ID A0A1V9XF17_9ACAR Unreviewed; 915 AA.
AC A0A1V9XF17;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=BIW11_10686 {ECO:0000313|EMBL:OQR71942.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR71942.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR71942.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR71942.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(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|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000256|ARBA:ARBA00006931, 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:OQR71942.1}.
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DR EMBL; MNPL01013011; OQR71942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XF17; -.
DR STRING; 418985.A0A1V9XF17; -.
DR InParanoid; A0A1V9XF17; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000192247; 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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495:SF7; GPI INOSITOL-DEACYLASE; 1.
DR PANTHER; PTHR15495; NEGATIVE REGULATOR OF VESICLE FORMATION-RELATED; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365011};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365011};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365011};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365011};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365011};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365011}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..915
FT /note="GPI inositol-deacylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013003567"
FT TRANSMEM 614..631
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 692..725
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 757..786
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 813..832
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 844..863
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
SQ SEQUENCE 915 AA; 102934 MW; DB17EB3002628190 CRC64;
MSVPSNVLVG SFAVLSALVS LRQLLDLPAN HCSMTYMPIP PQYIEVEMTE NVTKRFPRYR
LLLYGEGVVA RDLRRFGPRG IPLVFIHGNA GNPGQARAIG SILQLKAEMR NMLDSPVYSV
YTVDFDEELS ALYGGVLPQQ AEFLQECLRV VCQKWNSSHP DQPPRIIFVG HSMGGVVARS
LYLQPDFDIS LVGLHVELAS PSQRPVAYLD RGLWEFYERI NQVWSQVGHV LPPVLSIMGG
ERDLQVRANL GGSPQNLRVL SESVPQCWAS SDHLCVVWCK QLQLALSRAL LDIVHNGSII
EDRDRIIRVL NYHFVRKFAF HNSLQTLPRL PRSVDFAQGR EWQEMFEGSW RYMRKKVITG
ISLVVPVYKE LSVTLVAYGL ENDDWLFGCT RMKREGSVVS CLSGVDISRK NLLVPSLIKR
QEAMFESTGR GTGRVYHISP EEISARNFQS LVIAVPALME DVVILGERFI SRKRETTFDA
TALFNGFFQK KTVLSMHLSE KAIYQKLTLA GMQHLWQVYT IKVHSKLCMD GTTGASFASF
KPDWSKEEQF FRIRARPNAI TKFTLRLHSA PGHRENHNST LSFYFDPGCS YDVHLQFDLK
TSLAQLLVHH AEGLFSYCLA LVLVVIARQM VDLGQLGICF TFGDSLSRSS RFFALTLLPA
LIEAMTFLPT PPAPLAPYLS RPPSTTSTTE GYVVRILLYA LALGLISLLA KTLELVLDLC
SAIYIRTKKC MRQSWDDPRT MPQLNENATS RTLTATLVAV LGLTVGVGGG VGLTAAICVH
CIQVIVLSCQ NRFLEDRKGA SAFSSRWKLQ TSLLLVQLLC LPLYLPSLAI WIRQQFTPLA
NDPYLFSAPI CVFFATVVTQ PNVPHPNRYY YKSTGYCIYI LAILSVLVCR EAIFRMSYIQ
LIVFALLFFQ QNFKP
//
