMBL; U50322; AAA98668.1; JOINED; Genomic_DNA. DR EMBL; U50323; AAA98668.1; JOINED; Genomic_DNA. DR EMBL; U50324; AAA98668.1; JOINED; Genomic_DNA. DR EMBL; U50325; AAA98668.1; JOINED; Genomic_DNA. DR EMBL; AF144075; AAF66686.1; -; mRNA. DR EMBL; BT009858; AAP88860.1; -; mRNA. DR EMBL; AK290433; BAF83122.1; -; mRNA. DR EMBL; AC008481; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC024575; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013586; AAH13586.2; -; mRNA. DR EMBL; BC015154; AAH15154.1; ALT_INIT; mRNA. DR CCDS; CCDS32911.1; -. [P14314-1] DR CCDS; CCDS45977.1; -. [P14314-2] DR PIR; A32469; A32469. DR RefSeq; NP_001001329.1; NM_001001329.2. [P14314-2] DR RefSeq; NP_001276031.1; NM_001289102.1. [P14314-2] DR RefSeq; NP_002734.2; NM_002743.3. [P14314-1] DR RefSeq; XP_011526433.1; XM_011528131.1. DR RefSeq; XP_011526434.1; XM_011528132.1. DR RefSeq; XP_016882466.1; XM_017026977.1. DR PDB; 8D43; EM; 2.88 A; B=1-528. DR PDB; 8EMR; EM; 2.92 A; B=1-528. DR PDBsum; 8D43; -. DR PDBsum; 8EMR; -. DR AlphaFoldDB; P14314; -. DR EMDB; EMD-27173; -. DR EMDB; EMD-28262; -. DR SMR; P14314; -. DR BioGRID; 111575; 240. DR ComplexPortal; CPX-6822; Glucosidase II complex. DR IntAct; P14314; 72. DR MINT; P14314; -. DR STRING; 9606.ENSP00000466134; -. DR GlyConnect; 1269; 8 N-Linked glycans (2 sites). DR GlyCosmos; P14314; 9 sites, 14 glycans. DR GlyGen; P14314; 14 sites, 8 N-linked glycans (2 sites), 7 O-linked glycans (10 sites). DR iPTMnet; P14314; -. DR MetOSite; P14314; -. DR PhosphoSitePlus; P14314; -. DR SwissPalm; P14314; -. DR BioMuta; PRKCSH; -. DR DMDM; 116242499; -. DR CPTAC; CPTAC-574; -. DR CPTAC; CPTAC-575; -. DR EPD; P14314; -. DR jPOST; P14314; -. DR MassIVE; P14314; -. DR MaxQB; P14314; -. DR PaxDb; 9606-ENSP00000466134; -. DR PeptideAtlas; P14314; -. DR ProteomicsDB; 53041; -. [P14314-1] DR ProteomicsDB; 53042; -. [P14314-2] DR Pumba; P14314; -. DR TopDownProteomics; P14314-1; -. [P14314-1] DR TopDownProteomics; P14314-2; -. [P14314-2] DR Antibodypedia; 3848; 356 antibodies from 33 providers. DR DNASU; 5589; -. DR Ensembl; ENST00000587327.5; ENSP00000466012.1; ENSG00000130175.10. [P14314-2] DR Ensembl; ENST00000589838.5; ENSP00000465461.1; ENSG00000130175.10. [P14314-1] DR Ensembl; ENST00000591462.6; ENSP00000465489.1; ENSG00000130175.10. [P14314-2] DR GeneID; 5589; -. DR KEGG; hsa:5589; -. DR UCSC; uc010dyb.5; human. [P14314-1] DR AGR; HGNC:9411; -. DR CTD; 5589; -. DR DisGeNET; 5589; -. DR GeneCards; PRKCSH; -. DR HGNC; HGNC:9411; PRKCSH. DR HPA; ENSG00000130175; Low tissue specificity. DR MalaCards; PRKCSH; -. DR MIM; 174050; phenotype. DR MIM; 177060; gene. DR neXtProt; NX_P14314; -. DR OpenTargets; ENSG00000130175; -. DR Orphanet; 2924; Isolated polycystic liver disease. DR PharmGKB; PA33774; -. DR VEuPathDB; HostDB:ENSG00000130175; -. DR eggNOG; KOG2397; Eukaryota. DR GeneTree; ENSGT00510000047770; -. DR HOGENOM; CLU_016834_1_0_1; -. DR InParanoid; P14314; -. DR OrthoDB; 103990at2759; -. DR PhylomeDB; P14314; -. DR TreeFam; TF329550; -. DR BioCyc; MetaCyc:HS05346-MONOMER; -. DR BRENDA; 3.2.1.207; 2681. DR PathwayCommons; P14314; -. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle. DR Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling. DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR Reactome; R-HSA-901042; Calnexin/calreticulin cycle. DR Reactome; R-HSA-9683686; Maturation of spike protein. DR Reactome; R-HSA-9694548; Maturation of spike protein. DR SignaLink; P14314; -. DR UniPathway; UPA00957; -. DR BioGRID-ORCS; 5589; 48 hits in 1158 CRISPR screens. DR ChiTaRS; PRKCSH; human. DR GeneWiki; PRKCSH; -. DR GenomeRNAi; 5589; -. DR Pharos; P14314; Tbio. DR PRO; PR:P14314; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P14314; Protein. DR Bgee; ENSG00000130175; Expressed in stromal cell of endometrium and 205 other cell types or tissues. DR ExpressionAtlas; P14314; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0017177; C:glucosidase II complex; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IMP:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB. DR GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB. DR GO; GO:0001889; P:liver development; IBA:GO_Central. DR GO; GO:0006491; P:N-glycan processing; IDA:UniProtKB. 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; 1. 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; P14314; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Direct protein sequencing; KW Disease variant; Disulfide bond; Endoplasmic reticulum; Glycoprotein; KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal. FT SIGNAL 1..14 FT /evidence="ECO:0000269|PubMed:12665801" FT CHAIN 15..528 FT /note="Glucosidase 2 subunit beta" FT /id="PRO_0000004143" FT DOMAIN 37..71 FT /note="LDL-receptor class A 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 72..