ID A0A2R8ZBQ3_PANPA Unreviewed; 760 AA. AC A0A2R8ZBQ3; DT 20-JUN-2018, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 1. DT 07-OCT-2020, entry version 13. DE RecName: Full=ABPP {ECO:0000256|ARBA:ARBA00018220}; DE AltName: Full=Alpha-secretase C-terminal fragment {ECO:0000256|ARBA:ARBA00019925}; DE AltName: Full=Amyloid precursor protein {ECO:0000256|ARBA:ARBA00017734}; DE AltName: Full=Amyloid-beta A4 protein {ECO:0000256|ARBA:ARBA00016844}; DE AltName: Full=Amyloid-beta precursor protein {ECO:0000256|ARBA:ARBA00021782}; DE AltName: Full=Amyloid-beta protein 40 {ECO:0000256|ARBA:ARBA00015458}; DE AltName: Full=Amyloid-beta protein 42 {ECO:0000256|ARBA:ARBA00015461}; DE AltName: Full=Beta-APP40 {ECO:0000256|ARBA:ARBA00013772}; DE AltName: Full=Beta-APP42 {ECO:0000256|ARBA:ARBA00013799}; DE AltName: Full=Beta-secretase C-terminal fragment {ECO:0000256|ARBA:ARBA00018669}; DE AltName: Full=C31 {ECO:0000256|ARBA:ARBA00022319}; DE AltName: Full=C80 {ECO:0000256|ARBA:ARBA00022224}; DE AltName: Full=C83 {ECO:0000256|ARBA:ARBA00022212}; DE AltName: Full=C99 {ECO:0000256|ARBA:ARBA00022287}; DE AltName: Full=Gamma-CTF(50) {ECO:0000256|ARBA:ARBA00020145}; DE AltName: Full=Gamma-CTF(57) {ECO:0000256|ARBA:ARBA00019658}; DE AltName: Full=Gamma-CTF(59) {ECO:0000256|ARBA:ARBA00019677}; DE AltName: Full=Gamma-secretase C-terminal fragment 50 {ECO:0000256|ARBA:ARBA00014948}; DE AltName: Full=Gamma-secretase C-terminal fragment 57 {ECO:0000256|ARBA:ARBA00014942}; DE AltName: Full=Gamma-secretase C-terminal fragment 59 {ECO:0000256|ARBA:ARBA00014941}; DE AltName: Full=N-APP {ECO:0000256|ARBA:ARBA00015496}; DE AltName: Full=P3(40) {ECO:0000256|ARBA:ARBA00017924}; DE AltName: Full=P3(42) {ECO:0000256|ARBA:ARBA00017826}; DE AltName: Full=Soluble APP-alpha {ECO:0000256|ARBA:ARBA00020639}; DE AltName: Full=Soluble APP-beta {ECO:0000256|ARBA:ARBA00020817}; GN Name=APP {ECO:0000313|Ensembl:ENSPPAP00000002501}; OS Pan paniscus (Pygmy chimpanzee) (Bonobo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000002501, ECO:0000313|Proteomes:UP000240080}; RN [1] {ECO:0000313|Ensembl:ENSPPAP00000002501, ECO:0000313|Proteomes:UP000240080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=22722832; DOI=10.1038/nature11128; RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B., RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C., RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J., RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M., RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L., RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E., RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J., RA Paabo S.; RT "The bonobo genome compared with the chimpanzee and human genomes."; RL Nature 486:527-531(2012). RN [2] {ECO:0000313|Ensembl:ENSPPAP00000002501} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2018) to UniProtKB. CC -!- FUNCTION: N-APP binds TNFRSF21 triggering caspase activation and CC degeneration of both neuronal cell bodies (via caspase-3) and axons CC (via caspase-6). {ECO:0000256|ARBA:ARBA00003551}. CC -!- FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved CC peptides, including C31, are potent enhancers of neuronal apoptosis. CC {ECO:0000256|ARBA:ARBA00002651}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. CC Cell projection, growth cone {ECO:0000256|ARBA:ARBA00004624}. Cell CC surface {ECO:0000256|ARBA:ARBA00004241}. Cytoplasmic vesicle CC {ECO:0000256|ARBA:ARBA00004541}. Early endosome CC {ECO:0000256|ARBA:ARBA00004412}. Endosome CC {ECO:0000256|ARBA:ARBA00004177}. Membrane, clathrin-coated pit CC {ECO:0000256|ARBA:ARBA00004600}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. Perikaryon CC {ECO:0000256|ARBA:ARBA00004484}. Vesicle CC {ECO:0000256|ARBA:ARBA00004373}. CC -!- SIMILARITY: Belongs to the APP family. {ECO:0000256|ARBA:ARBA00009449}. 