ID A0A673Y4E6_SALTR Unreviewed; 770 AA.
AC A0A673Y4E6;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Amyloid-beta A4 protein {ECO:0000256|RuleBase:RU367156};
GN Name=APP {ECO:0000313|Ensembl:ENSSTUP00000029390.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000029390.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000029390.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A673Y4E6; -.
DR Ensembl; ENSSTUT00000030761.1; ENSSTUP00000029390.1; ENSSTUG00000006124.1.
DR GeneTree; ENSGT00530000063252; -.
DR Proteomes; UP000472277; 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 CDD; cd22607; Kunitz_ABPP-like; 1.
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; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz 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; 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; 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 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; SSF56491; A heparin-binding domain; 1.
DR SUPFAM; SSF89811; Amyloid beta a4 protein copper binding domain (domain 2); 1.
DR SUPFAM; SSF57362; BPTI-like; 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.
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, 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000472277};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..770
FT /note="Amyloid-beta A4 protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025567310"
FT TRANSMEM 701..723
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367156"
FT DOMAIN 39..200
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 312..362
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 376..567
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 39..134
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 142..200
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 201..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 401..461
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 557..584
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 240..283
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 84..128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 109..116
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 144..198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 155..185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 169..197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 770 AA; 87242 MW; DE39AE74A3E40FD8 CRC64;
SSPYFSIFVL LLFLKLTSLF VSPPSLPPLK VPTDGGMGLL AEPQVAMFCG KLNMHVDVQS
GKWESDPSGT KSCIGTKEGI LQYCQEVYPE LQITNVVEAN QPVSVQNWCK KGRKQCRSHL
HIVVPYRCLV GEFVSDALLV PDKCKFLHQE RMDMCESHLH WHTVAKESCG DRTLNLHDYG
MLLPCGIDRF RGVEFVCCPS DRETDSTEQD EDDSDVWWGG AETDYTDNRY TQELIQEEEP
APAMLEEDDE VLDNDQDGDG DEDDDEEEEE DDDDDDDVID ERDDSEPTTN IAMTTTTTTT
TESVEEVVRE VCWSNAETGP CRAMLARWYF DHEEGRCAQF IYGGCGGNRN NFESEEYCLS
ICSNVMPTAA PSSPDAVDRY LETPGDDNEH AHFAKAKESL EAKHRERMSQ VMREWEEAER
EAKSLPRADK KAVIQRFQEK VEALEQEAAS ERQQLVETHM ARVEALLNDH RRLALESYLT
SLQAEPPRPR HVFSLLKKYV RAEQKDRQHT LKHFEHVRMV DPKKAAQIRP QVLTHLRVIE
ERMNQSLGLL YKVPGVADDI QDQVELLQKE QADMAQQLSN LQSDVRVSYG NDALMPNSLP
DSTRATLDLL PQEEDLDMGL DGLGFIHPES FNQVNTDIQV EPVDAGPIPD RGFPTRPVSG
LKPEEIPELR MEAEERHSTG FEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL
VMLRKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN
//
