ID A0A182P3Z6_9DIPT Unreviewed; 760 AA.
AC A0A182P3Z6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI001632-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI001632-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI001632-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A182P3Z6; -.
DR STRING; 199890.A0A182P3Z6; -.
DR EnsemblMetazoa; AEPI001632-RA; AEPI001632-PA; AEPI001632.
DR VEuPathDB; VectorBase:AEPI001632; -.
DR OrthoDB; 2912447at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16476; RING-H2_RNF139-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR025754; TRC8_N_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22763:SF163; E3 UBIQUITIN-PROTEIN LIGASE RNF139; 1.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR Pfam; PF13705; TRC8_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 75..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 444..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 577..615
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 696..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 84782 MW; B8DFF101DAAB937A CRC64;
MSVVRTKVLG LVDVIMRVPS LFIIDEILKI GMGVPTGQST GQVANSTTIN LDPPVAAMLP
EDERGMQDSI EVYKFISFAV LKFLVCVFGA ISATCVFMLW TRHLVIVYMY IVSVGLIFLS
YWSNVSALSL ISDSPSLLED VLSLNMERLL DPGGVLISIL PHLLAQWLMG VIFAYIHLGP
RHKIVQKALP FSFLMPLLLA MLPLPSIVLK HSPAFAAILP LVLSKIALWS SSFDVVKTIL
SGYQHARNFA SNFGIATLIE NEWQRLNVPC VLRVFWTIRL SEHLISLLMS SEAPLRFAAM
VQSVLVSGCE TLTAVLGMTS IISLICHYIG KMFQLFLLSE DYDEDKSIGT VSAILFYILA
LQTGLTSLSP DKRIIRLCRN MCLLMTALLH FLHNIVAPIL MSLSAARNPS RKRHARALIV
CAFLLIAPGS LLAVLWASHS PSTWLLAVTA FSVEVIVKVL VSLATYTLFL LDARRQTFWE
KLDDYVYYIR AFGNSVEFCF GIFLFFNGAW ILIFESEMIP IGGAIRALMM GIHAYFNIWC
EARAGWVVFM KRRTAVHKIS SLPEATTAQL QQFDDVCAIC YQDMTSAKIT RCNHYFHGVC
LRKWLYVQDR CPLCHEIIMN QDGNPGDESI EEQANNTGST NRRIEARVGG AASDINNPQH
SAPQPTTILH GADQADAHTQ PLFDDQYLEE QINNLSRAAS ASRTQDDNVN GRSDVQADAS
KRTPLEEQYL EEYRLERLKF DMLHGTNANH NNPPGIALSN
//
