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Database: UniProt
Entry: U3KHN6_FICAL
LinkDB: U3KHN6_FICAL
Original site: U3KHN6_FICAL 
ID   U3KHN6_FICAL            Unreviewed;       693 AA.
AC   U3KHN6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Phospholipid phosphatase related 3 {ECO:0000313|Ensembl:ENSFALP00000014540.1};
GN   Name=PLPPR3 {ECO:0000313|Ensembl:ENSFALP00000014540.1};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000014540.1, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000014540.1, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000014540.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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DR   RefSeq; XP_005060153.1; XM_005060096.1.
DR   AlphaFoldDB; U3KHN6; -.
DR   STRING; 59894.ENSFALP00000014540; -.
DR   Ensembl; ENSFALT00000014602.2; ENSFALP00000014540.1; ENSFALG00000013931.2.
DR   GeneID; 101807343; -.
DR   KEGG; fab:101807343; -.
DR   CTD; 79948; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   GeneTree; ENSGT00940000160280; -.
DR   HOGENOM; CLU_021458_8_0_1; -.
DR   OMA; GNPWEWA; -.
DR   OrthoDB; 25293at2759; -.
DR   Proteomes; UP000016665; Chromosome 28.
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:UP000016665};
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        204..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        228..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          130..274
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          309..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..676
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  74318 MW;  3F5E3F373F01635B CRC64;
     MIPPKEKARA PKDSMTLLPC FYFVELPIVA SSVVTLYFLE LTDLFKPAKV GFQCHDRALS
     MPYVETNEEL IPLLMLLSLA FAAPAASIMV GEGMVYCLQS RLKGRAGAEG SINAGGCNFN
     SFLRRTVRFV GVHVFGLCAT ALVTDVIQLA TGYHAPFFLT VCKPNYTLLG TPCDANPYIT
     QDICSGTDKH AILSARKTFP SQHATLSAFA AVYVSMYFNS IISDSTKLLK PILVFAFAIA
     AGICGLTQIT QYRSHPADVY VGFLIGAGIA AYLAFHAVGN FRAPTERVPA QAPAKDALRA
     LTQRGHDSVY HQNKSVSTDE LNPQARLEEA ARPVPREKNS LGSLKRASVD VDLLAPRSPM
     GKENMVTFSN TLPRVNTPSM DDPARRHMTI HVPVDASRSK QLITEWKQKS LEGRSMTLAE
     EAAQGRGVGE PGEEVPPSLY PTVQARSAER VAVGPRVLIQ PRPGASQLVH IPEESQAGAG
     AAASAGAAVR AKWVMVAEKG GAQRVANPPR LMQVIAMSKQ QSLVSVTPKH SETSSSSTSS
     DSSQYRSPSE RDSSSIITID AHAPHHPVVH LSAGNGPWEW KSGPKGPDGP DTYELGEVGK
     DFHGFRPAKS AGVSPGSSVS DMEQDEPRYG SLAAIPGAAG GGGERVEAPP EGLLATASRD
     STLRRKPAER DGAADSEVDL YYKKMQAGRR FKD
//
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