ID C3YRU1_BRAFL Unreviewed; 901 AA.
AC C3YRU1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=BRAFLDRAFT_279100 {ECO:0000313|EMBL:EEN56846.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN56846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN56846.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN56846.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU365011}.
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DR EMBL; GG666548; EEN56846.1; -; Genomic_DNA.
DR RefSeq; XP_002600834.1; XM_002600788.1.
DR AlphaFoldDB; C3YRU1; -.
DR STRING; 7739.C3YRU1; -.
DR eggNOG; KOG3724; Eukaryota.
DR InParanoid; C3YRU1; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050185; F:phosphatidylinositol deacylase activity; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006505; P:GPI anchor metabolic process; IBA:GO_Central.
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}; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..901
FT /note="GPI inositol-deacylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002933832"
FT TRANSMEM 677..707
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 727..755
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 797..817
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 829..847
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 859..878
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
SQ SEQUENCE 901 AA; 101212 MW; FE779A430614461B CRC64;
MPILMLGLVL VGLFDILSNF ETNRCEMTWM YEYPEYLPVP LSENVTRSFP RYGLYLYGEG
AYARQSKNFK LTGVPVLFIP GNAGSHKQVR SLGSVALKKA QHLRTPFHFN YFSVDLNEEL
TGMFGAILSE QTEFVHRCIL KILTMYKKAD SPPKSVILVG HSVGGIVARA LFTLPDFDPS
MVNTIITQAT PHQSPVINAD QYMADFYNTV NQFWQDGMSS GRLSHVTIAS TGGAHRDYLV
RAGLTSLKGI VPESNAVSAV TSAIPKVWLS TDHLAIVWCK QLVLATKRSL FDIIDPKTRQ
VTTDVKHRMQ VFRHHFLHHP GSKSFSLTSV QSAVPPGDKW VEITDEVWEF SETRTEDVTN
YMFPIEKELG GRETFVATTN IVEDSWVYLC QDEGGKRCKE GLDMSSRGQL SPPLYSGHKV
VHLHLHSYRS FSHVVVSVPK SSKPVTVQTQ FYNGTEKSQE LQVPNVMSFA IRSVVEVEVP
NNTVFYNISL VGLQEVYHAF TANLVSDCED NDMTKMHMHI PWFKEDIYSV SQGSGNGKLS
LRLQSGKLVD ENTNAELRLY LNPKCNYKVQ VWVNFAEVLG QLIRFHGIVI PALAVTNILK
VLSYQVRTLG RGQPCPSFSE AQTAFCQPYR VAPLVNLFSL LLSYQGARLM YLSLGIPLPD
SEVIKAQGSW FRLLPILFYL FSSAICRMVS AALFGGVTMI GHCMVWFGKK TADPEEMARK
APHPAVLFVI SGAFLAVASQ FSGALAFALV LALYFGKTCR LYANTITLKN CLNLQNDKKK
PGPLADAEDT FHLQYTILYL IWFMSMLYMP SVVFWGKNLN FEYRLPADPA LYTAAAMSAC
FAFLYPLQGC YLRKKRSVVW LSWLVYVSAI LACMYSMVAL YRTPYFILLA FVVVAFCQRM
A
//
