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Q8IY17 (PLPL6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuropathy target esterase

EC=3.1.1.5
Alternative name(s):
Patatin-like phospholipase domain-containing protein 6
Gene names
Name:PNPLA6
Synonyms:NTE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1366 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Ref.7 Ref.8

Catalytic activity

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Enzyme regulation

Inhibited by a series a OPs such as mipafox (MPX), phenyl saligenin phosphate (PSP), phenyl dipentyl phosphinate (PDPP), diisopropyl fluorophosphate and paraoxon. Ref.8

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein; Cytoplasmic side. Note: Anchored to the cytoplasmic face of the endoplasmic reticulum by its amino-terminal transmembrane segment. Ref.8

Tissue specificity

Expressed in brain, placenta, kidney, neuron and skeletal muscle. Ref.1

Post-translational modification

Glycosylated. Ref.1

Involvement in disease

Spastic paraplegia 39, autosomal recessive (SPG39) [MIM:612020]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG39 is associated with a motor axonopathy affecting upper and lower limbs and resulting in progressive wasting of distal upper and lower extremity muscles.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Belongs to the NTE family.

Contains 3 cyclic nucleotide-binding domains.

Contains 1 patatin domain.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IY17-1)

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.
Isoform 2 (identifier: Q8IY17-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MGTSSHGLATNSSGAKVAERDGFQDVLAPGEGSAGRICGAQPVPFVPQ → MEAPLQTGM
Isoform 3 (identifier: Q8IY17-3)

The sequence of this isoform differs from the canonical sequence as follows:
     754-754: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8IY17-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEAPLQTGMM
Note: No experimental confirmation available.
Isoform 5 (identifier: Q8IY17-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MGTSSHGLATNSSGAKVAERDGFQDVLAPGEGSAGRICGAQPVPFVPQ → MEAPLQTGM
     511-536: Missing.
     754-754: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13661366Neuropathy target esterase
PRO_0000292199

Regions

Topological domain1 – 5050Lumenal Potential
Transmembrane51 – 7121Helical; Potential
Topological domain72 – 13661295Cytoplasmic Potential
Domain972 – 1138167Patatin
Nucleotide binding186 – 313128cNMP 1
Nucleotide binding502 – 624123cNMP 2
Nucleotide binding620 – 740121cNMP 3
Motif1003 – 10075GXSXG

Sites

Active site10051 By similarity

Amino acid modifications

Modified residue3451Phosphoserine Ref.9 Ref.10 Ref.11
Modified residue3521Phosphothreonine Ref.10
Modified residue3531Phosphoserine Ref.10
Glycosylation111N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 4848MGTSS…PFVPQ → MEAPLQTGM in isoform 2 and isoform 5.
VSP_026388
Alternative sequence11M → MEAPLQTGMM in isoform 4.
VSP_046064
Alternative sequence511 – 53626Missing in isoform 5.
VSP_046975
Alternative sequence7541Missing in isoform 3 and isoform 5.
VSP_026389
Natural variant4031A → P. Ref.2 Ref.5
Corresponds to variant rs17854645 [ dbSNP | Ensembl ].
VAR_032949
Natural variant9291R → H in SPG39. Ref.13
VAR_044409
Natural variant10241K → R. Ref.5
Corresponds to variant rs17854647 [ dbSNP | Ensembl ].
VAR_032950
Natural variant10511M → V in SPG39. Ref.13
VAR_044410

Experimental info

Sequence conflict34 – 374AGRI → TRPV in AAH38229. Ref.5
Sequence conflict6391T → A in BAG57380. Ref.2
Sequence conflict7051A → T in AAH38229. Ref.5
Sequence conflict9851I → W in CAB43674. Ref.6
Sequence conflict11691W → V in CAB43674. Ref.6
Sequence conflict12871E → G in CAB43674. Ref.6
Sequence conflict12931E → K in BAH13718. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: 705E9A4E2195C887

FASTA1,366149,995
        10         20         30         40         50         60 
MGTSSHGLAT NSSGAKVAER DGFQDVLAPG EGSAGRICGA QPVPFVPQVL GVMIGAGVAV 

        70         80         90        100        110        120 
VVTAVLILLV VRRLRVPKTP APDGPRYRFR KRDKVLFYGR KIMRKVSQST SSLVDTSVSA 

       130        140        150        160        170        180 
TSRPRMRKKL KMLNIAKKIL RIQKETPTLQ RKEPPPAVLE ADLTEGDLAN SHLPSEVLYM 

       190        200        210        220        230        240 
LKNVRVLGHF EKPLFLELCR HMVFQRLGQG DYVFRPGQPD ASIYVVQDGL LELCLPGPDG 

