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Protein

Lysophospholipase-like protein 1

Gene

LYPLAL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has depalmitoylating activity toward KCNMA1. Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site.2 Publications

Catalytic activityi

Palmitoyl-protein + H2O = palmitate + protein.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei124 – 1241Charge relay systemBy similarity
Active sitei179 – 1791Charge relay systemBy similarity
Active sitei211 – 2111Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

ESTHERihuman-LYPLAL1. LYsophospholipase_carboxylesterase.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipase-like protein 1 (EC:3.1.2.-)
Gene namesi
Name:LYPLAL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:20440. LYPLAL1.

Subcellular locationi

Isoform 1 :
Isoform 2 :

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134986975.

Chemistry

ChEMBLiCHEMBL2189133.

Polymorphism and mutation databases

BioMutaiLYPLAL1.
DMDMi74762275.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 237236Lysophospholipase-like protein 1PRO_0000227557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ5VWZ2.
MaxQBiQ5VWZ2.
PaxDbiQ5VWZ2.
PRIDEiQ5VWZ2.

PTM databases

iPTMnetiQ5VWZ2.
PhosphoSiteiQ5VWZ2.

Expressioni

Gene expression databases

BgeeiQ5VWZ2.
CleanExiHS_LYPLAL1.
GenevisibleiQ5VWZ2. HS.

Organism-specific databases

HPAiHPA045806.

Interactioni

Protein-protein interaction databases

BioGridi126031. 1 interaction.
IntActiQ5VWZ2. 2 interactions.
STRINGi9606.ENSP00000355895.

Structurei

Secondary structure

1
237
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 144Combined sources
Beta strandi22 – 276Combined sources
Helixi34 – 4512Combined sources
Beta strandi52 – 598Combined sources
Beta strandi63 – 653Combined sources
Helixi67 – 693Combined sources
Beta strandi73 – 753Combined sources
Beta strandi81 – 877Combined sources
Helixi91 – 11020Combined sources
Helixi115 – 1173Combined sources
Beta strandi118 – 1236Combined sources
Helixi125 – 13713Combined sources
Beta strandi141 – 1488Combined sources
Helixi156 – 1638Combined sources
Beta strandi171 – 1766Combined sources
Beta strandi180 – 1823Combined sources
Helixi184 – 19613Combined sources
Beta strandi201 – 2066Combined sources
Helixi215 – 22814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U0VX-ray1.72A1-237[»]
ProteinModelPortaliQ5VWZ2.
SMRiQ5VWZ2. Positions 9-230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2112. Eukaryota.
COG0400. LUCA.
GeneTreeiENSGT00390000009648.
HOGENOMiHOG000260139.
HOVERGENiHBG105375.
InParanoidiQ5VWZ2.
KOiK06999.
OMAiLEYPHIK.
OrthoDBiEOG7BZVTH.
PhylomeDBiQ5VWZ2.
TreeFamiTF314619.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR003140. PLipase/COase/thioEstase.
[Graphical view]
PfamiPF02230. Abhydrolase_2. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5VWZ2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAASGSVLQ RCIVSPAGRH SASLIFLHGS GDSGQGLRMW IKQVLNQDLT
60 70 80 90 100
FQHIKIIYPT APPRSYTPMK GGISNVWFDR FKITNDCPEH LESIDVMCQV
110 120 130 140 150
LTDLIDEEVK SGIKKNRILI GGFSMGGCMA IHLAYRNHQD VAGVFALSSF
160 170 180 190 200
LNKASAVYQA LQKSNGVLPE LFQCHGTADE LVLHSWAEET NSMLKSLGVT
210 220 230
TKFHSFPNVY HELSKTELDI LKLWILTKLP GEMEKQK
Length:237
Mass (Da):26,316
Last modified:January 23, 2007 - v3
Checksum:iA813A55DADDAF55E
GO
Isoform 2 (identifier: Q5VWZ2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     65-80: Missing.

Note: May be due to a competing acceptor splice site. No experimental confirmation available.
Show »
Length:221
Mass (Da):24,476
Checksum:iFD2558A6BB7B1017
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321D → G in BAF84231 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti131 – 1311I → M.3 Publications
Corresponds to variant rs940570 [ dbSNP | Ensembl ].
VAR_025607
Natural varianti197 – 1971L → V.
Corresponds to variant rs34201999 [ dbSNP | Ensembl ].
VAR_060992

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei65 – 8016Missing in isoform 2. 1 PublicationVSP_017556Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY341430 mRNA. Translation: AAQ17077.1.
AK291542 mRNA. Translation: BAF84231.1.
AL360093 Genomic DNA. Translation: CAH70459.1.
AL360093 Genomic DNA. Translation: CAH70460.1.
BC016711 mRNA. Translation: AAH16711.1.
CCDSiCCDS1522.1. [Q5VWZ2-1]
CCDS73032.1. [Q5VWZ2-2]
RefSeqiNP_001287698.1. NM_001300769.1.
NP_001287699.1. NM_001300770.1. [Q5VWZ2-2]
NP_001287700.1. NM_001300771.1.
NP_001287701.1. NM_001300772.1.
NP_620149.2. NM_138794.4. [Q5VWZ2-1]
UniGeneiHs.657617.

