GLU2B_HUMAN
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 03-AUG-2022, entry version 222.
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};
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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. [P14314-1]
DR RefSeq; XP_011526434.1; XM_011528132.1. [P14314-2]
DR RefSeq; XP_016882466.1; XM_017026977.1.
DR AlphaFoldDB; P14314; -.
DR SMR; P14314; -.
DR BioGRID; 111575; 187.
DR ComplexPortal; CPX-6822; Glucosidase II complex.
DR IntAct; P14314; 66.
DR MINT; P14314; -.
DR STRING; 9606.ENSP00000466134; -.
DR GlyConnect; 1269; 8 N-Linked glycans (2 sites).
DR GlyGen; P14314; 11 sites, 8 N-linked glycans (2 sites), 6 O-linked glycans (7 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; P14314; -.
DR PeptideAtlas; P14314; -.
DR PRIDE; P14314; -.
DR ProteomicsDB; 53041; -. [P14314-1]
DR ProteomicsDB; 53042; -. [P14314-2]
DR TopDownProteomics; P14314-1; -. [P14314-1]
DR TopDownProteomics; P14314-2; -. [P14314-2]
DR Antibodypedia; 3848; 316 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 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 PhylomeDB; P14314; -.
DR TreeFam; TF329550; -.
DR BioCyc; MetaCyc:HS05346-MON; -.
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; 42 hits in 1078 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 203 other tissues.
DR ExpressionAtlas; P14314; baseline and differential.
DR Genevisible; P14314; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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 CDD; cd00112; LDLa; 1.
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; IPR002172; LDrepeatLR_classA_rpt.
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 Alternative splicing; Calcium; Direct protein sequencing; Disease variant;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Metal-binding;
KW 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"
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
