ID A0A1U8JBK6_GOSHI Unreviewed; 457 AA.
AC A0A1U8JBK6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN Name=LOC107904263 {ECO:0000313|RefSeq:XP_016686063.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016686063.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|RefSeq:XP_016686063.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016686063.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Lipolytic acyl hydrolase (LAH).
CC {ECO:0000256|RuleBase:RU361262}.
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. {ECO:0000256|RuleBase:RU361262}.
CC -!- SIMILARITY: Belongs to the patatin family.
CC {ECO:0000256|RuleBase:RU361262}.
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DR RefSeq; XP_016686063.1; XM_016830574.1.
DR AlphaFoldDB; A0A1U8JBK6; -.
DR STRING; 3635.A0A1U8JBK6; -.
DR PaxDb; 3635-A0A1U8JBK6; -.
DR OMA; PMTRISG; -.
DR OrthoDB; 518048at2759; -.
DR Proteomes; UP000189702; Chromosome 19.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07199; Pat17_PNPLA8_PNPLA9_like; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR32241; PATATIN-LIKE PROTEIN 6; 1.
DR PANTHER; PTHR32241:SF3; PATATIN-LIKE PROTEIN 6; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU361262};
KW Lipid degradation {ECO:0000256|RuleBase:RU361262};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361262};
KW Reference proteome {ECO:0000313|Proteomes:UP000189702}.
FT DOMAIN 77..285
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 457 AA; 49965 MW; EFAB3D96B3982263 CRC64;
MSSNTPSEMQ EPSIDTDKLS YEIFSILESK FLFGYDDNQK LWIPKPISPP ASEPMVQPGD
ENSLPAIKNQ RGKICILSID SGGMKGILCG KALAYLEKAL KSKSGNPNAR IADYFDVAAG
SSVGGIFTAM LFATRDNNQP IFTAEETWRF LADNGKRIYR SGAGKNGGIL KKILKNGSTG
SSSNGMEKVM KEAFTAGRRS LTLKDTLKPV LIPCYDLSST APFLFSRADA LETDSFDFPL
WEVCRATSAE PGLSGPVLMQ SVDGQTKCVA VDGGLAMSNP TVAAITHVLH NKQEFPFVRG
VEDLLVLSLG TGQLLEVSYE YEQVRNWRLK DWAKPMTRIS GDGSADSVDQ TVAMAFQQCR
SSNYVRIQAN GSSLGRCGPN VDTDPSPSNV KLLMEIGEEM LKQKNVESIL FGGKRISEES
NMEKLDWFAG ELVLEHQRRS CRIAPTVAFK QPSPKIN
//