       250        260        270        280        290        300 
KECVVKEVVP GDSVNSLLSI LDVITGHQHP QRTVSARAAR DSTVLRLPVE AFSAVFTKYP 

       310        320        330        340        350        360 
ESLVRVVQII MVRLQRVTFL ALHNYLGLTN ELFSHEIQPL RLFPSPGLPT RTSPVRGSKR 

       370        380        390        400        410        420 
MVSTSATDEP RETPGRPPDP TGAPLPGPTG DPVKPTSLET PSAPLLSRCV SMPGDISGLQ 

       430        440        450        460        470        480 
GGPRSDFDMA YERGRISVSL QEEASGGSLA APARTPTQEP REQPAGACEY SYCEDESATG 

       490        500        510        520        530        540 
GCPFGPYQGR QTSSIFEAAK QELAKLMRIE DPSLLNSRVL LHHAKAGTII ARQGDQDVSL 

       550        560        570        580        590        600 
HFVLWGCLHV YQRMIDKAED VCLFVAQPGE LVGQLAVLTG EPLIFTLRAQ RDCTFLRISK 

       610        620        630        640        650        660 
SDFYEIMRAQ PSVVLSAAHT VAARMSPFVR QMDFAIDWTA VEAGRALYRQ GDRSDCTYIV 

       670        680        690        700        710        720 
LNGRLRSVIQ RGSGKKELVG EYGRGDLIGV VEALTRQPRA TTVHAVRDTE LAKLPEGTLG 

       730        740        750        760        770        780 
HIKRRYPQVV TRLIHLLSQK ILGNLQQLQG PFPAGSGLGV PPHSELTNPA SNLATVAILP 

       790        800        810        820        830        840 
VCAEVPMVAF TLELQHALQA IGPTLLLNSD IIRARLGASA LDSIQEFRLS GWLAQQEDAH 

       850        860        870        880        890        900 
RIVLYQTDAS LTPWTVRCLR QADCILIVGL GDQEPTLGQL EQMLENTAVR ALKQLVLLHR 

       910        920        930        940        950        960 
EEGAGPTRTV EWLNMRSWCS GHLHLRCPRR LFSRRSPAKL HELYEKVFSR RADRHSDFSR 

       970        980        990       1000       1010       1020 
LARVLTGNTI ALVLGGGGAR GCSHIGVLKA LEEAGVPVDL VGGTSIGSFI GALYAEERSA 

      1030       1040       1050       1060       1070       1080 
SRTKQRAREW AKSMTSVLEP VLDLTYPVTS MFTGSAFNRS IHRVFQDKQI EDLWLPYFNV 

      1090       1100       1110       1120       1130       1140 
TTDITASAMR VHKDGSLWRY VRASMTLSGY LPPLCDPKDG HLLMDGGYIN NLPADIARSM 

      1150       1160       1170       1180       1190       1200 
GAKTVIAIDV GSQDETDLST YGDSLSGWWL LWKRLNPWAD KVKVPDMAEI QSRLAYVSCV 

      1210       1220       1230       1240       1250       1260 
RQLEVVKSSS YCEYLRPPID CFKTMDFGKF DQIYDVGYQY GKAVFGGWSR GNVIEKMLTD 

      1270       1280       1290       1300       1310       1320 
RRSTDLNESR RADVLAFPSS GFTDLAEIVS RIEPPTSYVS DGCADGEESD CLTEYEEDAG 

      1330       1340       1350       1360 
PDCSRDEGGS PEGASPSTAS EMEEEKSILR QRRCLPQEPP GSATDA 

« Hide

Isoform 2 [UniParc].

Checksum: E823248C9B29DD84
Show »

FASTA1,327146,216
Isoform 3 [UniParc].

Checksum: 5EBEEC5A15759534
Show »

FASTA1,365149,924
Isoform 4 [UniParc].

Checksum: 1C9F2797FB6D8612
Show »

FASTA1,375150,954
Isoform 5 [UniParc].

Checksum: 849012C97C5156A5
Show »

