ID Q4ZHV6_MANSE Unreviewed; 804 AA. AC Q4ZHV6; DT 07-JUN-2005, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 3. DT 29-MAY-2024, entry version 63. DE SubName: Full=Beta amyloid protein-like protein {ECO:0000313|EMBL:AAY25024.3}; OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; OC Sphingidae; Sphinginae; Sphingini; Manduca. OX NCBI_TaxID=7130 {ECO:0000313|EMBL:AAY25024.3}; RN [1] {ECO:0000313|EMBL:AAY25024.3} RP NUCLEOTIDE SEQUENCE. RX PubMed=16229831; DOI=10.1016/j.ydbio.2005.09.029; RA Swanson T.L., Knittel L.M., Coate T.M., Farley S.M., Snyder M.A., RA Copenhaver P.F.; RT "The insect homologue of the amyloid precursor protein interacts with the RT heterotrimeric G protein Go alpha in an identified population of migratory RT neurons."; RL Dev. Biol. 288:160-178(2005). RN [2] {ECO:0000313|EMBL:AAY25024.3} RP NUCLEOTIDE SEQUENCE. RA Swanson T.L., Knittel L.M., Coate T.M., Farley S.M., Snyder M.A., RA Copenhaver P.F.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- INTERACTION: CC Q4ZHV6; P53359; NbExp=5; IntAct=EBI-8838689, EBI-8838702; 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 EMBL; DQ008058; AAY25024.3; -; mRNA. DR AlphaFoldDB; Q4ZHV6; -. DR IntAct; Q4ZHV6; 2. DR EnsemblMetazoa; XM_030181274.2; XP_030037134.1; LOC115452680. DR OrthoDB; 2907766at2759; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043005; C:neuron projection; IEA:TreeGrafter. DR GO; GO:0043025; C:neuronal cell body; IEA:TreeGrafter. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-UniRule. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR GO; GO:0007409; P:axonogenesis; IEA:TreeGrafter. DR GO; GO:0007417; P:central nervous system development; IEA:TreeGrafter. 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 Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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 InterPro; IPR011993; PH-like_dom_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 PRINTS; PR00203; AMYLOIDA4. 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 1: Evidence at protein level; 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 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..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..804 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004247556" FT TRANSMEM 731..754 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 25..192 FT /note="E1" FT /evidence="ECO:0000259|PROSITE:PS51869" FT DOMAIN 317..515 FT /note="E2" FT /evidence="ECO:0000259|PROSITE:PS51870" FT REGION 25..126 FT /note="GFLD subdomain" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" FT REGION 134..192 FT /note="CuBD subdomain" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" FT REGION 230..339 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 555..684 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 230..284 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 289..322 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 324..339 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 555..587 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 598..621 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 629..671 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 136..190 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" FT DISULFID 147..177 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" FT DISULFID 161..189 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" SQ SEQUENCE 804 AA; 88203 MW; C7222A7D39F73E57 CRC64; MTRAVLFISV FTIFLDVLHA GQASSGAEPQ VAVLCEAGST YHPQYMSAAG RWTPDLTTKP HNCLKDKMEI LDYCKKVYPS HDITNIVEAS HYVKVSNWCK LGTSNAAKCK VTRWVKPFRC LEGPFQSDAL LVPESCLFDH IHNQSRCWQF ARWNATAGRA CAQRGLRLRT FAMLLPCGIS LFSGVEFVCC PKHFKENVKM HKPMDVGVPV SPGGEDMLAA SAAMDERDDD LLDDDDALDD DDDDDTLNLS DDDDDDDADD DMDEDEDADL SRDDDAEDDD YTDADDSAWP RPESSSSPST TTSTTTTTTT TTASTATSDP YFSHFDPRTE HQSYKDAQQR LEETHREKIT KVMKEWSELE DRYQAMMSAD PAAAQTFRQR MTAKFQANVQ SLEEEGVAER RRLAALHQQR VLAHLAQRRR TALACYTRSL RDTPPNAHRV QKCLQRLVRA LAAERSGALA AWRRAAAAGR EAAAAERTSA ADRLQDADRA LQRALTALRR RPHLYASIGT AIEDYVQSMQ SKDDMAVSLM SMTPEAEELL LDRIEAEVQR EQAAREQLSV KRDQRARQRQ DIQNERAKTS NGVKESEESD DEASEPSENE TSTAAPTPTS APSSPASATP APSAAPVSVH DITTRSGFTQ DTTTTEMITT TVTDAPESET AETIEASETT SRRSTSETEG EGLRAALEHA EERAPPPPAH ALKHELQHSQ PGYTVRGAGP SGAGGAGGSG ALYPALCVGG AALAAAACVA LAVARRRDRA PHAQGFVQVE QTGVVAPTPE ERHVANMQIN GYENPTYKYF EVKE //