PATT5_SOLTU
ID PATT5_SOLTU Reviewed; 386 AA.
AC P15478; Q2VBJ6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Patatin-T5;
DE EC=3.1.1.-;
DE AltName: Full=Group B patatin;
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 [GENOMIC DNA].
RX DOI=10.1007/BF00333957;
RA Rosahl S., Schmidt R., Schell J., Willmitzer L.;
RT "Isolation and characterization of a gene from Solanum tuberosum encoding
RT patatin, the major storage protein of potato tubers.";
RL Mol. Gen. Genet. 203:214-220(1986).
RN [2]
RP PROTEIN SEQUENCE OF 24-30; 41-47 AND 66-71, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION AT ASN-60 AND ASN-90.
RX DOI=10.1007/BF00393687;
RA Sonnewald U., Sturm A., Chrispeels M.J., Willmitzer L.;
RT "Targeting and glycosylation of patatin the major potato tuber protein in
RT leaves of transgenic tobacco.";
RL Planta 179:171-180(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 255-386, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Kennebec; TISSUE=Stolon, and Tuber;
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 -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|Ref.2}.
CC -!- TISSUE SPECIFICITY: Tuber and stolon. {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 -!- PTM: N-glycosylated. {ECO:0000269|Ref.2}.
CC -!- MISCELLANEOUS: Patatin have a dual role as a somatic storage protein
CC and as an enzyme involved in host resistance. This tuber protein
CC represents approximately 40% of the total protein in mature tubers.
CC -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR EMBL; X03932; CAA27571.1; -; Genomic_DNA.
DR EMBL; DQ274462; ABB96228.1; -; mRNA.
DR EMBL; DQ274182; ABC58772.1; -; mRNA.
DR EMBL; DQ274196; ABC58786.1; -; mRNA.
DR EMBL; DQ274197; ABC58787.1; -; mRNA.
DR EMBL; DQ274201; ABC58791.1; -; mRNA.
DR EMBL; DQ274217; ABC58807.1; -; mRNA.
DR EMBL; DQ274244; ABC58832.1; -; mRNA.
DR EMBL; DQ274262; ABC58849.1; -; mRNA.
DR EMBL; DQ274268; ABC58855.1; -; mRNA.
DR EMBL; DQ274271; ABC58858.1; -; mRNA.
DR EMBL; DQ274279; ABC58866.1; -; mRNA.
DR EMBL; DQ274301; ABC58887.1; -; mRNA.
DR EMBL; DQ274332; ABC58916.1; -; mRNA.
DR EMBL; DQ274362; ABC58945.1; -; mRNA.
DR PIR; A26017; A26017.
DR AlphaFoldDB; P15478; -.
DR SMR; P15478; -.
DR Allergome; 639; Sola t 1.
DR PRIDE; P15478; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P15478; differential.
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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Plant defense; Reference proteome; Signal;
KW Storage protein; Vacuole.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 24..386
FT /note="Patatin-T5"
FT /id="PRO_0000032260"
FT DOMAIN 32..229
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
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 215..217
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 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.2"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.2"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 386 AA; 42338 MW; E7F7FAD1A04A1000 CRC64;
MATTNSFTIL IFMILATTSS TFATLGEMVT VLSIDGGGIK GIIPATILEF LEGQLQEVDN
NTDARLADYF DVIGGTSTGG LLTAMITTPN ETNRPFAAAK DIVPFYFEHG PKIFQSSGSI
FGPKYDGKYL MQVLQEKLGE TRVHQALTEV AISSFDIKTN KPVIFTKSNL AKSPELDAKM
YDICYSTAAA PTFFPPHYFA TNTSNGDKYE FNLVDGAVAT VDDPALLSIS VATKLAQVDP
KFASIKSLNY KQMLLLSLGT GTTSEFDKTY TAEETAKWGT ARWMLVIQKM TSAASSYMTD
YYLSTAFQAL DSQNNYLRVQ ENALTGTTTE LDDASEANMQ LLVQVGEDLL KKSVSKDNPE
TYEEALKRFA KLLSDRKKLR ANKASY
