ID Q9DGJ8_CHICK Unreviewed; 695 AA.
AC Q9DGJ8;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Amyloid-beta A4 protein {ECO:0000256|RuleBase:RU367156};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|EMBL:AAG00593.1};
RN [1] {ECO:0000313|EMBL:AAG00593.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16039787; DOI=10.1016/j.neuroscience.2005.05.020;
RA Carrodeguas J.A., Rodolosse A., Garza M.V., Sanz-Clemente A., Perez-Pe R.,
RA Lacosta A.M., Dominguez L., Monleon I., Sanchez-Diaz R., Sorribas V.,
RA Sarasa M.;
RT "The chick embryo appears as a natural model for research in beta-amyloid
RT precursor protein processing.";
RL Neuroscience 134:1285-1300(2005).
CC -!- FUNCTION: Functions as a cell surface receptor and performs
CC physiological functions on the surface of neurons relevant to neurite
CC growth, neuronal adhesion and axonogenesis.
CC {ECO:0000256|RuleBase:RU367156}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU367156}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU367156}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
CC -!- SIMILARITY: Belongs to the APP family. {ECO:0000256|ARBA:ARBA00009449,
CC ECO:0000256|PROSITE-ProRule:PRU01217, ECO:0000256|RuleBase:RU367156}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01217}.
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DR EMBL; AF289218; AAG00593.1; -; mRNA.
DR AlphaFoldDB; Q9DGJ8; -.
DR SMR; Q9DGJ8; -.
DR VEuPathDB; HostDB:geneid_374198; -.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005798; C:Golgi-associated vesicle; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-UniRule.
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:0008344; P:adult locomotory behavior; ISS:UniProtKB.
DR GO; GO:0008088; P:axo-dendritic transport; ISS:UniProtKB.
DR GO; GO:0016199; P:axon midline choice point recognition; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0048669; P:collateral sprouting in absence of injury; ISS:UniProtKB.
DR GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; ISS:UniProtKB.
DR GO; GO:0006878; P:intracellular copper ion homeostasis; ISS:UniProtKB.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR GO; GO:0007617; P:mating behavior; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0016322; P:neuron remodeling; ISS:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
DR GO; GO:0050803; P:regulation of synapse structure or activity; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0008542; P:visual learning; ISS:UniProtKB.
DR Gene3D; 1.20.120.770; Amyloid precursor protein, E2 domain; 1.
DR Gene3D; 4.10.230.10; Amyloidogenic glycoprotein, amyloid-beta peptide; 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; 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; 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:SF7; AMYLOID-BETA PRECURSOR 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 Pfam; PF03494; Beta-APP; 1.
DR PRINTS; PR00203; AMYLOIDA4.
DR PRINTS; PR00204; BETAAMYLOID.
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 2: Evidence at transcript level;
KW Amyloid {ECO:0000256|ARBA:ARBA00023087, ECO:0000256|RuleBase:RU367156};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367156};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01217}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367156};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367156};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367156}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..695
FT /note="Amyloid-beta A4 protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004326015"
FT TRANSMEM 626..648
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367156"
FT DOMAIN 28..189
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 299..490
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 28..123
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 131..189
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 196..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 324..384
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 196..210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..264
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 73..117
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 98..105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 133..187
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 144..174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 158..186
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 695 AA; 78566 MW; F201ED02AEC86D95 CRC64;
MLPHLALLLL AAGAARALEV PADGNAGLLA EPQIAMFCGK LNMHMNVQNG KWESDPSGTK
TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GWKQCNGHPH IVVPYRCLVG
EFVSDALLVP DKCKLLHQER MDVCETHLHW HTVAKESCSE KSMNLHDYGM LLPCGIDKFR
GVEFVCCPLA EESDNLDSAD AEDDDSDVWW GGADADYADG SDDKVVEEQP EEDEELTVVE
DEDADDDDDD DGDEIEETEE EYEEATERTT SIATTTTTTT ESVEEVVRVP TTAASTPDAV
DKYLETPGDE NEHAHFQKAK ERLEAKHRER MSQVMREWEE AERQAKNLPK ADKKAVIQHF
QEKVESLEQE AANERQQLVE THMARVEAML NDRRRIALEN YITALQTVPP RPRHVFNMLK
KYVRAEQKDR QHTLKHFEHV RMVDPKKAAQ IRSQVMTHLR VIYERMNQSL SFLYNVPAVA
EEIQDEVDEL LQKEQNYSDD VLANMISEPR ISYGNDALMP SLTETKTTVE LLPVDGEFSL
DDLQPWHPFG VDSVPANTEN EVEPVDARPA ADRGLTTRPG SGLTNVKTEE VSEVKMDAEF
RHDSGYEVHH QKLVFFAEDV GSNKGAIIGL MVGGVVIATV IVITLVMLKK KQYTSIHHGV
VEVDAAVTPE ERHLSKMQQN GYENPTYKFF EQMQN
//
