ID A0A0V1N8U0_9BILA Unreviewed; 1573 AA.
AC A0A0V1N8U0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 02-APR-2025, entry version 43.
DE SubName: Full=Protein dif-1 {ECO:0000313|EMBL:KRZ80268.1};
GN Name=dif-1 {ECO:0000313|EMBL:KRZ80268.1};
GN ORFNames=T10_4281 {ECO:0000313|EMBL:KRZ80268.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ80268.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ80268.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ80268.1};
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:KRZ80268.1}.
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DR EMBL; JYDO01000003; KRZ80268.1; -; Genomic_DNA.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:TreeGrafter.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0019369; P:arachidonate metabolic process; IEA:TreeGrafter.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
DR CDD; cd07211; Pat_PNPLA8; 1.
DR CDD; cd20384; Tudor_ZGPAT; 1.
DR Gene3D; 2.30.30.1190; -; 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; IPR000467; G_patch_dom.
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; PF01585; G-patch; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00443; G_patch; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
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 1308..1327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1334..1358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1364..1383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1417..1439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1463..1482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1494..1514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1520..1541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..368
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT DOMAIN 759..805
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT REPEAT 985..1073
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 1082..1172
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 1189..1275
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REGION 705..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 177..182
FT /note="GXGXXG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT MOTIF 210..214
FT /note="GXSXG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT MOTIF 355..357
FT /note="DGA/G"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT COMPBIAS 714..725
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 1573 AA; 175805 MW; F1C41D3997E03419 CRC64;
MRMNFMPVRW IRFLNNFKYH RLFASNDQNQ HELTKPIEPK RSDYGYSLSY IYDFLGSIWQ
SDAKDKKICA QKNAYTTSSY VSKEIIIQET LEIVRQLGIA KTVHDQLEVV NNLRHHLISF
PECRTIGEMR TVTPLLIQWQ RKTYGVGLRE QLSECLALMG HVQPVSGRGI RLLSIDGGGT
RGLMALEILE ALESACAGYR IHELFDYMVG VSTGAIIVAL IGGLRLNAAE CRTIYELVPA
RLFAQSKISG SLGLMRSHSY YSTETWVTLL RQALGEKTFL QTTHRKVHPK LGLVSCVPND
GRLFPFVFRN YNHPIGLRSN FEGSCQYRLW EAVQASAAAP GYFQECRLHN LLHQDGGMIA
NNPTAVGIHE CRHLWPNIPF QCILSIGNGS FRVNNRRCST ADYSSLRDRI AQIIESATET
EMVHRTISDL LQPSTYIRLN PYMSHRYSLD ESDVHRLKQM QLIELCHISV KKKVSICVSI
YCCSLVMDEK VATELIEQIR NIDALLEVTE LPDREDMLRL REDLMALLPS SSVNAESWAV
DLQEDSNVET SLTSDSDLFE QFIGLRCRVP CDNKHSSLLY HNAIIFDIED MTSSTSEDIL
VLYINPVERS MQPCKHFLDN SYSHGETVKF ADIIEYEEPD FENLSVGSKC LVKCGSEDLW
KLASVTSISL EEEQIAARLA NTGVLLAVNF EHVFPLNEQS SLKTEVSQTE ESLPKALPSS
SSAGSTGPVC STSAASGSLI GDWEVHTRFV MFNFFYLVQQ GIGTKLMEKM GYIRGQGLGK
DNLGQTEPIA VHVFPKGKSL DHCLQIQRNR ESKDLPVEKL RVHLDDKKYE AKLAKRTEAV
EKFFNMINGH LKTPDANQRK RTAENGATVV DISSKKSCHD LQITLLKVGE EVKQMKKRVS
SLKQALRRND GKDSVVAEDL QIKLKLAEEQ LQLSLGKQAR IEDEVKDRRE KQLLFFFCSA
NCIQINMVEN DSESIDRLVK QRQDTDPLRN FLAGGIGGVC CVVTGHPFDT IKVRLQTAST
ATGGFGTSTL SCLKKTVVDE GILALYKGMA APVAGVAPLF ALYFFGCSIG KRLQQTSADE
QLSIIKTFNA GALSGMMTTL IVAPGERIKC LLQVQHQHQR SEAQYTGPVD VFKKLYKEGG
IRSIYRGTVA TLLRDVPASG AYLATYECLM RSMKSSDYIS IVQSDTGELS VSKTLLAGGV
AGLANWAVAL PQDVLKSRLQ IAPSGMYPNG MRDVARQLIR EEGPLALYRG FTPVMLRAFP
ANAACFLGYE IAMKESCNLN VHQCDYINSR LQKHSVRVHV PIMGFQEFTG YFLIAFGTPL
AIFLRVIMHD PMRIILFVGA AFFYMLSILV AAIIWFILPH FDGMLCFTVF LFVFLQEIIR
YLYYQLIRRA QAGLDLVTEG NESVEGVHPL KHANHMISFV IGMGFGSMAG IIALVNGLAD
SSGPGTVGLP SALKLSDMHG SHHFFLISSI SVAALILLHV MWNVIIFHAC DKKATWLAMF
AIADHFLVTG ISFYNRSNAW AASLSCLYGS LLLFSGLAYA ISGGNVKNVR LFIRCIFNPR
MRAQNPPDVD QRF
//
