ID   PLAP_XENLA              Reviewed;         799 AA.
AC   Q6GM65; Q32N40; Q4KLW0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Phospholipase A-2-activating protein;
DE            Short=PLA2P;
DE            Short=PLAP;
GN   Name=plaa;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, Kidney, and Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in protein ubiquitination, sorting and
CC       degradation through its association with VCP. Involved in ubiquitin-
CC       mediated membrane proteins trafficking to late endosomes in an ESCRT-
CC       dependent manner, and hence plays a role in synaptic vesicle recycling.
CC       May play a role in macroautophagy, regulating for instance the
CC       clearance of damaged lysosomes. Plays a role in cerebellar Purkinje
CC       cell development. Positively regulates cytosolic and calcium-
CC       independent phospholipase A2 activities in a tumor necrosis factor
CC       alpha (TNF-alpha)- or lipopolysaccharide (LPS)-dependent manner, and
CC       hence prostaglandin E2 biosynthesis. {ECO:0000250|UniProtKB:P27612,
CC       ECO:0000250|UniProtKB:Q9Y263}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27612}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P27612}. Synapse {ECO:0000250|UniProtKB:P27612}.
CC       Note=Recruited to damaged lysosomes decorated with K48-linked ubiquitin
CC       chains. {ECO:0000250|UniProtKB:Q9Y263}.
CC   -!- DOMAIN: The PUL domain is composed of 6 armadillo-like repeats and
CC       mediates the interaction with VCP C-terminus.
CC       {ECO:0000250|UniProtKB:Q9Y263}.
CC   -!- DOMAIN: The PFU domain mediates interaction with ubiquitin.
CC       {ECO:0000250|UniProtKB:Q9Y263}.
CC   -!- SIMILARITY: Belongs to the WD repeat PLAP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH74216.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH98975.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI08855.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC074216; AAH74216.1; ALT_INIT; mRNA.
DR   EMBL; BC098975; AAH98975.1; ALT_INIT; mRNA.
DR   EMBL; BC108854; AAI08855.1; ALT_INIT; mRNA.
DR   RefSeq; XP_018099272.1; XM_018243783.1.
DR   AlphaFoldDB; Q6GM65; -.
DR   SMR; Q6GM65; -.
DR   PRIDE; Q6GM65; -.
DR   GeneID; 443698; -.
DR   KEGG; xla:443698; -.
DR   CTD; 443698; -.
DR   Xenbase; XB-GENE-17340768; plaa.S.
DR   OMA; HNVCALD; -.
DR   OrthoDB; 1274776at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 443698; Expressed in muscle tissue and 20 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR   GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR   GO; GO:1900045; P:negative regulation of protein K63-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:1903861; P:positive regulation of dendrite extension; ISS:UniProtKB.
DR   GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
DR   GO; GO:0032430; P:positive regulation of phospholipase A2 activity; ISS:UniProtKB.
DR   GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; ISS:UniProtKB.
DR   GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 3.10.20.870; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015155; PFU.
DR   InterPro; IPR038122; PFU_sf.
DR   InterPro; IPR013535; PUL_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF09070; PFU; 1.
DR   Pfam; PF08324; PUL; 1.
DR   Pfam; PF00400; WD40; 6.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS51394; PFU; 1.
DR   PROSITE; PS51396; PUL; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Neurogenesis; Nucleus;
KW   Reference proteome; Repeat; Synapse; WD repeat.
FT   CHAIN           1..799
FT                   /note="Phospholipase A-2-activating protein"
FT                   /id="PRO_0000239987"
FT   REPEAT          21..62
FT                   /note="WD 1"
FT   REPEAT          69..113
FT                   /note="WD 2"
FT   REPEAT          116..154
FT                   /note="WD 3"
FT   REPEAT          155..194
FT                   /note="WD 4"
FT   REPEAT          196..233
FT                   /note="WD 5"
FT   REPEAT          235..274
FT                   /note="WD 6"
FT   REPEAT          276..314
FT                   /note="WD 7"
FT   DOMAIN          372..471
FT                   /note="PFU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00727"
FT   DOMAIN          537..798
FT                   /note="PUL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00729"
FT   REPEAT          550..592
FT                   /note="ARM 1"
FT   REPEAT          593..624
FT                   /note="ARM 2"
FT   REPEAT          625..673
FT                   /note="ARM 3"
FT   REPEAT          674..719
FT                   /note="ARM 4"
FT   REPEAT          720..759
FT                   /note="ARM 5"
FT   REPEAT          760..799
FT                   /note="ARM 6"
FT   CONFLICT        517..518
FT                   /note="Missing (in Ref. 1; AAI08855)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        569
FT                   /note="E -> K (in Ref. 1; AAI08855)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   799 AA;  87870 MW;  123CA3A589A385D9 CRC64;
     MSQAGRDGGD SCYRLRCSLL GHELDVRGVA RCPLWPGEGF VSVSRDRSSR LWVPDSPNRG
     FIELQRMSGH SNFVSCVCIL PPSDLYPRGL IATGGNDQNI CVFSLDSEKP LYTLKGHKNT
     VCSLSSGKFG TLLSGSWDTT GKVWLNDKCM MTLQGHTAAV WAVKILPEQG LMLTGSADKS
     IKLWKAGRCE MTFLGHEDCV RGLATINDTE FLSCSNDASV RRWLITGECL QIYYGHTNYI
     YSVCLFPNSQ DFVTTSEDRS IRIWRKGECT QTIRLPAQSV WCCCVLDNGD IVVGASDGII
     RVFTESPDRI ASIEEIQAFE NELSKATIDP KTGDLGDIKI DDLPGRDHLN EPGTRDGQTR
     LIKEDGKVEA YQWSTGEGRW MKIGDVVGSS GATQQTSGRV LFEGKEYDYV FTIDVNESGP
     SHKLPYNLTE DPWLVAYNFL QKNDLNPMFL DQVAKFIIDN TAGQTPSTNL GYTDPLTGGG
     RYIPGSSSTD NNGADPFTGG NRYVPGSSLQ SDYSAAAADP FTGKNAYRSS TAPTPNAYFP
     KTKPVTFDQA NPSQILGKLK ELNESAPEER KLPEEDLMQL DKLLSVAVNP SGGTVTAQQL
     DTLWRVVNWP EDLIFPALDV LRISIKNPTV NEMFCNEKEG SQFSSYLLQL MSPSGKQANQ
     LLALRTFCNS FFCDPGSCLL MVERDNVLSK VIELKTVNNK NIHIALATLM LNYAICLHKV
     SDIEGKAQCL SAISSVIEVV QDLEAIFRLL VALGTLISGD TNAMQLAKSL GVDSQIKKYM
     SVTEPAKVNE CCRLLLNML