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}.
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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
//