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PLPR2_BOVIN
ID   PLPR2_BOVIN             Reviewed;         389 AA.
AC   Q29RT8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Phospholipid phosphatase-related protein type 2 {ECO:0000250|UniProtKB:Q96GM1};
DE   AltName: Full=Inactive phospholipid phosphatase PLPPR2 {ECO:0000250|UniProtKB:Q6WAY2};
DE   AltName: Full=Lipid phosphate phosphatase-related protein type 2 {ECO:0000303|Ref.1};
DE   AltName: Full=Plasticity-related gene 4 protein {ECO:0000250|UniProtKB:Q96GM1};
DE            Short=PRG-4 {ECO:0000250|UniProtKB:Q96GM1};
GN   Name=PLPPR2 {ECO:0000250|UniProtKB:Q96GM1};
GN   Synonyms=LPPR2 {ECO:0000303|Ref.1}, PRG4 {ECO:0000250|UniProtKB:Q8VCY8};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Has most probably no phospholipid phosphatase activity (By
CC       similarity). This is supported by the fact that the phosphatase
CC       sequence motifs as well as the His residue acting as a nucleophile in
CC       active phosphatases of the PA-phosphatase related phosphoesterase
CC       family are not conserved (By similarity).
CC       {ECO:0000250|UniProtKB:Q6WAY2}.
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DR   EMBL; BC114023; AAI14024.1; -; mRNA.
DR   RefSeq; NP_001039713.1; NM_001046248.2.
DR   AlphaFoldDB; Q29RT8; -.
DR   STRING; 9913.ENSBTAP00000043142; -.
DR   PaxDb; Q29RT8; -.
DR   PRIDE; Q29RT8; -.
DR   GeneID; 520247; -.
DR   KEGG; bta:520247; -.
DR   CTD; 64748; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   InParanoid; Q29RT8; -.
DR   OrthoDB; 1621899at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR   GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR028679; LPPR2.
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; PTHR10165; 1.
DR   PANTHER; PTHR10165:SF15; PTHR10165:SF15; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..389
FT                   /note="Phospholipid phosphatase-related protein type 2"
FT                   /id="PRO_0000317537"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          255..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..338
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         236
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCY8"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCY8"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   389 AA;  41632 MW;  9A5166C408797A44 CRC64;
     MAGGRPQLKR SFSIIPCFVF VEILLGELAR AFFPAPPSAV PIIGESTIVS GACCRFSPPL
     RRLVRFLGVY SFGLFTTTIF ANAGQVVTGN PTPHFLSVCR PNYTALGCPP PSPDRPGPDR
     FVNDQGACAG SPSLVAAARR AFPCKDAALC AYAVTYTAMY VTLVFRVKGS RLVKPSLCLA
     LLCPAFLVGV VRVAEYRNHW SDVLAGFLTG AAIATFLVTC VVHNFQSRPP SGRRLSPWED
     LSQAPTMDSP LEKLSVAQEP EGCRSHSTPA RLTPSKPQNC ARRGHLIPNC VSSRAPAMCS
     SPRVPRPRLR SEPTPLPLPL PLPAPAPSQG PSPSSPGPGG PGGGGSRGRK LLLPTPLLRD
     LYTLSGLYPS PFHRDNFSPY LFASRDHLL
 
 
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