ID Q4ZHV6_MANSE Unreviewed; 804 AA. AC Q4ZHV6; DT 07-JUN-2005, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 3. DT 12-AUG-2020, entry version 55. 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; Holometabola; 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. 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 IntAct; Q4ZHV6; 2. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008201; F:heparin binding; IEA:InterPro. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR Gene3D; 1.20.120.770; -; 1. DR Gene3D; 2.30.29.30; -; 1. DR Gene3D; 3.30.1490.140; -; 1. DR Gene3D; 3.90.570.10; -; 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; PTHR23103; 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; SSF109843; SSF109843; 1. DR SUPFAM; SSF56491; SSF56491; 1. DR SUPFAM; SSF89811; SSF89811; 1. DR PROSITE; PS00319; APP_CUBD; 1. DR PROSITE; PS00320; APP_INTRA; 1. PE 2: Evidence at transcript level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW 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 21..191 FT /note="A4_EXTRA" FT /evidence="ECO:0000259|SMART:SM00006" 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 COILED 389..409 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 481..501 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 230..284 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 289..322 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 324..339 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 555..587 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 598..621 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 629..671 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 //