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; AJFE02056590; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJFE02056591; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJFE02056592; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJFE02056593; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJFE02056594; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJFE02056595; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJFE02056596; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJFE02056597; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJFE02065450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJFE02065451; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPPAT00000012046; ENSPPAP00000002501; ENSPPAG00000002732. DR GeneTree; ENSGT00530000063252; -. DR Proteomes; UP000240080; Chromosome 21. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell. DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0007399; P:nervous system development; IEA:InterPro. DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW. DR CDD; cd00109; KU; 1. 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 Gene3D; 4.10.230.10; -; 1. DR Gene3D; 4.10.410.10; -; 1. DR InterPro; IPR036669; Amyloid_Cu-bd_sf. DR InterPro; IPR008155; Amyloid_glyco. DR InterPro; IPR013803; Amyloid_glyco_Abeta. DR InterPro; IPR037071; Amyloid_glyco_Abeta_sf. 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; IPR028866; APP. DR InterPro; IPR019543; APP_amyloid_C. DR InterPro; IPR019744; APP_CUBD_CS. DR InterPro; IPR036176; E2_sf. DR InterPro; IPR002223; Kunitz_BPTI. DR InterPro; IPR036880; Kunitz_BPTI_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR020901; Prtase_inh_Kunz-CS. DR PANTHER; PTHR23103; PTHR23103; 1. DR PANTHER; PTHR23103:SF7; PTHR23103:SF7; 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 Pfam; PF03494; Beta-APP; 1. DR Pfam; PF00014; Kunitz_BPTI; 1. DR PRINTS; PR00203; AMYLOIDA4. DR PRINTS; PR00759; BASICPTASE. DR PRINTS; PR00204; BETAAMYLOID. DR SMART; SM00006; A4_EXTRA; 1. DR SMART; SM00131; KU; 1. DR SUPFAM; SSF109843; SSF109843; 1. DR SUPFAM; SSF56491; SSF56491; 1. DR SUPFAM; SSF57362; SSF57362; 1. DR SUPFAM; SSF89811; SSF89811; 1. DR PROSITE; PS00319; APP_CUBD; 1. DR PROSITE; PS00320; APP_INTRA; 1. DR PROSITE; PS00280; BPTI_KUNITZ_1; 1. DR PROSITE; PS50279; BPTI_KUNITZ_2; 1. PE 3: Inferred from homology; KW Amyloid {ECO:0000256|ARBA:ARBA00023087}; KW Coated pit {ECO:0000256|ARBA:ARBA00023176}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Copper {ECO:0000256|ARBA:ARBA00023008}; KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Endocytosis {ECO:0000256|ARBA:ARBA00022583}; KW Endosome {ECO:0000256|ARBA:ARBA00022753}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976}; KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690}; KW Reference proteome {ECO:0000313|Proteomes:UP000240080}; KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Sulfation {ECO:0000256|ARBA:ARBA00022641}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 691..713 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 281..331 FT /note="BPTI/Kunitz inhibitor" FT /evidence="ECO:0000259|PROSITE:PS50279" FT REGION 184..274 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 389..409 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 415..449 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 545..565 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 185..200 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 215..253 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 257..274 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 760 AA; 86077 MW; BAAF0A30E0C1593C CRC64; MLPSLFFFQV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSVMSQSLL KTTQEPLARD PVKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL QAVPPRPRHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET KTTVELLPVN GEFSLDDLQP WHSFGADSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN IKTEEISEVK MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN //