ID A0A3Q2HIF9_HORSE Unreviewed; 793 AA. AC A0A3Q2HIF9; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 12-AUG-2020, entry version 8. DE RecName: Full=ABPP {ECO:0000256|ARBA:ARBA00018220}; DE AltName: Full=Alpha-secretase C-terminal fragment {ECO:0000256|ARBA:ARBA00019925}; DE AltName: Full=Alzheimer disease amyloid A4 protein homolog {ECO:0000256|ARBA:ARBA00021367}; 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:ENSECAP00000032992, GN ECO:0000313|VGNC:VGNC:15428}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000032992, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000032992, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000032992, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O., RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T., RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T., RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S., RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G., RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R., RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000032992} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000032992}; RG Ensembl; RL Submitted (JAN-2019) 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 Ensembl; ENSECAT00000031786; ENSECAP00000032992; ENSECAG00000021011. DR VGNC; VGNC:15428; APP. DR GeneTree; ENSGT00530000063252; -. DR Proteomes; UP000002281; Chromosome 26. DR ExpressionAtlas; A0A3Q2HIF9; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008201; F:heparin binding; IEA:InterPro. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR GO; GO:0007399; P:nervous system development; IEA:InterPro. DR CDD; cd00109; KU; 1. DR Gene3D; 1.20.120.770; -; 2. 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; 2. DR PANTHER; PTHR23103:SF7; PTHR23103:SF7; 2. DR Pfam; PF10515; APP_amyloid; 1. DR Pfam; PF12924; APP_Cu_bd; 1. DR Pfam; PF12925; APP_E2; 2. 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; 2. 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 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:UP000002281}; KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}; 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..17 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 18..793 FT /note="ABPP" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5018645516" FT TRANSMEM 724..746 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 291..341 FT /note="BPTI/Kunitz inhibitor" FT /evidence="ECO:0000259|PROSITE:PS50279" FT REGION 194..284 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 466..500 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 596..616 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 195..210 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 225..263 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 267..284 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 793 AA; 89742 MW; DB87BD4953F3E252 CRC64; MLPGLALVLL AAWTARALEV PTDGNAGLLA EPQIAMFCGK LNMHMNVQNG KWESDPSGTK TCIGTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHAH IVIPYRCLVG EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEDVADVEEE EAEDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSVMSQSLL KTPQEPLPQD PVKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQAQ LQTFPLAFGS VHELISRKSW VDIKDEKRKL YFPTKQISLV MREWEEAERQ AKNLPKADKK AVIQHFQEKV ESLEQEAANE RQQLVETHMA RVEAMLNDRR RLALENYITA LQAVPPRPRH VFNMLKKYVR AEQKDRQHTL KHFEHVRMVD PKKAAQIRSQ VMTHLRVIYE RMNQSLSLLY NVPAVAEEIQ DEVDELLQKE QNYSDDVLAN MISEPRISYG NDALMPSLTE TKTTVELLPV NGEFSLDDLQ PWHPFGVDSV PANTENEGSG LTNIKTEEIS EVKMDAEFRH DSGYEVHHQK LVFFAEDVGS NKGAIIGLMV GGVVIATVIV ITLVMLKKKQ YTSIHHGVVE VDAAVTPEER HLSKMQQNGY ENPTYKFFEQ MQN //