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Database: UniProt
Entry: A0A2G8JNZ6_STIJA
LinkDB: A0A2G8JNZ6_STIJA
Original site: A0A2G8JNZ6_STIJA 
ID   A0A2G8JNZ6_STIJA        Unreviewed;       515 AA.
AC   A0A2G8JNZ6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   11-DEC-2019, entry version 6.
DE   RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
DE   Flags: Fragment;
GN   ORFNames=BSL78_25734 {ECO:0000313|EMBL:PIK37439.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK37439.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK37439.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK37439.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK37439.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIK37439.1}.
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DR   EMBL; MRZV01001505; PIK37439.1; -; Genomic_DNA.
DR   Proteomes; UP000230750; Unassembled WGS sequence.
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; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR012908; PGAP1-like.
DR   InterPro; IPR039529; PGAP1/BST1.
DR   PANTHER; PTHR15495; PTHR15495; 2.
DR   Pfam; PF07819; PGAP1; 2.
DR   SUPFAM; SSF53474; SSF53474; 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:UP000230750};
KW   Transport {ECO:0000256|RuleBase:RU365011}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PIK37439.1"
SQ   SEQUENCE   515 AA;  57668 MW;  D0093E8BF53AED52 CRC64;
     PVPGLQEKTD NAFPRYSLYL YSEGAKKTSN FKLSGIPVLF IPGNAGSYRQ VRSLGSVAIT
     KAEESDYHFN YFSVDLNGEK NALYGGFLLE QTEFVHQCIR HILSFYSEAK NKPKSVVVVG
     HSMYWKANQE ALNHVTLLSV GGGHRDIMVK SAATDLNGIV LPSRRISSVS MSVPHVWLAA
     DHQCIVWCKE LVLATKRALF DMIDPKTSLI SEDAEHRMKV FRYHFTDHSG SKVYQGHVED
     TIKFSDKQNL TFKIATDSRL HIAAFNKDKI TYYLFPIPSS NHGFVATTKI PAARWIFLCT
     KATTTTCEEG IDITKRGRVV PPLKASVREI HLSPEELEGH KFVVVRVLSG IGGVINAEMY
     DYEDGNAVVT LPPFFSLQPQ TVMNVTGKSY ISMVLEDFTS VSTAYVAELV HVMCPSDVTA
     KINSTLRFEV PWKEEDTFSV AAVKDTNSLS LKLQSGRPPK ADNESMPRLS VYMDPRCRYA
     VTLRYSHKEG YGQCHCVLSL CSKEFITDDI RFGIE
//
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