ID H2SQF9_TAKRU Unreviewed; 309 AA.
AC H2SQF9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Phospholipid phosphatase-related protein type 5-like {ECO:0000313|Ensembl:ENSTRUP00000014646.3};
GN Name=LOC101073565 {ECO:0000313|Ensembl:ENSTRUP00000014646.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000014646.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000014646.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000014646.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR AlphaFoldDB; H2SQF9; -.
DR STRING; 31033.ENSTRUP00000014646; -.
DR Ensembl; ENSTRUT00000014714.3; ENSTRUP00000014646.3; ENSTRUG00000006024.3.
DR GeneTree; ENSGT00940000158610; -.
DR HOGENOM; CLU_021458_1_0_1; -.
DR InParanoid; H2SQF9; -.
DR OMA; EYRNHWT; -.
DR OrthoDB; 3806856at2759; -.
DR Proteomes; UP000005226; Chromosome 22.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd03384; PAP2_wunen; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR PANTHER; PTHR10165:SF17; PHOSPHOLIPID PHOSPHATASE-RELATED PROTEIN TYPE 5; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..309
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025571018"
FT TRANSMEM 55..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..255
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 272..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 33556 MW; C715095FA6F38EC7 CRC64;
MLYFQVVILA AVVMLAYYCE FTDTFSPAEQ GFICRDPALT KPDPGPEQDG RIQPVILYSV
VGGLPVVLIS GVEIIIFLLH HNSNLYDTEN VVMMGDCCYV NPMVRRTFQF LGVYVFGLFV
TDIFVNAGQL ITGSLAPHFL SVCRPNYTAL GCQGAAQFVS QTDACTGDPD DIMRARKTFP
SKEAALSLYT AVYLAMYIMS CVGSQAGCLT GPVLSLSLVS LALLIGINRV AEYRNHWTDV
IAGQAIGGAI AVFLVVFVVQ YFRKYHVLSH SPSDAETADT DEPTRSKAAM QTSDKHAVAQ
SPGSFSEVT
//
