ID A0A087XZI7_POEFO Unreviewed; 717 AA.
AC A0A087XZI7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Amyloid beta precursor like protein 2 {ECO:0000313|Ensembl:ENSPFOP00000011190.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000011190.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000011190.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the APP family. {ECO:0000256|PROSITE-
CC ProRule:PRU01217}.
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; AYCK01004877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01004878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01004879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007552389.1; XM_007552327.2.
DR AlphaFoldDB; A0A087XZI7; -.
DR STRING; 48698.ENSPFOP00000011190; -.
DR Ensembl; ENSPFOT00000011206.2; ENSPFOP00000011190.2; ENSPFOG00000011028.2.
DR GeneID; 103138217; -.
DR KEGG; pfor:103138217; -.
DR CTD; 334; -.
DR eggNOG; KOG3540; Eukaryota.
DR GeneTree; ENSGT00530000063252; -.
DR OMA; THRVQKC; -.
DR OrthoDB; 2907766at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-UniRule.
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; 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:SF14; AMYLOID BETA PRECURSOR LIKE PROTEIN 2; 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 PRINTS; PR00203; AMYLOIDA4.
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 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|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..717
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001833761"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..196
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 319..510
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 35..130
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 138..196
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 200..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 377..404
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 208..232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 80..124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 105..112
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 140..194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 151..181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 165..193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 717 AA; 81281 MW; 5A45F29CCC51B521 CRC64;
MGSVPAISAL VLGIVVPALA GYIEALAANA GTGLGAVEPQ VAMFCGKLNM HVNIQTGRWE
PDPSGTKSCV GTKEGVLQYC QEMYPDLKIT NVVEANQPVR IENWCKKEKK VCKGHAHIVV
PYMCLVGEFV SDVLLVPEKC KFFHKERMDL CISHQQWHAV AKEACSRSSM MLHSYGMLLP
CDIDKFHGTE YVCCPASRFA ESPPPSLPSQ EEDDDDEDEH VENEDVALGD DEPLEETVTK
ANKEPIQKEE AVDEDEDEEE EEEDEDEYNY VYGDEETNIN AEEEKEEKEE ESSNQPKKIK
QNQISLRKND FHPVAWSDDV DVYFETPADD KEHGRFQKAK EQLEVRHRNR MERVRKEWEE
ADRQARNIPR AERQTLVQHF QAMVESLEEE AASEKQQLVE THLARVEAML NDRRRVALEN
YLAALQADPP RPHRIMQALK KYVRAENKDR QHTVRHYQHV LAVDPEKAAQ MKSQVMTHLR
VIEERMNQSL SLLYKVPYVA EELQDEIDDL LQEQKADMDQ FLSSISESQP DVTVSSEESV
EVPVSEGKPY RPIQVTSLGA RSEPEGDLSD SPRAFKKGSA MAGLDGLIGA EERVINSKPK
MGEDLVIDES LDVNEVVYSA ERVSVMHGDE LPYRPLGEDF SIGYSNTALI GLLVIAVAIA
TVIVISLVLL RKRQYGTISH GIVEVDPMLT PEERHLNKMQ NHGYENPTYK YLEQMQI
//
