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Database: UniProt
Entry: A0A1B6QBE9_SORBI
LinkDB: A0A1B6QBE9_SORBI
Original site: A0A1B6QBE9_SORBI 
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
//
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