GenomeNet

Database: UniProt
Entry: A0A6I8VI41_DROPS
LinkDB: A0A6I8VI41_DROPS
Original site: A0A6I8VI41_DROPS 
ID   A0A6I8VI41_DROPS        Unreviewed;       938 AA.
AC   A0A6I8VI41;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Amyloid-beta-like protein isoform X6 {ECO:0000313|RefSeq:XP_015041408.2};
GN   Name=LOC4815376 {ECO:0000313|RefSeq:XP_015041408.2};
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_015041408.2};
RN   [1] {ECO:0000313|RefSeq:XP_015041408.2}
RP   IDENTIFICATION.
RC   STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_015041408.2};
RC   TISSUE=Whole body {ECO:0000313|RefSeq:XP_015041408.2};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the APP family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01217}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01217}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_015041408.2; XM_015185922.2.
DR   AlphaFoldDB; A0A6I8VI41; -.
DR   Proteomes; UP000001819; Chromosome X.
DR   ExpressionAtlas; A0A6I8VI41; baseline.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   Gene3D; 1.20.120.770; Amyloid precursor protein, E2 domain; 1.
DR   Gene3D; 3.30.1490.140; Amyloidogenic glycoprotein, copper-binding domain; 1.
DR   Gene3D; 3.90.570.10; Amyloidogenic glycoprotein, heparin-binding domain; 1.
DR   InterPro; IPR036669; Amyloid_Cu-bd_sf.
DR   InterPro; IPR008155; Amyloid_glyco.
DR   InterPro; IPR011178; Amyloid_glyco_Cu-bd.
DR   InterPro; IPR024329; Amyloid_glyco_E2_domain.
DR   InterPro; IPR008154; Amyloid_glyco_extra.
DR   InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR   InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
DR   InterPro; IPR019745; Amyloid_glyco_intracell_CS.
DR   InterPro; IPR019543; APP_amyloid_C.
DR   InterPro; IPR019744; APP_CUBD_CS.
DR   InterPro; IPR036176; E2_sf.
DR   PANTHER; PTHR23103; ALZHEIMER'S DISEASE BETA-AMYLOID RELATED; 1.
DR   PANTHER; PTHR23103:SF15; AMYLOID-BETA-LIKE PROTEIN; 1.
DR   Pfam; PF10515; APP_amyloid; 1.
DR   Pfam; PF12924; APP_Cu_bd; 1.
DR   Pfam; PF12925; APP_E2; 1.
DR   Pfam; PF02177; APP_N; 1.
DR   SMART; SM00006; A4_EXTRA; 1.
DR   SUPFAM; SSF56491; A heparin-binding domain; 1.
DR   SUPFAM; SSF89811; Amyloid beta a4 protein copper binding domain (domain 2); 1.
DR   SUPFAM; SSF109843; CAPPD, an extracellular domain of amyloid beta A4 protein; 1.
DR   PROSITE; PS00319; APP_CUBD; 1.
DR   PROSITE; PS51869; APP_E1; 1.
DR   PROSITE; PS51870; APP_E2; 1.
DR   PROSITE; PS00320; APP_INTRA; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU01217}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001819};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..938
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5026256862"
FT   TRANSMEM        863..885
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..203
FT                   /note="E1"
FT                   /evidence="ECO:0000259|PROSITE:PS51869"
FT   DOMAIN          438..636
FT                   /note="E2"
FT                   /evidence="ECO:0000259|PROSITE:PS51870"
FT   REGION          33..137
FT                   /note="GFLD subdomain"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT   REGION          145..203
FT                   /note="CuBD subdomain"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT   REGION          235..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          662..707
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        282..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..327
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..758
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        147..201
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT   DISULFID        158..188
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT   DISULFID        172..200
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ   SEQUENCE   938 AA;  103261 MW;  8A3675B347984B8B CRC64;
     MCAALRQRNL WLRSLWAVAV VVLAIGTVQG ASPRWEPQIA VLCEAGQIYQ PQYLSEEGRW
     VTDLSKKTTG ATCLRDKMDL LDYCKKAYPN RDITNIVESS HYQKIGGWCR QGALNAAKCK
     GSHRWIKPFR CLEGPFQSDA LLVPEGCLFD HIHNASRCWP FVRWNQTGAA ACQERGMQMR
     SFAMLLPCGI SLFSGVEFVC CPKHFKTDEI HVKKTDLPVM PPAQISSAND ELNLNANEED
     DSNDSNYSKD ANDDELDDED DLMADDEEDE MVADEAAAAG GTGTGTGSSS AATGDASSGS
     LDDINAEYDS GEDGDNYEED GAGSEGDNDS DTWDQNGSSS GAKPVGLKVP IFSMASSSSS
     PSSLPVGSDA IGSSGKTPVK PDQVTRIPIY SPAQAAAKDA AISNANHINR LAAAAAAAAS
     AAAATGAAGA PPSTAQPTSD PYFTHFDPHY EHQSYKRLEE SHREKVTRVM KDWSDLEEKY
     QDMRLADPKA AQSFKQRMTA RFQTSVQALE EEGNAEKHQL AAMHQQRVLA HINQRKREAM
     TCYTQALTEQ PPNAHHVEKC LQKLLRALHK DRAHALAHYR HLLNSGGPGG LEAAASERPR
     TLERLIDIDR AVNQSMTMLK RYPELSAKIA QLMNDYILAL RSKDDIPGSS LGMSEEAEAG
     ILDKYRIEIE RKVAEKERLR LAEKQRKEQR AAEREKLREE KLRMEAKKVD DMLKSQAAEQ
     QSQSPSQFQS SSQSQSPAQL QAQQQQQQSQ QQDKSINSKE LGIDGGLVTA ANLNLDTTKS
     EKDLADAEYA EATVSTKVQT VLPTVDDDAV QRAVEDVAAA VAHQEAEPQV QHFMTHDLGH
     RESSFSLRRE FAHAHAAKEG RNVYFTLSFA GIALMAAVFV GVAVAKWRTS RSPHAQGFIE
     VDQNVTTHHP IVQEEKIVPN MQINGYENPT YKYFEVKE
//
DBGET integrated database retrieval system