GLU2B_BOVIN
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 03-AUG-2022, entry version 148.
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.ENSBTAP00000010787; -.
DR PaxDb; Q28034; -.
DR PeptideAtlas; Q28034; -.
DR PRIDE; Q28034; -.
DR Ensembl; ENSBTAT00000010787; ENSBTAP00000010787; ENSBTAG00000008202.
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 OrthoDB; 632472at2759; -.
DR TreeFam; TF329550; -.
DR UniPathway; UPA00957; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000008202; Expressed in dorsal thalamus and 105 other 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 CDD; cd00112; LDLa; 1.
DR Gene3D; 2.70.130.10; -; 1.
DR Gene3D; 4.10.400.10; -; 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; 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; 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 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
