ID   Q95TH2_DROME            Unreviewed;       699 AA.
AC   Q95TH2;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   SubName: Full=SD05126p {ECO:0000313|EMBL:AAL13999.1};
GN   ORFNames=CG17019 {ECO:0000313|EMBL:AAL13999.1,
GN   ECO:0000313|FlyBase:FBgn0033783};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AAL13999.1};
RN   [1] {ECO:0000313|EMBL:AAL13999.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA   Chavez C., Dorsett V., Farfan D., Frise E., George R., Gonzalez M.,
RA   Guarin H., Li P., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.,
RA   Paragas V., Park S., Phouanenavong S., Wan K., Yu C., Lewis S.E.,
RA   Rubin G.M., Celniker S.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
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DR   EMBL; AY058770; AAL13999.1; -; mRNA.
DR   AlphaFoldDB; Q95TH2; -.
DR   AGR; FB:FBgn0033783; -.
DR   FlyBase; FBgn0033783; CG17019.
DR   VEuPathDB; VectorBase:FBgn0033783; -.
DR   HOGENOM; CLU_383667_0_0_1; -.
DR   OrthoDB; 383715at2759; -.
DR   ExpressionAtlas; Q95TH2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; IBA:GO_Central.
DR   CDD; cd15750; FYVE_CARP; 1.
DR   CDD; cd16500; RING-HC_CARP; 1.
DR   Gene3D; 1.10.720.140; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR14879; CASPASE REGULATOR, RING FINGER DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR14879:SF5; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          652..687
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          139..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   699 AA;  76963 MW;  9FBAB90337B4696B CRC64;
     MPCESCGVEF TVFRRKRACF DCKRYYCANC IASRRCKRCS VFAQRPLSRT DLLKLKPKDL
     IFYLQSKHIS TEGCLEKEEL VGLVLTHVAQ VDRSRGSNAS SNSPGRGQAN PIDSLKQSCQ
     NFFSNLSDNI SDSLASFDSK ITTKPPESRQ PEVPTHIFEQ PRVSTREIPT YASAVNGGPQ
     HVHVQQQATT TNGGSQSSSS PSTSTQASNN RDASSSSQAH VAHQEARNEE QKDAQSKSDC
     ECSDEEIMAT FSERVSMSLK TDTSGRRVNA AAEPSPVDLA NGDNGPAGNT APSPGCSKSG
     SSSSKADASS QSSFEELGAI GGISDESKAN TDTNSSHLDQ WQVLEVNRIE AVEETPTTSA
     ADEILEVTLR SRPAVEGDDS EMGESTQALN VNQRPANPSP AFYPAVPQRT KVTRRRSDGY
     LNRRYHSSDD ESPVAPGGPG LSLGLSTLSE HPEHGLHPHS HRQSCQRCGK NKTNIRRHVE
     KMRRHLENSQ MSEEDIKREL QEFLTYLEQR TKSVDASDAD SHAVSPLSVD AISVAAGGRS
     PDMPITPTIE FSPTQDDDIR WDDDEGIHVY AAPSDFEPTA GIDSRFVNLE DFEDLKDLEG
     LTVKQLKEVL MLHRVDYKGC CEKQELLDRV SRLWKTMREC PAVEKLATDE LCKICMDAPI
     ECVFLECGHM ATCTSCGKVL NECPICRQYI VRVVRFFRA
//