ID A0A1B6QBE9_SORBI Unreviewed; 688 AA.
AC A0A1B6QBE9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=SORBI_3002G147100 {ECO:0000313|EMBL:KXG35221.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG35221.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG35221.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins
CC which plays important roles in the quality control and ER-associated
CC degradation of GPI-anchored proteins. {ECO:0000256|RuleBase:RU365011}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU365011}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000256|RuleBase:RU365011}.
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DR EMBL; CM000761; KXG35221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6QBE9; -.
DR STRING; 4558.A0A1B6QBE9; -.
DR EnsemblPlants; KXG35221; KXG35221; SORBI_3002G147100.
DR Gramene; KXG35221; KXG35221; SORBI_3002G147100.
DR eggNOG; KOG3724; Eukaryota.
DR InParanoid; A0A1B6QBE9; -.
DR OMA; LGHYFAH; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000000768; Chromosome 2.
DR ExpressionAtlas; A0A1B6QBE9; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR PANTHER; PTHR47346; HYDROLASES, ACTING ON ESTER BOND; 1.
DR PANTHER; PTHR47346:SF1; HYDROLASES, ACTING ON ESTER BOND; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU365011};
KW Hydrolase {ECO:0000256|RuleBase:RU365011};
KW Membrane {ECO:0000256|RuleBase:RU365011};
KW Protein transport {ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|RuleBase:RU365011}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..688
FT /note="GPI inositol-deacylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008589589"
FT REGION 397..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 74930 MW; 54290CEF2C8FF2F8 CRC64;
MGGGGGGFRG SCRVGAVLLF SAWVAVAALS RLLRPVPNGC VMTYMYPAYI PIAATPRNIS
SDRYGLFLYH EGWKQIDFAK HIRGLRGVPV LFIPGNGGSY KQVRSLAAES FRAYQNGPLE
PTFYREASST LPADELKDFS IPSRYGRMLD WFAVDLEGEH SAMDGRILEE HTEYVVYAIH
RILDQYKESQ LERSKGGAKS SHDLPSSVIL VGHSMGGFVA RAAVVHPNLR KSAVETILTL
SSPHQYPPIA LQPSLGHFFS HVNEEWRKGY GTGVSHASNS KLSNVVVVSV SGGIHDYQIR
SRLASLDGIV PSTHGFMVGS SSMKNVWLSM EHQSILWCNQ LAVQVAHTLL SIVDPVDRHP
FSSTQKRVFV FTKMLQSAVP QSLSSMAHVP ASLSQTLPAN GNQNAGELHK KGSLSCPPST
QWTSDGLEKD LYILSNSVTV LAMDGRRRWL DIKKLGSNGR RHFVFVTNLA PCSGVRIHLW
PEKHHSPVLN ELSASKKIVE VTSKMVQIPA GPAPKQVEPG SQTEQPPPSA FLLLSPEEMS
GFSFITVSVA PRPTISGRPP PAASMAVGQF FNPEEGASAL SIGTIIRSSF APEEIFLLED
HPLALNLSFS ASLGLLPVTL SLKTAGCGIK KAGDQMEAER NNLCKLRCFP PVALAWDSVS
GLHIIPNIYS ETIVVDSSPA FWDSHERD
//