GLU2B_ORYSI
ID GLU2B_ORYSI Reviewed; 614 AA.
AC A2WNF5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Glucosidase 2 subunit beta;
DE AltName: Full=Glucosidase II subunit beta;
DE Flags: Precursor;
GN ORFNames=OsI_01383;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Regulatory subunit of glucosidase II. May be required for
CC defense response elicited by pathogen-associated molecular patterns
CC (PAMPs) (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC -!- SUBUNIT: Heterodimer of a catalytic alpha subunit and a beta subunit.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
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; CM000126; EAY73501.1; -; Genomic_DNA.
DR AlphaFoldDB; A2WNF5; -.
DR SMR; A2WNF5; -.
DR STRING; 39946.A2WNF5; -.
DR PRIDE; A2WNF5; -.
DR EnsemblPlants; BGIOSGA001897-TA; BGIOSGA001897-PA; BGIOSGA001897.
DR Gramene; BGIOSGA001897-TA; BGIOSGA001897-PA; BGIOSGA001897.
DR HOGENOM; CLU_016834_3_0_1; -.
DR OMA; KCVYRME; -.
DR UniPathway; UPA00957; -.
DR Proteomes; UP000007015; Chromosome 1.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006491; P:N-glycan processing; IEA:InterPro.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR026874; Glucosidase_2_bsu.
DR InterPro; IPR039794; Gtb1-like.
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 PANTHER; PTHR12630:SF16; PTHR12630:SF16; 1.
DR Pfam; PF12999; PRKCSH-like; 1.
DR Pfam; PF13015; PRKCSH_1; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51914; MRH; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Plant defense;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..614
FT /note="Glucosidase 2 subunit beta"
FT /id="PRO_0000425978"
FT DOMAIN 497..592
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 194..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 499..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 549..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 563..590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 614 AA; 69347 MW; 39FD7FD2A379A357 CRC64;
MGLHTLLLLL LLRISASAAA SRPPLDTLGI PPQDEAYFRG GVIRCRDGSG RFARDKLNDD
FCDCPDGTDE PGTSACPEGK FYCQNAGHSP ITIFSSRVND GICDCCDGSD EYDSNVTCKN
TCWEAGKAAR DKLKKKVATY KSGVVIRNQE IQKAKVAFAK DEAELAKLKG EEKILQGLVD
KLTEQKKLIE KAEEEERLRK EKEEKRMKEE AEKQAADEKK ASDASQEVDS QENHETVQED
ESKVAEHHDG HATSHDNHTP ESESSVEQHD PESQDDISIK AAPADESPPE ETSAAPTKEQ
ESTPADSEGL SREELGRLVA SRWTGEKVDE VSKDDKNEHE AEHDMPEHSE ETHEDESDVP
ESAEDSYAGY HSEVEDDRHK YDDEDFSHES DDEYVDDHDE HVASYKSDDD QKGDDHSDFT
ASGQASWLDK IQQTVQNVLR TFNFFKTPVD LSEASRVRKE YDDASSKLSK IQSRISTLTD
KLKHDFGKEK EFYYFYDQCF ESKEGKYVYK VCPFKKASQV EGHSTTSLGR WDKFEESYRV
MQFSNGDRCW NGPDRSLKVR LRCGLNNELN GVDEPSRCEY VAVLSTPALC DEQKLKELEQ
KLEASSNQRD HDEL