Genome annotation databases

EnsembliENST00000366927; ENSP00000355894; ENSG00000143353. [Q5VWZ2-2]
ENST00000366928; ENSP00000355895; ENSG00000143353. [Q5VWZ2-1]
GeneIDi127018.
KEGGihsa:127018.
UCSCiuc001hlq.5. human. [Q5VWZ2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY341430 mRNA. Translation: AAQ17077.1.
AK291542 mRNA. Translation: BAF84231.1.
AL360093 Genomic DNA. Translation: CAH70459.1.
AL360093 Genomic DNA. Translation: CAH70460.1.
BC016711 mRNA. Translation: AAH16711.1.
CCDSiCCDS1522.1. [Q5VWZ2-1]
CCDS73032.1. [Q5VWZ2-2]
RefSeqiNP_001287698.1. NM_001300769.1.
NP_001287699.1. NM_001300770.1. [Q5VWZ2-2]
NP_001287700.1. NM_001300771.1.
NP_001287701.1. NM_001300772.1.
NP_620149.2. NM_138794.4. [Q5VWZ2-1]
UniGeneiHs.657617.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U0VX-ray1.72A1-237[»]
ProteinModelPortaliQ5VWZ2.
SMRiQ5VWZ2. Positions 9-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126031. 1 interaction.
IntActiQ5VWZ2. 2 interactions.
STRINGi9606.ENSP00000355895.

Chemistry

ChEMBLiCHEMBL2189133.

Protein family/group databases

ESTHERihuman-LYPLAL1. LYsophospholipase_carboxylesterase.

PTM databases

iPTMnetiQ5VWZ2.
PhosphoSiteiQ5VWZ2.

Polymorphism and mutation databases

BioMutaiLYPLAL1.
DMDMi74762275.

Proteomic databases

EPDiQ5VWZ2.
MaxQBiQ5VWZ2.
PaxDbiQ5VWZ2.
PRIDEiQ5VWZ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366927; ENSP00000355894; ENSG00000143353. [Q5VWZ2-2]
ENST00000366928; ENSP00000355895; ENSG00000143353. [Q5VWZ2-1]
GeneIDi127018.
KEGGihsa:127018.
UCSCiuc001hlq.5. human. [Q5VWZ2-1]

Organism-specific databases

CTDi127018.
GeneCardsiLYPLAL1.
H-InvDBHIX0001597.
HGNCiHGNC:20440. LYPLAL1.
HPAiHPA045806.
MIMi616548. gene.
neXtProtiNX_Q5VWZ2.
PharmGKBiPA134986975.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2112. Eukaryota.
COG0400. LUCA.
GeneTreeiENSGT00390000009648.
HOGENOMiHOG000260139.
HOVERGENiHBG105375.
InParanoidiQ5VWZ2.
KOiK06999.
OMAiLEYPHIK.
OrthoDBiEOG7BZVTH.
PhylomeDBiQ5VWZ2.
TreeFamiTF314619.

Miscellaneous databases

ChiTaRSiLYPLAL1. human.
GenomeRNAii127018.
NextBioi81986.
PROiQ5VWZ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VWZ2.
CleanExiHS_LYPLAL1.
GenevisibleiQ5VWZ2. HS.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR003140. PLipase/COase/thioEstase.
[Graphical view]
PfamiPF02230. Abhydrolase_2. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Zhou G., Yu R., Cao L., Ke R., Li H., Shen C., Zhong G., Lin L., Yang S.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT MET-131.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-131.
    Tissue: Placenta.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-131.
    Tissue: Bone marrow.
  5. Bienvenut W.V., Claeys D.
    Submitted (JAN-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11 AND 56-64, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Distinct acyl protein transferases and thioesterases control surface expression of calcium-activated potassium channels."
    Tian L., McClafferty H., Knaus H.G., Ruth P., Shipston M.J.
    J. Biol. Chem. 287:14718-14725(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity despite close relationship to acyl protein thioesterases."
    Burger M., Zimmermann T.J., Kondoh Y., Stege P., Watanabe N., Osada H., Waldmann H., Vetter I.R.
    J. Lipid Res. 53:43-50(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS), FUNCTION.

Entry informationi

Entry nameiLYPL1_HUMAN
AccessioniPrimary (citable) accession number: Q5VWZ2
Secondary accession number(s): A8K677
, Q5VWZ3, Q7Z4A3, Q96AV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.