GLU2B_USTMA
ID GLU2B_USTMA Reviewed; 583 AA.
AC P0CT24; A0A0D1DMI5; Q4P0B9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Glucosidase 2 subunit beta;
DE AltName: Full=Alpha-glucosidase 2 subunit beta;
DE Flags: Precursor;
GN ORFNames=UMAG_12045;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit of glucosidase 2, which cleaves sequentially the 2
CC innermost alpha-1,3-linked glucose residues from the
CC Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature
CC glycoproteins in the endoplasmic reticulum (ER). Specifically required
CC for the cleavage of the final glucose. The subunit beta retains the
CC catalytic subunit alpha in the ER (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of a catalytic subunit alpha and a subunit beta.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
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DR EMBL; CM003162; KIS65739.1; -; Genomic_DNA.
DR RefSeq; XP_011392753.1; XM_011394451.1.
DR AlphaFoldDB; P0CT24; -.
DR SMR; P0CT24; -.
DR STRING; 5270.UM06444P0; -.
DR EnsemblFungi; KIS65739; KIS65739; UMAG_12045.
DR GeneID; 23567831; -.
DR KEGG; uma:UMAG_12045; -.
DR VEuPathDB; FungiDB:UMAG_12045; -.
DR eggNOG; KOG2397; Eukaryota.
DR OrthoDB; 632472at2759; -.
DR Proteomes; UP000000561; Chromosome 23.
DR GO; GO:0017177; C:glucosidase II complex; IBA:GO_Central.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR026874; Glucosidase_2_bsu.
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; PTHR12630; 1.
DR PANTHER; PTHR12630:SF1; PTHR12630:SF1; 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 Coiled coil; Disulfide bond; Endoplasmic reticulum; Reference proteome;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..583
FT /note="Glucosidase 2 subunit beta"
FT /id="PRO_0000423830"
FT DOMAIN 455..562
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT COILED 130..252
FT /evidence="ECO:0000255"
FT MOTIF 580..583
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT DISULFID 91..115
FT /evidence="ECO:0000250"
FT DISULFID 457..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 519..548
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 533..560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 583 AA; 64265 MW; E42B01F4B737BC43 CRC64;
MVRLNLAVVA LAAGALSASA SASSSATPLR GLLTDAAKYQ PTKDAQSQLR WKCLDGSKEL
SWSAVNDDYC DCPDGSDEPG TSACPNSSFY CHNTGHMPAY IRSSRVDDGI CDPECCDGSD
ESDGKIRCPN RCEKVGKEYR KKLAELDNLR RAGAKVRDKY IAEGRKQKEL LHAEIAKLEI
EVQVATENEA RFKAELTRAE TSDKALIDAK VKTPLYTKLV DYQNAIRALH VKNAALKAEL
QTLTLLLDDL AKGYNPNYQD MAVKGAVVAY KEWRGIASAA AAATATGEVK EEGENNVDQI
AGENTKLNEL LDEGDWPWAK LSTLLSDDPL DLMDRGLGGA LDDKRVYASE TDGGLLFRIH
EYLPDGIVPY FEAMVDTLLD VLMKANVITD VKRMRPKSSV GSESEPETVS VARRAHTDAA
AHLSRTTHEL SSLKQKLSEF STRYGRSAEF KALENKCFSK DMGEYTYEYC FFGRATQIPN
NGGAQISLGT FTNFNPKHDK SADEDAYWLQ QIYARGQKCW NGPERSAIVD LECSTENKVL
DVFEAEKCIY SIKVATPAVC FPPQQQQAQQ TQQDGGHQVK DEL
