ID A0A3Q1EDN9_9TELE Unreviewed; 694 AA.
AC A0A3Q1EDN9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Amyloid-beta A4 protein {ECO:0000256|RuleBase:RU367156};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000000962.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000000962.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU367156};
CC Single-pass type I membrane protein {ECO:0000256|RuleBase:RU367156}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the APP family. {ECO:0000256|PROSITE-
CC 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 AlphaFoldDB; A0A3Q1EDN9; -.
DR Ensembl; ENSAPOT00000015984.1; ENSAPOP00000000962.1; ENSAPOG00000002239.1.
DR GeneTree; ENSGT00530000063252; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0005798; C:Golgi-associated vesicle; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 6.10.250.1670; -; 1.
DR Gene3D; 1.20.120.770; Amyloid precursor protein, E2 domain; 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; 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 3: Inferred from homology;
KW Amyloid {ECO:0000256|ARBA:ARBA00023087, ECO:0000256|RuleBase:RU367156};
KW Cell membrane {ECO:0000256|RuleBase:RU367156};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01217}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367156};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..694
FT /note="Amyloid-beta A4 protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018640016"
FT TRANSMEM 625..647
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367156"
FT DOMAIN 29..190
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 306..497
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 29..124
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 132..190
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 215..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..384
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 231..262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 74..118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 99..106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 134..188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 145..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 159..187
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 694 AA; 78324 MW; E8DBB94237AEF32F CRC64;
MGELTAFVLL LAATLTLSSE VPADDSVGLL TEPQVAMFCG KLNMHINVQS GKWESDPSGT
NSCTGTKEGI LQYCQEVYPE LQITNVVEAN QPVSIPNWCK KGRKQCRSHT HIVLPYRCLV
GEFVSDALLV PDKCKFLHQE RMDQCESHLH WHTVAKESCG DRYMNLHDYG MLLPCGIDRF
RGVEFVCCPA EVERESDSAE LDGEESDVWW GGAETEYSDN SMTRPSDTEP ATAEDDEDED
EEVDTFERDE NGDGDADDED DIDMTDERYS EERNANVAMT TTTTTTTESV EEVVRVPTMA
PSPPDAVDRY LESPGDDNEH TDFQKAKESL EAKHREKMSQ VMREWEEAER QAKNLPRADK
KAVIQHFQEK VEALEQEAAG ERQQLVETHM ARVEALLNSR RRLSLENYLS ALQANPPRPR
QVLSLLKKYV RAEQKDRQHT LKHYEHVRTV DPKKAAQIRP QVLTHLRVID ERMNQSLGLL
YKVPSVANEI QNQVAVIVQR VQSELSQQVS SLQSDGRVDG RVSYGNDALM PDQAYSSAPM
DPGLDGLGFI HPESFNQPNT ENHVEPVDAR PIPDRGLPTR PVSALKPEEM PEVRMETEER
QSTGYEVYHQ KLVFFAEDVG SNKGAIIGLM VGGVVIATVI VITLVMLRKK QYTSIHHGVI
EVDAAVTPEE RHLAKMQQNG YENPTYKFFE QMQN
//
