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Database: UniProt
Entry: A0A0M4EW43_DROBS
LinkDB: A0A0M4EW43_DROBS
Original site: A0A0M4EW43_DROBS 
ID   A0A0M4EW43_DROBS        Unreviewed;      1019 AA.
AC   A0A0M4EW43;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=CG10362 {ECO:0000313|EMBL:ALC49610.1};
GN   ORFNames=Dbus_chrXg1466 {ECO:0000313|EMBL:ALC49610.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC49610.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC49610.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC49610.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP012528; ALC49610.1; -; Genomic_DNA.
DR   RefSeq; XP_017852924.1; XM_017997435.1.
DR   AlphaFoldDB; A0A0M4EW43; -.
DR   STRING; 30019.A0A0M4EW43; -.
DR   GeneID; 108606902; -.
DR   OMA; RRTPYTH; -.
DR   OrthoDB; 3681901at2759; -.
DR   Proteomes; UP000494163; Chromosome x sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IEA:InterPro.
DR   GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IEA:InterPro.
DR   CDD; cd20825; C1_PDZD8; 1.
DR   CDD; cd21674; SMP_PDZD8; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR039275; PDZD8.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR031468; SMP_LBD.
DR   PANTHER; PTHR21519; PDZ DOMAIN-CONTAINING PROTEIN 8; 1.
DR   PANTHER; PTHR21519:SF1; PDZ DOMAIN-CONTAINING PROTEIN 8; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS51847; SMP; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00023055};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        7..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..273
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000259|PROSITE:PS51847"
FT   DOMAIN          340..410
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          716..766
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          468..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1019 AA;  112765 MW;  CBE92C74A6E8162D CRC64;
     MEIPISNILL LCLIFLLIGG VIMILLQYLI FIKFSNLPDE SEEQKQMNAK YTLPQNIKHT
     ARHLKTQIEG NNCEHKDNHA QDSSALASLN FVMQFLFHEF KNSNRVRKWF YRKLSIELDE
     LITKTTTGKL LDKLTIKELE LGDQFPDIKS MSVHNVQLDE AEQRIENLDL LLDINYIGNF
     STSIDADMVL GKKGSIMLKV KQLSGMARLQ FTRRPYTHWS LSFLGDPELN LVIESKYQGR
     QMQSNITNLI SNQIRKAVRR KHTLPNYKLR YKPFFHWTAD EEANDCDIQP NGRLTVRVAE
     LSRLMHWPGV AEVYCSITLA PVPFIEAQQR DNRHVLITLD VLVHKAKNQQ IGIVFKQSSG
     QAVKIESVLP NTPACKSNLQ SGDALVAIQG KPVSSIQQIA KVVKNLQSTV CSLRIERLIP
     GIIRNDAILE DLEKYDDLCD MRQQQQQQRL ESEEQLTAEL SAKHLAVKAR GSNDSSLSGT
     PTNSPKKSNI IAKAIKKTMS RESPDTQKDR ELREKPKVEE ASVALEEVNY FYQHSTIDCA
     FKELIHMDDV CHFQLDANSR YLNVCVFGKC AGERVLLGYN NIQISQVLGE CSETSLNQCL
     KQLALNPAAL INSKTHVLSN QSGFNPNLCF GDITFGFSWL GNPNATASDS SAAAKSSSSS
     SSGKSQSPAR NQASAVGAQD ELSAGGDSNS LKSGTLSADS AISSGTRSSD ASVSKAHNFI
     RTHFHRATQC DFCGKKIWLK DAMQCKDCAF CCHKKCIAKC QIATVCGPVD CISVGAISTQ
     PGGNSVVVNK PEFTITQADY EEDFEGGREE SPMEPALDVH RASLTGMLAQ GIKRQASNLD
     IPGIVSTLTG TGSSSPQLNS KSLPPSPQHT PCSRKVSISE EATALSNRSS SVNPFELVTP
     QLAALGAECT TLSYEQVSLL TEPILRHARH EDLMNLAKSY SKQLYAESPP TERVHKINEL
     LTNLKLALDA ETEGYSDAEE ATSQQHRMES KSEERVQALS IIMLYLCTGL QHAQGSVNA
//
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