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Database: UniProt
Entry: A0A1A6H928_NEOLE
LinkDB: A0A1A6H928_NEOLE
Original site: A0A1A6H928_NEOLE 
ID   A0A1A6H928_NEOLE        Unreviewed;       776 AA.
AC   A0A1A6H928;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
DE   Flags: Fragment;
GN   ORFNames=A6R68_14681 {ECO:0000313|EMBL:OBS74811.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS74811.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS74811.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS74811.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS74811.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT   lepida.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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:OBS74811.1}.
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DR   EMBL; LZPO01044393; OBS74811.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A6H928; -.
DR   STRING; 56216.A0A1A6H928; -.
DR   Proteomes; UP000092124; Unassembled WGS sequence.
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:SF14; PHOSPHOLIPID PHOSPHATASE-RELATED PROTEIN TYPE 3; 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:UP000092124};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          132..304
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          339..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..488
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..733
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..759
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         776
FT                   /evidence="ECO:0000313|EMBL:OBS74811.1"
SQ   SEQUENCE   776 AA;  83210 MW;  D1F453E1A3ABA7E8 CRC64;
     MIAMKEKNKT PKDSMTLLPC FYFVELPIVA SSIVSLYFLE LTDLFKPAKV GFQCYDRSLS
     MPYVETNEEL IPLLMLLSLA FAAPAASIMV GEGMVYCLQS RLWGRSSGGA EGSINAGGCN
     FNSFLRRTVR FVGVHVFGLC ATALVTDVIQ LATGYHTPFF LTVCKPNYTL LGTSCEANPY
     ITQDICSGHD THAILSARKT FPSQHATLSA FAAVYVSVSE SPQCCTLCPP VGSSYNLDPA
     YLLAQMYFNS VISDTTKLLK PILVFAFAIA AGVCGLTQIT QYRSHPVDVY AGFLIGAGIA
     AYLACHAVGN FQAPTAEKVS VPAPAKDALR ALTQRGHESM YQQNKAVSTD ELGPPGRLEG
     VPRPVAREKT SLGSLKRASV DVDLLAPRSP MGKEGMVTFS NTLPRVSTPS LDDPARRHMT
     IHVPLDASRS KQLISEWKQK SLEGRGLGLP DEGSPVHLRA PAEPMAEEEE EEEEEEEEEE
     EEEEEEGPVP PSLYPTVQAR PGLGPRVILP PRPGPQPLVH IPEEGVQAGA GLSPKSSSSV
     RAKWLSMAEK GGAPVAVAPS QPRVANPPRL LQVIAMSKAA GGPKAETASS SSASSDSSQY
     RSPSDRDSAS IVTIDAHAPH HPVVHLSAGS TPWEWKAKVV EGDGSYELGD LARGFRSSCK
     QPSMGPGSPV SDVDQEEPRF GAVATVNLAT GEGLPPPGAS DGAMGAGSRE STLRRQVGGL
     GDREVEAEAE SYYRRMQARS NNRKQKNRAV SWQRNSGSGK KKNWEGRGGK KKVAKH
//
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