PLAP_RAT
ID PLAP_RAT Reviewed; 795 AA.
AC P54319;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Phospholipase A-2-activating protein;
DE Short=PLA2P;
DE Short=PLAP;
GN Name=Plaa; Synonyms=Plap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-795.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7665086; DOI=10.1016/0378-1119(95)00253-3;
RA Wang H., Lemasters J.J., Herman B.;
RT "Cloning of a rat cDNA encoding a protein with high homology to mouse
RT phospholipase A2-activating protein.";
RL Gene 161:237-241(1995).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in protein ubiquitination, sorting and
CC degradation through its association with VCP (By similarity). Involved
CC in ubiquitin-mediated membrane proteins trafficking to late endosomes
CC in an ESCRT-dependent manner, and hence plays a role in synaptic
CC vesicle recycling (By similarity). May play a role in macroautophagy,
CC regulating for instance the clearance of damaged lysosomes (By
CC similarity). Plays a role in cerebellar Purkinje cell development.
CC Positively regulates cytosolic and calcium-independent phospholipase A2
CC activities in a tumor necrosis factor alpha (TNF-alpha)- or
CC lipopolysaccharide (LPS)-dependent manner, and hence prostaglandin E2
CC biosynthesis (By similarity). {ECO:0000250|UniProtKB:P27612,
CC ECO:0000250|UniProtKB:Q9Y263}.
CC -!- SUBUNIT: Interacts with ubiquitin. Interacts with UBXN6, VCP and YOD1;
CC may form a complex involved in macroautophagy.
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=AAA79979.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AABR03040245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U17901; AAA79979.1; ALT_SEQ; mRNA.
DR PIR; JC4239; JC4239.
DR RefSeq; NP_446318.3; NM_053866.3.
DR AlphaFoldDB; P54319; -.
DR SMR; P54319; -.
DR IntAct; P54319; 1.
DR MINT; P54319; -.
DR STRING; 10116.ENSRNOP00000010621; -.
DR iPTMnet; P54319; -.
DR PhosphoSitePlus; P54319; -.
DR jPOST; P54319; -.
DR PaxDb; P54319; -.
DR PRIDE; P54319; -.
DR Ensembl; ENSRNOT00000010621; ENSRNOP00000010621; ENSRNOG00000007753.
DR GeneID; 116645; -.
DR KEGG; rno:116645; -.
DR UCSC; RGD:621245; rat.
DR CTD; 9373; -.
DR RGD; 621245; Plaa.
DR eggNOG; KOG0301; Eukaryota.
DR GeneTree; ENSGT00550000074944; -.
DR HOGENOM; CLU_011791_2_0_1; -.
DR InParanoid; P54319; -.
DR OMA; HNVCALD; -.
DR OrthoDB; 1274776at2759; -.
DR PhylomeDB; P54319; -.
DR TreeFam; TF105944; -.
DR PRO; PR:P54319; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007753; Expressed in liver and 19 other tissues.
DR Genevisible; P54319; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0016005; F:phospholipase A2 activator activity; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0010992; P:ubiquitin recycling; IBA:GO_Central.
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; 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; SSF50978; SSF50978; 1.
DR PROSITE; PS51394; PFU; 1.
DR PROSITE; PS51396; PUL; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Developmental protein; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; WD repeat.
FT CHAIN 1..795
FT /note="Phospholipase A-2-activating protein"
FT /id="PRO_0000051132"
FT REPEAT 17..56
FT /note="WD 1"
FT REPEAT 63..107
FT /note="WD 2"
FT REPEAT 110..148
FT /note="WD 3"
FT REPEAT 149..188
FT /note="WD 4"
FT REPEAT 190..227
FT /note="WD 5"
FT REPEAT 229..268
FT /note="WD 6"
FT REPEAT 270..307
FT /note="WD 7"
FT DOMAIN 366..465
FT /note="PFU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00727"
FT DOMAIN 533..794
FT /note="PUL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00729"
FT REPEAT 546..588
FT /note="ARM 1"
FT REPEAT 589..620
FT /note="ARM 2"
FT REPEAT 621..669
FT /note="ARM 3"
FT REPEAT 670..715
FT /note="ARM 4"
FT REPEAT 716..755
FT /note="ARM 5"
FT REPEAT 756..795
FT /note="ARM 6"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 529
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y263"
FT CONFLICT 528
FT /note="S -> F (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="I -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 795 AA; 87084 MW; 648139781B618E32 CRC64;
MASGAARYRL SCSLPGHELD VRGLVCCLYP PGAFVSVSRD RTTRLWAPDS PNRGFTEMHC
MSGHSNFVSC VCIIPSSDIY PHGLIATGGN DHNICIFSLD SPMPLYILKG HKDTVCSLSS
GKFGTLLSGS WDTTAKVWLN DKCMMTLQGH TAAVWAVKIL PEQGLMLTGS ADKTIKLWKA
GRCERTFSGH EDCVRGLAIL SETEFLSCAN DASIRRWQIT GECLGVYYGH TNYIYSISVF
PNCRDFVTTA EDRSLRIWKH GECAQTIRLP AQSIWCCCVL DNGDIVVGAS DGIIRVFTEA
DERTASAEEI KAFERELSQA TIDSKTGDLG DINAEQLPGR EHLNEPGTRE GQTRLIRDGE
RVEAYQWSVS DGRWIKIGDV VGSSGANQQT SGKVLYEGKE FDYVFSIDVN EGGPSYKLPY
NVSDDPWLVA YNFLQKNDLN PMFLDQVAKF IIDNTKGQTL GLGNTSFSDP FTGGGRYVPG
TSGPSNTVQT ADPFTGAGRY MPGSAGMDTT MAGVDPFTGN SAYRSAASKT VNIYFPKKEA
LTFDQANPTQ ILGKLKELNG SAPEEKKLTE DDLVLLEKIL SLICGNASEK PTAQQLQVLW
KAINWPEDIV FPALDILRLS IKHPSVNENF CNEKEGDQFS SHLINLLNPK GKPANQLLAL
RTFCNCFVSQ AGQKLMMSQR ESLMSHAIEL KSGSNKNIHI ALATLTLNYS VCFHKDHNIE
GKAQCLSVIS TILEVVQDLE ATFRLLVALG TLISDDSNAI QLAKSLGVDS QIKKYASVSE
PAKVSECCRL ILNLL
