ID A0A0V1NTM8_9BILA Unreviewed; 1315 AA.
AC A0A0V1NTM8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Protein dif-1 {ECO:0000313|EMBL:KRZ87292.1};
GN Name=dif-1 {ECO:0000313|EMBL:KRZ87292.1};
GN ORFNames=T08_11938 {ECO:0000313|EMBL:KRZ87292.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ87292.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ87292.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ87292.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the APH-1 family.
CC {ECO:0000256|ARBA:ARBA00005577}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375}.
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:KRZ87292.1}.
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DR EMBL; JYDM01000103; KRZ87292.1; -; Genomic_DNA.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
DR CDD; cd07211; Pat_PNPLA8; 1.
DR CDD; cd20384; Tudor_ZGPAT; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR009294; Aph-1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_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; PF06105; Aph-1; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1050..1069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1076..1100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1106..1125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1159..1181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1205..1224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1236..1256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1262..1283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 162..357
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REPEAT 737..823
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 832..922
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 939..1025
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 1315 AA; 146232 MW; 5AA7B6C9B99B04AC CRC64;
MTTVSFMIIK LFTSNDQNQL ELTKPIEPKR SDYGYSLSYI YDFLGSIWQS DTKDKKICVQ
KNAYTTSSYV SKETIIQETL EIVRQLGIAK TVHDQLEVVN NLRHHLNSFP ECRTIREMRT
VTPLLIQWHR KTCGGELREQ LSECLALMGH VQPVSGSGIR LLSIDGGGTR GLMALEILEA
LESACAGYRI HELFDYMVGV STGAIIVALI GGLGLNAAEC RTIYELVPAR LFAQSKISGS
LGLVRSHSYY STETWITLLR QALGEKTFLQ TTHKKMHPKL GLVSCFPHDG RLYPFVFRNY
NHPIGLRSSF EGSCQYRLWE AVQASAAAPG YFQECRLHNL LHQDGGMIAN NPTAVGIHEC
RHLWPNIPFQ CILSIGNGSF RVNNKRSPTT DYSSLRDRIA QIIESATETE MVHRTISDLV
QPSIYVRLNP YMSQRYSLDE SDVHRLKQMH YSHGETVKFG DIIEYEEPDF ENLSVGSRCL
VKCGSEDLWK LASVTSISLE EEQIAARLAN TGVVLAVNFE HVFPLNEQSS LKIEVNQAEE
SLPKALLSSS SSAGSTDPVC RKSLDHCLQI QRNKESKDLP VEKLRVHLDD KKYEAKLAKR
TEAVEKFFDM INGHLQTPEA NQRKRTAEKG ATVVDISSKK SCHDLQITLL KVGEEVKQMK
KRVNSLKQAL RRNDGKDSVV AGDLQIKLKL AEEQLQLSLG KQARIENEVK DRREKQHTDM
VENDSESIDL VKPRQDTDPL RNFLAGGIGG VCCVVTGHPF DTIKVRLQTA SVATGGISTL
SCLKKTVVEE GVLALYKGMA APVVGVAPLF ALYFFGCSIG KRLQQTNADE QLSIIKTFNA
GALSGMMTTL IVAPGERIKC LLQVQHQHQR SEAQYTGPVD VFKKLYKEGG IRSIYRGTVA
TLLRDVPASG AYLATYEFLM RSMKSSDYIF IVQSDTGELS VSKTLLAGGV AGLANWAVAL
PQDVLKSRLQ IAPSGMYPNG MRDVARQLIR EEGPLALYRG FTPVMLRAFP ANAACFLGYE
IAMKGLIKLG FRLQKHSVRV HVSTMGFQEF TGYFLIAFGT PLAIFLRVIM HDPMRIILFV
GAAFFYMISI LLAAIIWFIL PHFDGILCFT VFLFVFLQEV IRYLYYKLIR RAQAGLDVVT
EANDSVEGVH PLKHANHMIS FVIGMGFGSM AGVIALVNGL ADSSGPGTVG LPSALKLNDM
HGSHHFFLIS SISVAALILL HVMWNVIIFH ACDKKATWLA MFAIADHFLV AGISFYNRSN
VWAASLSCLY GSLLLFSGLA YAVSGGNVKN ACLFIRCIFD PRLRAQNPPN VDQRF
//
