ID C9IZF6_HUMAN Unreviewed; 190 AA. AC C9IZF6; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 16-JAN-2019, entry version 65. DE SubName: Full=Patatin-like phospholipase domain-containing protein 4 {ECO:0000313|Ensembl:ENSP00000406698}; DE Flags: Fragment; GN Name=PNPLA4 {ECO:0000313|Ensembl:ENSP00000406698}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000406698, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000406698, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [2] {ECO:0000313|Ensembl:ENSP00000406698} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01161}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC005296; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; C9IZF6; -. DR SMR; C9IZF6; -. DR jPOST; C9IZF6; -. DR MaxQB; C9IZF6; -. DR PeptideAtlas; C9IZF6; -. DR PRIDE; C9IZF6; -. DR Ensembl; ENST00000442940; ENSP00000406698; ENSG00000006757. DR UCSC; uc064xxg.1; human. DR EuPathDB; HostDB:ENSG00000006757.11; -. DR HGNC; HGNC:24887; PNPLA4. DR OpenTargets; ENSG00000006757; -. DR eggNOG; KOG3773; Eukaryota. DR eggNOG; ENOG410XSQS; LUCA. DR GeneTree; ENSGT00940000162022; -. DR HOGENOM; HOG000007467; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; ENSG00000006757; Expressed in 212 organ(s), highest expression level in oocyte. DR ExpressionAtlas; C9IZF6; baseline and differential. DR GO; GO:0050253; F:retinyl-palmitate esterase activity; IEA:InterPro. DR GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd07222; Pat_PNPLA4; 1. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR033562; PLPL. DR InterPro; IPR033902; PNPLA4. DR InterPro; IPR002641; PNPLA_dom. DR PANTHER; PTHR12406; PTHR12406; 1. DR PANTHER; PTHR12406:SF39; PTHR12406:SF39; 1. DR Pfam; PF01734; Patatin; 1. DR SUPFAM; SSF52151; SSF52151; 1. DR PROSITE; PS51635; PNPLA; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01161}; KW Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU01161}; KW Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU01161}; KW Proteomics identification {ECO:0000213|EPD:C9IZF6, KW ECO:0000213|MaxQB:C9IZF6, ECO:0000213|PeptideAtlas:C9IZF6}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 190 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002997559. FT DOMAIN 6 176 PNPLA. {ECO:0000259|PROSITE:PS51635}. FT MOTIF 41 45 GXSXG. {ECO:0000256|PROSITE- FT ProRule:PRU01161}. FT MOTIF 163 165 DGA/G. {ECO:0000256|PROSITE- FT ProRule:PRU01161}. FT ACT_SITE 43 43 Nucleophile. {ECO:0000256|PROSITE- FT ProRule:PRU01161}. FT ACT_SITE 163 163 Proton acceptor. {ECO:0000256|PROSITE- FT ProRule:PRU01161}. FT NON_TER 190 190 {ECO:0000313|Ensembl:ENSP00000406698}. SQ SEQUENCE 190 AA; 20649 MW; B244E7B144697C64 CRC64; MKHINLSFAA CGFLGIYHLG AASALCRHGK KLVKDVKAFA GASAGSLVAS VLLTAPEKIE ECNQFTYKFA EEIRRQSFGA VTPGYDFMAR LRSGMESILP PSAHELAQNR LHVSITNAKT RENHLVSTFS SREDLIKVLL ASSFVPIYAG LKLVEYKGQK WVDGGLTNAL PILPVGRTVT ISPFSGRLDI //