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Database: UniProt
Entry: A0A1U8K9Q5_GOSHI
LinkDB: A0A1U8K9Q5_GOSHI
Original site: A0A1U8K9Q5_GOSHI 
ID   A0A1U8K9Q5_GOSHI        Unreviewed;       247 AA.
AC   A0A1U8K9Q5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN   Name=LOC107913325 {ECO:0000313|RefSeq:XP_016697364.1};
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016697364.1};
RN   [1] {ECO:0000313|Proteomes:UP000189702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX   PubMed=25893780; DOI=10.1038/nbt.3208;
RA   Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA   Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA   Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA   Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA   Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT   "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT   provides insights into genome evolution.";
RL   Nat. Biotechnol. 33:524-530(2015).
RN   [2] {ECO:0000313|RefSeq:XP_016697364.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016697364.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_016697364.1; XM_016841875.1.
DR   AlphaFoldDB; A0A1U8K9Q5; -.
DR   GeneID; 107913325; -.
DR   OrthoDB; 5487271at2759; -.
DR   Proteomes; UP000189702; Chromosome 21.
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; PTHR47909; ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR47909:SF2; GPI INOSITOL-DEACYLASE; 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:UP000189702};
KW   Transport {ECO:0000256|RuleBase:RU365011}.
SQ   SEQUENCE   247 AA;  27130 MW;  96D860DC685EC136 CRC64;
     MALGLPPLNF KPHCSSTSTF SSSSTNYRPA VILPGLGNNT GDYKKLEFTL QEYGVPTVVA
     KVSRIDWLRN AAGLVDPNYW KGTLQPRPVL DWYLKRVDDA VQEAEELAQG GKLSVIGHSA
     GGWLARVYME EFGLSHISLL LTLGTPHLPP PKGLPGVIDQ TRGLLYYVQQ HCKKAVYTPE
     LKYVCIAGRY LQGARFVNDS KVAVESMATI DDDQQVSDVA VVKNKTDSTP VSTTFQARFV
     GQGYKQP
//
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