PLPL5_MOUSE
ID PLPL5_MOUSE Reviewed; 432 AA.
AC Q32LZ8; Q9D603;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Patatin-like phospholipase domain-containing protein 5 {ECO:0000305};
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:Q7Z6Z6};
GN Name=Pnpla5 {ECO:0000312|MGI:MGI:1923022};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Has abundant triacylglycerol lipase activity.
CC {ECO:0000250|UniProtKB:Q7Z6Z6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000250|UniProtKB:Q7Z6Z6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:Q7Z6Z6};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q32LZ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q32LZ8-2; Sequence=VSP_026374;
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DR EMBL; AK014771; BAB29543.1; -; mRNA.
DR EMBL; BC109360; AAI09361.1; -; mRNA.
DR EMBL; BC109361; AAI09362.1; -; mRNA.
DR CCDS; CCDS49685.1; -. [Q32LZ8-1]
DR RefSeq; NP_083703.1; NM_029427.1. [Q32LZ8-1]
DR RefSeq; XP_006521583.1; XM_006521520.2.
DR AlphaFoldDB; Q32LZ8; -.
DR STRING; 10090.ENSMUSP00000019012; -.
DR iPTMnet; Q32LZ8; -.
DR PhosphoSitePlus; Q32LZ8; -.
DR PaxDb; Q32LZ8; -.
DR PRIDE; Q32LZ8; -.
DR ProteomicsDB; 289765; -. [Q32LZ8-1]
DR ProteomicsDB; 289766; -. [Q32LZ8-2]
DR Antibodypedia; 27565; 91 antibodies from 17 providers.
DR Ensembl; ENSMUST00000019012; ENSMUSP00000019012; ENSMUSG00000018868. [Q32LZ8-1]
DR Ensembl; ENSMUST00000230566; ENSMUSP00000155268; ENSMUSG00000018868. [Q32LZ8-2]
DR GeneID; 75772; -.
DR KEGG; mmu:75772; -.
DR UCSC; uc007xbu.1; mouse. [Q32LZ8-2]
DR UCSC; uc007xbv.1; mouse. [Q32LZ8-1]
DR CTD; 150379; -.
DR MGI; MGI:1923022; Pnpla5.
DR VEuPathDB; HostDB:ENSMUSG00000018868; -.
DR eggNOG; KOG3773; Eukaryota.
DR GeneTree; ENSGT00940000162116; -.
DR HOGENOM; CLU_018371_0_1_1; -.
DR InParanoid; Q32LZ8; -.
DR OMA; FYCGTIP; -.
DR OrthoDB; 1204225at2759; -.
DR PhylomeDB; Q32LZ8; -.
DR TreeFam; TF314272; -.
DR Reactome; R-MMU-163560; Triglyceride catabolism.
DR BioGRID-ORCS; 75772; 1 hit in 77 CRISPR screens.
DR PRO; PR:Q32LZ8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q32LZ8; protein.
DR Bgee; ENSMUSG00000018868; Expressed in lip and 19 other tissues.
DR Genevisible; Q32LZ8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; ISO:MGI.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR033562; PLPL.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR12406; PTHR12406; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..432
FT /note="Patatin-like phospholipase domain-containing protein
FT 5"
FT /id="PRO_0000292022"
FT DOMAIN 12..181
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 404..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 16..21
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 47..51
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 168..170
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 49
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT VAR_SEQ 427..432
FT /note="WFPGMD -> FADCALG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026374"
SQ SEQUENCE 432 AA; 48480 MW; 9BE58A53D690BE41 CRC64;
MDFLEAEGGW NLSFSGSGYM GLYHVGVTQC LRQRAPRLIQ GARRFYGSSS GALNAMAIVF
GKSADFACSN LLDLVKLVER LSLGIFHPAY GPAEHIRKKL YENLPDNCHI LASQRLGISM
TRWPDGKNFI VTDFATRDEF IQALICTLYL PLYCGVIPPA FRGQRFIDGA LSNNLPFSDC
PTTITVSPFN GTVDICPQNI SHSLFELTAF NASFQISTRN FFRGLKSVFP PKPEVVADHC
RQGYLDALRF LERRGLTKEP VLWSLVSKEP PALVEGPRGT GHDQGQKTGP TVRWDIPNVL
VKDVPNFELL SPELEAALRK ACKRDFWTRV QCSVPGKVLA YLLLPCTLPF EYAYFRSRRL
MEWLPEAPDD LDWMRSILKS TTLEVYSMAK SWLLRLGSPP GTRADSGLLR QQRGTAPSGN
RPLNHRWFPG MD
