ID A0A0B0MJ15_GOSAR Unreviewed; 1319 AA.
AC A0A0B0MJ15;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN ORFNames=F383_20126 {ECO:0000313|EMBL:KHF99448.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHF99448.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHF99448.1}.
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DR EMBL; JRRC01079634; KHF99448.1; -; Genomic_DNA.
DR RefSeq; XP_017645837.1; XM_017790348.1.
DR GeneID; 108486342; -.
DR KEGG; gab:108486342; -.
DR OMA; FNAFYHA; -.
DR OrthoDB; 5477952at2759; -.
DR Proteomes; UP000032142; Unassembled WGS sequence.
DR GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07211; Pat_PNPLA8; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR045217; PNPLA8-like.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR24185; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR PANTHER; PTHR24185:SF1; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361262};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361262};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361262};
KW Reference proteome {ECO:0000313|Proteomes:UP000032142};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
SQ SEQUENCE 1319 AA; 145892 MW; D0C4066DC9D58308 CRC64;
MSWGLGWKRP SEIFRLSLNY GYEKSAEDLD HTSPVSSSLS SPESSTPQDQ KELGFRIDLD
WVAGDDEDQV AIRLQSKLMV ALPEPQDTVS VELRETEEKL VGVEMKVEKR REPLRAVTMA
KAAGSGQQSD GVGVLVRLLR SNLVPSGDSG LVACGDHWRS VTLLSLCGCG LTTLPVKLTQ
LPVLEKLYLD NNKLSVLPPE LGELKTLKVL RVDNNMLISV PAELRQCVGL VELSLEHNKL
VRPLLDFRAM AELQILRLFG NPLEFLPEIL PLHKLRHLSL ANIRIVADEN LRSVNVQIEM
ENSSYFGASR HKLSAFFSLI FRFSSCHHPL LASALVKIIT QDQGNRVVIG KDENAVRQLI
SMISSEDRHV VEQACSALST LGGDVSVAMQ LMKCDIMQPI ETVMKSPDPV ELVSVLQVVV
TLAIGSDIVA QKMLTKDVLR SLKLLCAHKN PEVQRLALLA VGNLAFCLEN RCILVTSESL
KELLMRLTVG PEPRVNKAAA RALAILGENE NLRRAIRGRQ IPKQGLRILS MDGGGMKGLA
TVQILKEIEK GTGKRIHELF DLICGTSTGG MLAVALGIKL LTLDQCEEIY KNLGKLVFAE
PVPKDNEAAT WREKLDMLYK SSSQSFRVVV HGSKHSADQF ERLLKEMCAD EDGDLLIESA
VKNIPKVFVV STLVSVMPAQ PFIFRNYQYP VGTPEVPLSI SESAGITTLG SPTTGAQVGY
KRSAFIGSCK HHIWQAIRAS SAAPYYLDDF SDDVNRWQDG AIVANNPTIF SIREAQLLWP
DTKIDCIVSI GCGSVPTKAR KGGWRYLDTG QVLIESACSV DRTEEALSTL VPMLPEIQYF
RFNPVDERCD MELDETDPTV WLKLEACVKD YIENNSESFK NACERLILPF AHDEKWTENL
KSQHFAKAKA SDADENSPSL GWRRNVLLVE ALHSPDSGRI VHHARALESF CARNGIRLSL
LHDISGLSKA LPATTFPTPF TSPLITGSFP SSPLLFSTDT GLQRLGRIDT VPPLSLDGLQ
SVKIAISPPT SPSAPRQLSL PVRSLHEKLQ NLPQVGIIHL ALQNDSVGSV LSWQNDVFVV
AEPGELADKF LQSVKLSMLS VLQSQRQKCV SPFANITTIA DLVRCKPYFQ VGKIGHRYIG
RQTQVMEDDI EIGAYMFRRT VPSLHLTPDD VRWMVGAWRD RIIICTGTYG PNANLIKAFL
DSGAKAVICP AAEPHDVSVN ISGEYNVLEN GKFEIGEEDA EDEEVEVETI SPVSDWDSDM
EKNEEHCTGF GDEEEELSRF VCQVYDLIFR EGARVDVALK TALASNRKLR YCCHLPNVK
//
