LYPL1_HUMAN
ID LYPL1_HUMAN Reviewed; 237 AA.
AC Q5VWZ2; A8K677; Q5VWZ3; Q7Z4A3; Q96AV0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Lysophospholipase-like protein 1 {ECO:0000305};
DE EC=3.1.2.22 {ECO:0000269|PubMed:22399288};
GN Name=LYPLAL1 {ECO:0000312|HGNC:HGNC:20440};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-131.
RA Zhou G., Yu R., Cao L., Ke R., Li H., Shen C., Zhong G., Lin L., Yang S.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-131.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-131.
RC TISSUE=Bone marrow;
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).
RN [5]
RP PROTEIN SEQUENCE OF 2-11 AND 56-64, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (JAN-2006) to UniProtKB.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RX PubMed=22399288; DOI=10.1074/jbc.m111.335547;
RA Tian L., McClafferty H., Knaus H.G., Ruth P., Shipston M.J.;
RT "Distinct acyl protein transferases and thioesterases control surface
RT expression of calcium-activated potassium channels.";
RL J. Biol. Chem. 287:14718-14725(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS), AND FUNCTION.
RX PubMed=22052940; DOI=10.1194/jlr.m019851;
RA Burger M., Zimmermann T.J., Kondoh Y., Stege P., Watanabe N., Osada H.,
RA Waldmann H., Vetter I.R.;
RT "Crystal structure of the predicted phospholipase LYPLAL1 reveals
RT unexpected functional plasticity despite close relationship to acyl protein
RT thioesterases.";
RL J. Lipid Res. 53:43-50(2012).
CC -!- FUNCTION: Has depalmitoylating activity toward KCNMA1. Does not exhibit
CC phospholipase nor triacylglycerol lipase activity, able to hydrolyze
CC only short chain substrates due to its shallow active site.
CC {ECO:0000269|PubMed:22052940, ECO:0000269|PubMed:22399288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000269|PubMed:22399288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234;
CC Evidence={ECO:0000305|PubMed:22399288};
CC -!- INTERACTION:
CC Q5VWZ2; Q8WUE5: CT55; NbExp=3; IntAct=EBI-6268634, EBI-6873363;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:22399288}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:22399288}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VWZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VWZ2-2; Sequence=VSP_017556;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000305}.
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DR EMBL; AY341430; AAQ17077.1; -; mRNA.
DR EMBL; AK291542; BAF84231.1; -; mRNA.
DR EMBL; AL360093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016711; AAH16711.1; -; mRNA.
DR CCDS; CCDS1522.1; -. [Q5VWZ2-1]
DR CCDS; CCDS73032.1; -. [Q5VWZ2-2]
DR RefSeq; NP_001287698.1; NM_001300769.1.
DR RefSeq; NP_001287699.1; NM_001300770.1. [Q5VWZ2-2]
DR RefSeq; NP_001287700.1; NM_001300771.1.
DR RefSeq; NP_001287701.1; NM_001300772.1.
DR RefSeq; NP_620149.2; NM_138794.4. [Q5VWZ2-1]
DR PDB; 3U0V; X-ray; 1.72 A; A=1-237.
DR PDB; 5KRE; X-ray; 2.00 A; A=1-237.
DR PDBsum; 3U0V; -.
DR PDBsum; 5KRE; -.
DR AlphaFoldDB; Q5VWZ2; -.
DR SMR; Q5VWZ2; -.
DR BioGRID; 126031; 64.
DR IntAct; Q5VWZ2; 10.
DR MINT; Q5VWZ2; -.
DR STRING; 9606.ENSP00000355895; -.
DR BindingDB; Q5VWZ2; -.
DR ChEMBL; CHEMBL2189133; -.
DR ESTHER; human-LYPLAL1; LYsophospholipase_carboxylesterase.
DR GlyGen; Q5VWZ2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VWZ2; -.
DR PhosphoSitePlus; Q5VWZ2; -.
DR BioMuta; LYPLAL1; -.
DR DMDM; 74762275; -.
DR EPD; Q5VWZ2; -.
DR jPOST; Q5VWZ2; -.
DR MassIVE; Q5VWZ2; -.
