PAT01_SOLTU
ID PAT01_SOLTU Reviewed; 387 AA.
AC Q2MY50;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Patatin-01;
DE EC=3.1.1.-;
DE Flags: Precursor;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Kennebec;
RX PubMed=16322504; DOI=10.1534/genetics.105.051219;
RA Stupar R.M., Beaubien K.A., Jin W., Song J., Lee M.-K., Wu C., Zhang H.-B.,
RA Han B., Jiang J.;
RT "Structural diversity and differential transcription of the patatin
RT multicopy gene family during potato tuber development.";
RL Genetics 172:1263-1275(2006).
CC -!- FUNCTION: Probable lipolytic acyl hydrolase (LAH), an activity which is
CC thought to be involved in the response of tubers to pathogens.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Tuber. {ECO:0000269|PubMed:16322504}.
CC -!- DEVELOPMENTAL STAGE: Accumulates progressively during tuber formation
CC from stolon. {ECO:0000269|PubMed:16322504}.
CC -!- DOMAIN: The nitrogen atoms of the two glycine residues in the GGXR
CC motif define the oxyanion hole, and stabilize the oxyanion that forms
CC during the nucleophilic attack by the catalytic serine during substrate
CC cleavage.
CC -!- MISCELLANEOUS: Patatin have a dual role as a somatic storage protein
CC and as an enzyme involved in host resistance.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR EMBL; DQ274488; ABC55688.1; -; mRNA.
DR AlphaFoldDB; Q2MY50; -.
DR SMR; Q2MY50; -.
DR PRIDE; Q2MY50; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q2MY50; baseline.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Plant defense; Reference proteome; Signal; Storage protein; Vacuole.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..387
FT /note="Patatin-01"
FT /id="PRO_0000296687"
FT DOMAIN 32..230
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COILED 361..385
FT /evidence="ECO:0000255"
FT MOTIF 36..41
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 75..79
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 216..218
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 387 AA; 42608 MW; 6D75D338654B5A27 CRC64;
MATTKSFLIL SVMILATTSS TFASLEEMVT VLSIDGGGIK GIIPGTILEF LEGQLQKMDN
NADARLADYF DVIGGTSTGG LLTAMITTPN ENNRPFAAAN EIVPFYFEHG PHIFNSSTGQ
FFGPKYDGKY LMQVLQEKLG ETRVHQALTE VAISSFDIKT NKPVIFTKSN LAKSPELDAK
MYDICYSTAA APTYFPPHYF ATNTINGDKY EFNLVDGAVA TVADPALLSV SVATRRAQED
PAFASIRSLN YKKMLLLSLG TGTTSEFDKT HTAEETAKWG ALQWMLVIQQ MTEAASSYMT
DYYLSTVFQD LHSQNNYLRV QENALTGTTT KADDASEANM ELLAQVGENL LKKPVSKDNP
ETYEEALKRF AKLLSDRKKL RANKASY