ID   GLU2B_BOVIN             Reviewed;         533 AA.
AC   Q28034; A7E3R7; Q3SX37;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=Glucosidase 2 subunit beta;
DE   AltName: Full=80K-H protein;
DE   AltName: Full=Glucosidase II subunit beta;
DE   AltName: Full=Protein kinase C substrate 60.1 kDa protein heavy chain;
DE            Short=PKCSH;
DE   AltName: Full=Vacuolar system-associated protein 60 {ECO:0000303|PubMed:10684806};
DE            Short=VASAP-60 {ECO:0000303|Ref.2};
DE   Flags: Precursor;
GN   Name=PRKCSH;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Holstein; TISSUE=Corpus luteum;
RX   PubMed=10684806; DOI=10.1095/biolreprod62.3.642;
RA   Brule S., Rabahi F., Faure R., Beckers J.-F.M.P., Silversides D.W.,
RA   Lussier J.G.;
RT   "Vacuolar system-associated protein-60: a protein characterized from bovine
RT   granulosa and luteal cells that is associated with intracellular vesicles
RT   and related to human 80K-H and murine beta-glucosidase II.";
RL   Biol. Reprod. 62:642-654(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Brule S., Silversides D., Lussier J.G.;
RT   "Bos taurus vacuolar system associated protein-60 (VASAP-60) promotor and
RT   complete gene sequences.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Required for efficient PKD1/Polycystin-1
CC       biogenesis and trafficking to the plasma membrane of the primary cilia
CC       (By similarity). {ECO:0000250|UniProtKB:O08795,
CC       ECO:0000250|UniProtKB:P14314}.
CC   -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC       {ECO:0000250|UniProtKB:O08795}.
CC   -!- SUBUNIT: Heterodimer of a catalytic alpha subunit (GANAB) and a beta
CC       subunit (PRKCSH). Binds glycosylated PTPRC.
CC       {ECO:0000250|UniProtKB:O08795}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in liver, spleen,
CC       lung, duodenum, stomach, adrenal gland, pituitary, testis, corpus
CC       luteum, uterus and fetal ovary. {ECO:0000269|PubMed:10684806}.
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DR   EMBL; U49178; AAA92060.1; -; mRNA.
DR   EMBL; AF299077; AAQ14482.1; -; Genomic_DNA.
DR   EMBL; BT030688; ABS45004.1; -; mRNA.
DR   EMBL; BC104524; AAI04525.1; -; mRNA.
DR   RefSeq; NP_788835.1; NM_176662.1.
DR   RefSeq; XP_005208774.1; XM_005208717.1.
DR   AlphaFoldDB; Q28034; -.
DR   SMR; Q28034; -.
DR   STRING; 9913.ENSBTAP00000072069; -.
DR   GlyCosmos; Q28034; 2 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000010787; -.
DR   PeptideAtlas; Q28034; -.
DR   Ensembl; ENSBTAT00000010787.4; ENSBTAP00000010787.3; ENSBTAG00000008202.4.
DR   GeneID; 338067; -.
DR   KEGG; bta:338067; -.
DR   CTD; 5589; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008202; -.
DR   VGNC; VGNC:33335; PRKCSH.
DR   eggNOG; KOG2397; Eukaryota.
DR   GeneTree; ENSGT00510000047770; -.
DR   HOGENOM; CLU_016834_1_0_1; -.
DR   InParanoid; Q28034; -.
DR   TreeFam; TF329550; -.
DR   Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR   UniPathway; UPA00957; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000008202; Expressed in dorsal thalamus and 105 other cell types or tissues.
DR   ExpressionAtlas; Q28034; baseline and differential.
DR   GO; GO:0017177; C:glucosidase II complex; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0001889; P:liver development; IBA:GO_Central.
DR   GO; GO:0006491; P:N-glycan processing; ISS:UniProtKB.
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; 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; 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.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW   Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..13
FT                   /evidence="ECO:0000250|UniProtKB:P14314"
FT   CHAIN           14..533
FT                   /note="Glucosidase 2 subunit beta"
FT                   /id="PRO_0000004142"
FT   DOMAIN          36..70
FT                   /note="LDL-receptor class A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          71..112
FT                   /note="LDL-receptor class A 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          208..243
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          244..279
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          418..519
FT                   /note="MRH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   REGION          284..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           530..533
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        286..307
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..337
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with catalytic subunit"
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   BINDING         52
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with catalytic subunit"
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   BINDING         54
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   BINDING         62
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         93
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   BINDING         95
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   BINDING         97
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   BINDING         103
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         221
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         223
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         225
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         232
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14314"
FT   MOD_RES         88
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         165
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14314"
FT   MOD_RES         388
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         395
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         439
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        38..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        55..69
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   DISULFID        76..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        96..111
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   DISULFID        99..115
FT                   /evidence="ECO:0000250|UniProtKB:O08795"
FT   DISULFID        420..433
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        476..505
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        490..517
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ   SEQUENCE   533 AA;  60151 MW;  50785B677FB81E01 CRC64;
     MLLLLLLLPM CWAVEVRRPR GVSLTNHHFY DESKPFTCLD GSASIPFDQV NDDYCDCKDG
     SDEPGTAACP NGSFHCTNTG YKALYISSRW VNDGVCDCCD GTDEYNSGIV CENTCKEKGR
     KERETLQQMA EVTREGFRLK KILIEDWKKA REEKQKKLIE LQAGKKSLED QVEVLRTLKE
     EAEKPEEAAK DQHRRLWEEQ QAISKEQRER ELAASAFQEL DDDMDGAVSV AELQTHPELD
     TDGDGALSEG EAQTLLGGDA QMDAAFFYDR VWAAIRDKYR SEVLPTEYPP SPPAPDVMEP
     KEEQPPMPSP PTEEEDEDEE DEETEEDEDE EDEDSQGEQP KDAPPPAPAP QTASPTEEDR
     MPPYDEQTQA FINAAQEARN KFEEAERSLK DMEESIRNLE QEISFDFGPN GEFAYLYSQC
     YELTTNEYVY RLCPFKLVSQ KPKLGGSPTS LGTWGSWAGP DHDKFSAMKY EQGTGCWQGP
     NRSTTVRLLC GKETVVTSTT EPSRCEYLME LMTPAACPEP PPEYPVEGDH DEL
//