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   24-JAN-2024, entry version 93.
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}.
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DR   EMBL; CM000126; EAY73501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2WNF5; -.
DR   SMR; A2WNF5; -.
DR   STRING; 39946.A2WNF5; -.
DR   EnsemblPlants; BGIOSGA001897-TA; BGIOSGA001897-PA; BGIOSGA001897.
DR   Gramene; BGIOSGA001897-TA; BGIOSGA001897-PA; BGIOSGA001897.
DR   HOGENOM; CLU_016834_3_0_1; -.
DR   OMA; YENGQHC; -.
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   Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 1.
DR   InterPro; IPR039794; Gtb1-like.
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; PF12999; PRKCSH-like; 1.
DR   Pfam; PF13015; PRKCSH_1; 1.
DR   SUPFAM; SSF50911; Mannose 6-phosphate receptor domain; 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
//