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 413..514 FT /note="MRH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT REGION 234..266 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 281..357 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 525..528 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138, FT ECO:0000269|PubMed:10929008" FT COMPBIAS 309..338 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:0000250|UniProtKB:O08795" FT BINDING 50 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 53 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 53 FT /ligand="substrate" FT /ligand_note="ligand shared with catalytic subunit" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 55 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 57 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 63 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 64 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 91 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 94 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 96 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 98 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 104 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:O08795" FT BINDING 105 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:O08795" 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; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 89 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000255" FT MOD_RES 166 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:O08795" FT MOD_RES 168 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 383 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000255" FT MOD_RES 390 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000255" FT MOD_RES 434 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000255" FT CARBOHYD 72 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 476 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 39..58 FT /evidence="ECO:0000250|UniProtKB:O08795" FT DISULFID 56..70 FT /evidence="ECO:0000250|UniProtKB:O08795" FT DISULFID 77..99 FT /evidence="ECO:0000250|UniProtKB:O08795" FT DISULFID 97..112 FT /evidence="ECO:0000250|UniProtKB:O08795" FT DISULFID 100..116 FT /evidence="ECO:0000250|UniProtKB:O08795" FT DISULFID 415..428 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 471..500 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 485..512 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT VAR_SEQ 337..346 FT /note="EAPPPLSPPQ -> VQGEQPK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_043749" FT VARIANT 18..528 FT /note="Missing (in PCLD1)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080939" FT VARIANT 74 FT /note="S -> N (in dbSNP:rs10406672)" FT /id="VAR_028761" FT VARIANT 156..528 FT /note="Missing (in PCLD1)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080940" FT VARIANT 198..528 FT /note="Missing (in PCLD1)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080941" FT VARIANT 291 FT /note="A -> T (in dbSNP:rs11557488)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4" FT /id="VAR_028762" FT VARIANT 338 FT /note="A -> G (in dbSNP:rs35847588)" FT /id="VAR_048658" FT VARIANT 414..528 FT /note="Missing (in PCLD1)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080942" FT VARIANT 423..528 FT /note="Missing (in PCLD1)" FT /evidence="ECO:0000269|PubMed:28375157" FT /id="VAR_080943" FT CONFLICT 325 FT /note="Missing (in Ref. 1; AAA52493, 2; AAA98668, 4; FT AAP88860 and 6; AAH13586)" FT /evidence="ECO:0000305" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:8EMR" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:8EMR" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:8EMR" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:8EMR" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:8EMR" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:8EMR" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:8EMR" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:8EMR" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:8EMR" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:8EMR" FT TURN 104..108 FT /evidence="ECO:0007829|PDB:8EMR" SQ SEQUENCE 528 AA; 59425 MW; 8DAD9776037E878E CRC64; MLLPLLLLLP MCWAVEVKRP RGVSLTNHHF YDESKPFTCL DGSATIPFDQ VNDDYCDCKD GSDEPGTAAC PNGSFHCTNT GYKPLYIPSN RVNDGVCDCC DGTDEYNSGV ICENTCKEKG RKERESLQQM AEVTREGFRL KKILIEDWKK AREEKQKKLI ELQAGKKSLE DQVEMLRTVK EEAEKPEREA KEQHQKLWEE QLAAAKAQQE QELAADAFKE LDDDMDGTVS VTELQTHPEL DTDGDGALSE AEAQALLSGD TQTDATSFYD RVWAAIRDKY RSEALPTDLP APSAPDLTEP KEEQPPVPSS PTEEEEEEEE EEEEEAEEEE EEEDSEEAPP PLSPPQPASP AEEDKMPPYD EQTQAFIDAA QEARNKFEEA ERSLKDMEES IRNLEQEISF DFGPNGEFAY LYSQCYELTT NEYVYRLCPF KLVSQKPKLG GSPTSLGTWG SWIGPDHDKF SAMKYEQGTG CWQGPNRSTT VRLLCGKETM VTSTTEPSRC EYLMELMTPA ACPEPPPEAP TEDDHDEL //