DR MaxQB; Q5VWZ2; -.
DR PaxDb; Q5VWZ2; -.
DR PeptideAtlas; Q5VWZ2; -.
DR PRIDE; Q5VWZ2; -.
DR ProteomicsDB; 65567; -. [Q5VWZ2-1]
DR ProteomicsDB; 65568; -. [Q5VWZ2-2]
DR Antibodypedia; 34624; 184 antibodies from 28 providers.
DR DNASU; 127018; -.
DR Ensembl; ENST00000366927.3; ENSP00000355894.3; ENSG00000143353.12. [Q5VWZ2-2]
DR Ensembl; ENST00000366928.10; ENSP00000355895.5; ENSG00000143353.12. [Q5VWZ2-1]
DR GeneID; 127018; -.
DR KEGG; hsa:127018; -.
DR MANE-Select; ENST00000366928.10; ENSP00000355895.5; NM_138794.5; NP_620149.2.
DR UCSC; uc001hlq.5; human. [Q5VWZ2-1]
DR CTD; 127018; -.
DR DisGeNET; 127018; -.
DR GeneCards; LYPLAL1; -.
DR HGNC; HGNC:20440; LYPLAL1.
DR HPA; ENSG00000143353; Low tissue specificity.
DR MIM; 616548; gene.
DR neXtProt; NX_Q5VWZ2; -.
DR OpenTargets; ENSG00000143353; -.
DR PharmGKB; PA134986975; -.
DR VEuPathDB; HostDB:ENSG00000143353; -.
DR eggNOG; KOG2112; Eukaryota.
DR GeneTree; ENSGT00940000159171; -.
DR HOGENOM; CLU_049413_3_6_1; -.
DR InParanoid; Q5VWZ2; -.
DR OMA; LEYPHIK; -.
DR OrthoDB; 1373549at2759; -.
DR PhylomeDB; Q5VWZ2; -.
DR TreeFam; TF314619; -.
DR PathwayCommons; Q5VWZ2; -.
DR SignaLink; Q5VWZ2; -.
DR BioGRID-ORCS; 127018; 13 hits in 1075 CRISPR screens.
DR ChiTaRS; LYPLAL1; human.
DR GenomeRNAi; 127018; -.
DR Pharos; Q5VWZ2; Tbio.
DR PRO; PR:Q5VWZ2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VWZ2; protein.
DR Bgee; ENSG00000143353; Expressed in kidney epithelium and 187 other tissues.
DR Genevisible; Q5VWZ2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; NAS:UniProtKB.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central.
DR GO; GO:0002084; P:protein depalmitoylation; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..237
FT /note="Lysophospholipase-like protein 1"
FT /id="PRO_0000227557"
FT ACT_SITE 124
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 211
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT VAR_SEQ 65..80
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_017556"
FT VARIANT 131
FT /note="I -> M (in dbSNP:rs940570)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_025607"
FT VARIANT 197
FT /note="L -> V (in dbSNP:rs34201999)"
FT /id="VAR_060992"
FT CONFLICT 32
FT /note="D -> G (in Ref. 2; BAF84231)"
FT /evidence="ECO:0000305"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:3U0V"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:3U0V"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:3U0V"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:3U0V"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3U0V"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:3U0V"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3U0V"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:3U0V"
FT HELIX 91..110
FT /evidence="ECO:0007829|PDB:3U0V"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3U0V"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3U0V"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:3U0V"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:3U0V"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:3U0V"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3U0V"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3U0V"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:3U0V"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:3U0V"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:3U0V"
SQ SEQUENCE 237 AA; 26316 MW; A813A55DADDAF55E CRC64;
MAAASGSVLQ RCIVSPAGRH SASLIFLHGS GDSGQGLRMW IKQVLNQDLT FQHIKIIYPT
APPRSYTPMK GGISNVWFDR FKITNDCPEH LESIDVMCQV LTDLIDEEVK SGIKKNRILI
GGFSMGGCMA IHLAYRNHQD VAGVFALSSF LNKASAVYQA LQKSNGVLPE LFQCHGTADE
LVLHSWAEET NSMLKSLGVT TKFHSFPNVY HELSKTELDI LKLWILTKLP GEMEKQK
