A4_TAKRU
ID A4_TAKRU Reviewed; 737 AA.
AC O93279;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Amyloid-beta A4 protein;
DE AltName: Full=ABPP;
DE Short=APP;
DE AltName: Full=Alzheimer disease amyloid A4 protein homolog;
DE AltName: Full=Amyloid precursor protein {ECO:0000305};
DE AltName: Full=Amyloid-beta precursor protein {ECO:0000305};
DE Contains:
DE RecName: Full=Amyloid-beta protein;
DE AltName: Full=A-beta;
DE AltName: Full=APP-beta;
DE Flags: Precursor;
GN Name=app;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9599080; DOI=10.1016/s0378-1119(98)00032-8;
RA Villard L., Tassone F., Crnogorac-Jurcevic T., Clancy K., Gardiner K.;
RT "Analysis of pufferfish homologues of the AT-rich human APP gene.";
RL Gene 210:17-24(1998).
CC -!- FUNCTION: Functional neuronal receptor which couples to intracellular
CC signaling pathway through the GTP-binding protein G(O). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the APP family. {ECO:0000255|PROSITE-
CC ProRule:PRU01217}.
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DR EMBL; AF090120; AAD13392.1; -; Genomic_DNA.
DR AlphaFoldDB; O93279; -.
DR SMR; O93279; -.
DR STRING; 31033.ENSTRUP00000027587; -.
DR eggNOG; KOG3540; Eukaryota.
DR InParanoid; O93279; -.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IEA:InterPro.
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:0007399; P:nervous system development; IEA:InterPro.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IEA:UniProt.
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; 4.10.410.10; -; 1.
DR InterPro; IPR036669; Amyloid_Cu-bd_sf.
DR InterPro; IPR008155; Amyloid_glyco.
DR InterPro; IPR013803; Amyloid_glyco_Abeta.
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; PS51869; APP_E1; 1.
DR PROSITE; PS51870; APP_E2; 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; Copper; Disulfide bond; Glycoprotein; Membrane; Metal-binding;
KW Protease inhibitor; Reference proteome; Serine protease inhibitor; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..737
FT /note="Amyloid-beta A4 protein"
FT /id="PRO_0000000197"
FT CHAIN 639..681
FT /note="Amyloid-beta protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000000198"
FT TOPO_DOM 19..668
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..737
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..190
FT /note="E1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DOMAIN 286..344
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 354..545
FT /note="E2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01218"
FT REGION 29..124
FT /note="GFLD subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT REGION 132..190
FT /note="CuBD subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT REGION 193..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..729
FT /note="Clathrin-binding"
FT /evidence="ECO:0000250"
FT MOTIF 724..729
FT /note="YENPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT COMPBIAS 195..209
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..260
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT BINDING 152
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT BINDING 169
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT SITE 171
FT /note="Required for Cu(2+) reduction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT SITE 300..301
FT /note="Reactive bond"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 74..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 99..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 134..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 145..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 159..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 290..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 299..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 315..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 737 AA; 82857 MW; 6FAD01E2E3B2B7E2 CRC64;
MGETTAFVLL LVATLTRSSE IPADDTVGLL TEPQVAMFCG KLNMHINVQN GKWESDPSGT
KSCLNTKEGI LQYCQEVYPE LQITNVVEAN QPVSIQNWCK KGRKQCRSHT HIVVPYRCLV
GEFVSDALLV PDKCKFLHQE RMNQCESHLH WHTVAKESCG DRSMNLHDYG MLLPCGIDRF
RGVKFVCCPA ETEQETDSSE VEGEESDVWW GGADPEYSEN SPPTPSRATY VAGDAFERDE
NGDGDEDEED DEDVDPTDEQ ESDERTANVA MTTTTTTTTE SVEEVVRAVC WAQAESGPCR
AMLERWYFNP KKRRCVPFLF GGCGGNRNNF ESEEYCLAVC SSSLPTVAPS PPDAVDQYFE
APGDDNEHAD FRKAKESLEA KHRERMSQVM REWEEAERQA KNLPRADKKA VIQHFQEKVE
ALEQEAAGER QQLVETHMAR VEALLNSRRR LTLENYLGAL QANPPRARQV LSLLKKYVRA
EQKDRQHTLK HYEHVRTVDP KKAAQIRPQV LTHLRVIDER MNQSLALLYK VPSVASEIQN
QIYPAAGSDC KDPVEHCVCP QVDGLVSYGN DALMPDQAYS SAPMDMGVDG LGSIDQSFNQ
ANTENHVEPV DARPIPDRGL PTRPVSSLKL EEMPEVRTET DKRQSAGYEV YHQKLVFFAD
DVGSNKGAII GLMVGGVVIA TVIVITLVML RKKQYTSIHH GVIEVDAAVT PEERHLARMQ
QNGYENPTYK FFEQMQN