FASTA1,300143,351

References

« Hide 'large scale' references
[1]"Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man."
Lush M.J., Li Y., Read D.J., Willis A.C., Glynn P.
Biochem. J. 332:1-4(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), GLYCOSYLATION, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[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. expand/collapse author list , 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] (ISOFORMS 4 AND 5), VARIANT PRO-403.
Tissue: Cerebellum.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-1366 (ISOFORM 3), VARIANTS PRO-403 AND ARG-1024.
Tissue: Brain, Duodenum and Testis.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 985-1366 (ISOFORMS 1/2).
Tissue: Brain.
[7]"The pathogenesis of organophosphate polyneuropathy."
Lotti M.
Crit. Rev. Toxicol. 21:465-487(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Neuropathy target esterase and its yeast homologue degrade phosphatidylcholine to glycerophosphocholine in living cells."
Zaccheo O., Dinsdale D., Meacock P.A., Glynn P.
J. Biol. Chem. 279:24024-24033(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345; THR-352 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Neuropathy target esterase gene mutations cause motor neuron disease."
Rainier S., Bui M., Mark E., Thomas D., Tokarz D., Ming L., Delaney C., Richardson R.J., Albers J.W., Matsunami N., Stevens J., Coon H., Leppert M., Fink J.K.
Am. J. Hum. Genet. 82:780-785(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG39 HIS-929 AND VAL-1051.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ004832 mRNA. Translation: CAA06164.1.
AK294021 mRNA. Translation: BAG57380.1.
AK302462 mRNA. Translation: BAH13718.1.
AC008878 Genomic DNA. No translation available.
AC009003 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69029.1.
BC038229 mRNA. Translation: AAH38229.1.
BC050553 mRNA. Translation: AAH50553.1.
BC051768 mRNA. Translation: AAH51768.1.
AL050362 mRNA. Translation: CAB43674.1.
CCDSCCDS32891.1. [Q8IY17-2]
CCDS54206.1. [Q8IY17-4]
CCDS54207.1. [Q8IY17-5]
CCDS59343.1. [Q8IY17-3]
RefSeqNP_001159583.1. NM_001166111.1. [Q8IY17-4]
NP_001159584.1. NM_001166112.1. [Q8IY17-5]
NP_001159585.1. NM_001166113.1. [Q8IY17-2]
NP_001159586.1. NM_001166114.1. [Q8IY17-3]
NP_006693.3. NM_006702.4. [Q8IY17-2]
UniGeneHs.631863.

3D structure databases

ProteinModelPortalQ8IY17.
SMRQ8IY17. Positions 527-714.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116114. 2 interactions.
STRING9606.ENSP00000221249.

Chemistry

ChEMBLCHEMBL2189129.

PTM databases

PhosphoSiteQ8IY17.

Polymorphism databases

DMDM150403921.

Proteomic databases

MaxQBQ8IY17.
PaxDbQ8IY17.
PRIDEQ8IY17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221249; ENSP00000221249; ENSG00000032444. [Q8IY17-2]
ENST00000414982; ENSP00000407509; ENSG00000032444. [Q8IY17-4]
ENST00000450331; ENSP00000394348; ENSG00000032444. [Q8IY17-2]
ENST00000545201; ENSP00000443323; ENSG00000032444. [Q8IY17-5]
ENST00000600737; ENSP00000473211; ENSG00000032444. [Q8IY17-3]
GeneID10908.
KEGGhsa:10908.
UCSCuc002mgq.2. human. [Q8IY17-2]
uc002mgs.3. human. [Q8IY17-3]

Organism-specific databases

CTD10908.
GeneCardsGC19P007598.
HGNCHGNC:16268. PNPLA6.
HPAHPA007522.
MIM603197. gene.
612020. phenotype.
neXtProtNX_Q8IY17.
Orphanet1180. Ataxia - hypogonadism - choroidal dystrophy.
139480. Autosomal recessive spastic paraplegia type 39.
1173. Cerebellar ataxia - hypogonadism.
PharmGKBPA145148268.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0664.
HOVERGENHBG053067.
InParanoidQ8IY17.
KOK14676.
OMAKQRAREW.
OrthoDBEOG7QRQT1.
PhylomeDBQ8IY17.
TreeFamTF300519.

Gene expression databases

ArrayExpressQ8IY17.
BgeeQ8IY17.
CleanExHS_PNPLA6.
GenevestigatorQ8IY17.

Family and domain databases

Gene3D2.60.120.10. 3 hits.
InterProIPR016035. Acyl_Trfase/lysoPLipase.
IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR001423. LysoPLipase_patatin_CS.
IPR002641. Patatin/PLipase_A2-rel.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamPF00027. cNMP_binding. 3 hits.
PF01734. Patatin. 1 hit.
[Graphical view]
SMARTSM00100. cNMP. 3 hits.
[Graphical view]
SUPFAMSSF51206. SSF51206. 3 hits.
SSF52151. SSF52151. 1 hit.
PROSITEPS50042. CNMP_BINDING_3. 3 hits.
PS01237. UPF0028. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNeuropathy_target_esterase.
GenomeRNAi10908.
NextBio35535401.
PROQ8IY17.
SOURCESearch...

Entry information

Entry namePLPL6_HUMAN
AccessionPrimary (citable) accession number: Q8IY17
Secondary accession number(s): A6NGQ0 expand/collapse secondary AC list , B4DFB9, B7Z7T2, F5H5K9, J3KQS3, O60859, Q86W58, Q9UG58
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: July 9, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM