ID A0A0V0Y2D8_TRIPS Unreviewed; 1557 AA.
AC A0A0V0Y2D8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Protein dif-1 {ECO:0000313|EMBL:KRX94365.1};
GN Name=dif-1 {ECO:0000313|EMBL:KRX94365.1};
GN ORFNames=T4E_2265 {ECO:0000313|EMBL:KRX94365.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX94365.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX94365.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX94365.1};
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 -!- FUNCTION: Transcription repressor. {ECO:0000256|ARBA:ARBA00004062}.
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:KRX94365.1}.
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DR EMBL; JYDU01000073; KRX94365.1; -; Genomic_DNA.
DR STRING; 6337.A0A0V0Y2D8; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; 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 InterPro; IPR000571; Znf_CCCH.
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 SMART; SM00356; ZnF_C3H1; 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.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT TRANSMEM 1292..1311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1318..1342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1348..1367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1401..1423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1447..1466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1478..1498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1504..1525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..368
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT DOMAIN 625..652
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 772..818
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT REPEAT 997..1085
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 1094..1184
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 1194..1280
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT ZN_FING 625..652
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 730..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 898..957
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1557 AA; 174093 MW; DE080A28ECC6EF39 CRC64;
MRMNFMPVRW IRFLNNFKYH RLFTSSDQNQ HELTKPTEPK RSDYGYSLSY IYDFLGSIWQ
SDAKDKKICA QKNAYTTSSY VSKENIIQET LEIVRQLGNA KTVHDQLEVV NNLRHHLISF
PECRTIGEMR TVTPLLIQWQ RKTYGVGLRE QLSECLALMG HVQPVSGNGI RLLSIDGGGT
RGLMALEILE ALESACAGYR IHELFDYMVG VSTGAIIVAL IGGLRLNAAE CRTIYELVPA
RLFAQSKISG SLGLVRSHSY YSTETWVTLL RQALGEKTFL QTTHRKVHPK LGLVSCVPND
GRLFPFVFRN YNHPIGLRST FEGSCQYRLW EAVQASAAAP GYFQECRLHN LLHQDGGMIA
NNPTAVGIHE CRHLWPNIPF QCILSIGNGS FRVNNKRCST ADYSSLRDRI AQIIESATET
EMVHRTISDL LQPSTYVRLN PYMSHRYSLD ESDVQRLKQM QYDAKIYLRK NSRKIKTASE
LLLKKKKKVS ICVSVYCRSL VMDEKVATEL MEQIRNIDAL LEVTELPDRE DMLRLREDLM
ALLPSSSLNG ESWAVDLQED SNVETSLTSD TDLFEQFIGL RCRVPCDNKH SSLSYHNAII
FDIEDMSSST SEDILVKVLY INPVERSMQP CKHFLDNRCT FNENCRYSHG ETVKFADIIE
YEEPDFENLS VGSKCLVKCG SEELWKLASV TSISLEEEQI AARLANTGVL LAVNFEHVFP
LNDQSSLKTE VSQTQESLPE ALPSSSSAGS ARPVCSTSAA SGSLIGDWEV HTRGIGTKLM
EKMGYIRGQG LGKDNLGQTE PIAVHVFPKG KSVDHCLQIQ RNRESKDLPV EKLRVHLDDK
KYEAKLAKRT EAVEKFFNMI NGHLKTPDAN QRKRAAEKGT TVVDISSKKS CHDLQITLLK
VGEEVKQMKK RVNSLKQALR RNDGKDSVVA EDLQIKLKLA EEQLQLSLEK QARIEDEVKD
RREKQLLFFF CSANCIQINM VENDSESIDL VKQRQDTDPL RNFLAGGIGG VCCVVTGHPF
DTIKVRLQTA STATGGFGPS TLSCLKKTVV DEGILALYKG MAAPVVGVAP LFALYFFGCS
IGKRLQQANA DEQLSIIKTF NAGALSGMMT TLIVAPGERI KCLLQVQHQH QRSEAQYAGP
VDVFKKLYKE GGIRSIYRGT VATLLRDVPA SGAYLATYEF LMRSMTSSDD TGELSVSKTL
LAGGVAGLAN WAVALPQDVL KSRLQIAPSG MYPNGMRDVA RQLIREEGPL ALYRGFTPVM
LRAFPANADY IHSRLQKHSV RVHVPIMGFQ EFTGYFLIAF GTPLAIFLRV IMHDPMRIIL
FVGAAFFYML SILVAAIIWF ILPHFDGMLC FTVFLFVFLQ EIIRYLYYQL IRRAQAGLDL
VTEGNEGVEG VHPLKHANHM ISFVIGMGFG SMAGIIALVN GLADSSGPGT VGLPSALKLS
DMHGSHHFFL ISSISVAALI LLHVMWNVII FHACDKKATW LAMFAIADHF LVTGISFYNR
SNAWAASLSC LYGSLLLFSG LAYAISGGNV KNVRLFIRCI FNPRLRAQNP PDVDQRF
//
