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Database: UniProt
Entry: A0A1D1VCI9_RAMVA
LinkDB: A0A1D1VCI9_RAMVA
Original site: A0A1D1VCI9_RAMVA 
ID   A0A1D1VCI9_RAMVA        Unreviewed;       888 AA.
AC   A0A1D1VCI9;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN   Name=RvY_07686 {ECO:0000313|EMBL:GAU96208.1};
GN   Synonyms=RvY_07686.1 {ECO:0000313|EMBL:GAU96208.1};
GN   ORFNames=RvY_07686-1 {ECO:0000313|EMBL:GAU96208.1};
OS   Ramazzottius varieornatus (Water bear) (Tardigrade).
OC   Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC   Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX   NCBI_TaxID=947166 {ECO:0000313|EMBL:GAU96208.1, ECO:0000313|Proteomes:UP000186922};
RN   [1] {ECO:0000313|EMBL:GAU96208.1, ECO:0000313|Proteomes:UP000186922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAU96208.1,
RC   ECO:0000313|Proteomes:UP000186922};
RX   PubMed=27649274; DOI=10.1038/ncomms12808;
RA   Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA   Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA   Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA   Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA   Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT   "Extremotolerant tardigrade genome and improved radiotolerance of human
RT   cultured cells by tardigrade-unique protein.";
RL   Nat. Commun. 7:12808-12808(2016).
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:GAU96208.1}.
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DR   EMBL; BDGG01000003; GAU96208.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D1VCI9; -.
DR   STRING; 947166.A0A1D1VCI9; -.
DR   Proteomes; UP000186922; 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:UP000186922};
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   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        586..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        617..633
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        645..665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        672..692
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        712..744
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        765..786
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
FT   TRANSMEM        841..859
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
SQ   SEQUENCE   888 AA;  100112 MW;  DC0F2E0D483FAEEF CRC64;
     MDIPKRFVAV VIVLGLFAVG ILDVLFNYEQ NLCQMTYMFE QPDYTRIPLN ESVVENFPSY
     GLYVYGEGQR ATQYKRNIFN GIPVLFIPGN AGSFRQGRSI GSVLLRMAEK KRHSKVHFDV
     FTIDFDEEFS GLYGGFLQAQ THFVLQCLDK IGAMYKRKVP PKVVLIGHSL GGMIARGLFL
     NPSFDTASVS TIFTLSTPHR PIIVADFDYG EYFDDVNDYW TRSVNGSLRH VVMVSFAGGH
     RDVLVRSDRS DLTLLFGDND RFISITTTSI PAVWASTDHL CIVWCKQLVI ATARAIFDMV
     DFEKNSIIDN VQQRKAIVQK HFLNTLERTR HGDAQNFDFK ERSVRDHKAD TKTSSLDIRT
     KKFDEPFYQL YTFPENLSHD IFITWNRWMG REFIHVCDVS DCSRARTLTV KPVALPLTSE
     DSSFYTLIPQ SELQLDFALL FEVPKRDEAI ELYASLTLPW TNVTRITFVD ALMGSLGRGS
     VFVLSGQKYA RFNISLHEVW KAIDVRVASD EKCSGVMKFS VPGFAQDTYK RLDSKQSRTV
     FPLKLQSAVK DGEQSLLELF LEPGCSYEVS IGVDWTGILG QLIRFYVMHL PAYFAAVVIL
     RLLPLSLHRK VRLVDHVIVN AGAICVVIAS RFIPELKGFD VGFEGASVVS AVELWIVFYV
     IAWSIVQALE TLLRVAVIAY SYPVHFVAKL SVRRVNSLYS RLPGWASRRL MVIPVLSVLG
     FVVASATCGE NGMIFAVVLY FLRVCHARRN SQMTSEGAST DVEDYSTMLL LALLVTMVNI
     VPALVWTKKL PSALLSQWRS VFTGLDPDPS FMVSVLVGVV LDLTSRSRVK KAVLSRASEV
     MDLLMSFLIF TAAALILVFA QKTFYLINVF LGPFLTALSC DRFLKTFM
//
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