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Database: UniProt
Entry: A0A3B4UHJ4_SERDU
LinkDB: A0A3B4UHJ4_SERDU
Original site: A0A3B4UHJ4_SERDU 
ID   A0A3B4UHJ4_SERDU        Unreviewed;       561 AA.
AC   A0A3B4UHJ4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Glycerophosphodiester phosphodiesterase domain-containing protein 5-like {ECO:0000313|Ensembl:ENSSDUP00000018151.1};
GN   Name=GDPD5 {ECO:0000313|Ensembl:ENSSDUP00000018151.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000018151.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000018151.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC       family. {ECO:0000256|ARBA:ARBA00007277}.
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DR   AlphaFoldDB; A0A3B4UHJ4; -.
DR   Ensembl; ENSSDUT00000018479.1; ENSSDUP00000018151.1; ENSSDUG00000013206.1.
DR   GeneTree; ENSGT00940000159690; -.
DR   OMA; CKHCRYR; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   InterPro; IPR030395; GP_PDE_dom.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   PANTHER; PTHR23344:SF6; GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE DOMAIN-CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR23344; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR   Pfam; PF03009; GDPD; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS51704; GP_PDE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        42..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        499..518
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          228..486
FT                   /note="GP-PDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51704"
SQ   SEQUENCE   561 AA;  64007 MW;  CDCA96CDABEBC194 CRC64;
     MVKHQPLQVY ERQLCLSCIT GIYGCRWKRY QRSHDDTTKW ELLWSLILLF TFCLLLVWFY
     FWWEAHNDYN EFNWFLYNRS GVWSDGTVPI LATTAAGFTY IAFLMVLALC HIALGQQLNL
     HWLHKIGVTA ALLTTIIGVI SVNQTWGQEW DVIPISLQAT GPFLHIGALA AVTALSWIVA
     GQVARAEKTM FQVVVVLLYL SVLLGLYVMP LYITSPCIME PTSLKPRPDV IGHQGAPMLA
     PENTLWSFQR ALQMNVTGLE ADVAISVDGV PFLMHDSTLR RTTDVEKVFP DRQMDEASFF
     NWTDLQQLNA GQWFLKDDPF WTVHTLSQHE KTLIANQSVC SLEQLLKLAS YHNSTVVFRL
     RRPPPDHPCY YSWINDTLQA VQQSGVPPSL VMWTPDEQRA QVRQLAPGLI QTSVEKLSPQ
     SLHQSGISRL LLRYNQASTQ DISDFSESHI NLTLYTVNEP WLYSVLWCSG VSSVSSEAPH
     ILRKVPYPIW LMRPHGYCLM WVSADLISFA VVIGIFIFQK YRMSGMHSYN PEQIMLSAAV
     RRSSRDISVM KEKLIFSGQS Q
//
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