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Database: UniProt
Entry: A0A1U8JBK6_GOSHI
LinkDB: A0A1U8JBK6_GOSHI
Original site: A0A1U8JBK6_GOSHI 
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
//
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