ID I3J3N3_ORENI Unreviewed; 708 AA.
AC I3J3N3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Amyloid beta precursor like protein 1 {ECO:0000313|Ensembl:ENSONIP00000003473.2};
GN Name=APLP1 {ECO:0000313|Ensembl:ENSONIP00000003473.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000003473.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000003473.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; I3J3N3; -.
DR STRING; 8128.ENSONIP00000042813; -.
DR Ensembl; ENSONIT00000003474.2; ENSONIP00000003473.2; ENSONIG00000002769.2.
DR eggNOG; KOG3540; Eukaryota.
DR GeneTree; ENSGT00530000063252; -.
DR HOGENOM; CLU_014607_2_1_1; -.
DR TreeFam; TF317274; -.
DR Proteomes; UP000005207; Linkage group LG11.
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 CDD; cd21708; JMTM_APLP1; 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; 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:SF13; AMYLOID BETA PRECURSOR LIKE PROTEIN 1; 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 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:UP000005207};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..708
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025507126"
FT TRANSMEM 640..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..190
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 335..526
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 30..125
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 133..190
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 193..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..285
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 75..119
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 100..107
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 146..176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 708 AA; 81715 MW; 114CB8ABFA6F0369 CRC64;
LVSSLFLYIF PFLFRSLALA MAEVNGPVPQ VAEPQIAMFC GRQLLHMNTQ TGQWEPDPQG
RQGCFKEPSQ IQSYCQEMYP GLSISHIEES KRPVTIPAWC KKGWGHCQTH PFIVLPYRCL
EGEYVSEALL VPDRCRFLHK EQMDVCESFV YWHNIAKEEC TSDNLELHSY GLLLPCGDHY
RGVEYVCCPG RGSSGDKGDA EERDVPAGPK TLAFQTSGKL SSVTKVTAPT PSPFPEIDLD
DDLEFEDNEV VEDEDEDEEQ EEEEEEEVDE DEAEGEEEEE EMATKDTEYE YPIDSGPYQT
SDYLDTFYYE KSQKPTTSSP LMKGDSLTTA RPTDGVDVYF EKPVDDTEHA NFLRAKTDLE
ERRMKRINEI MKEWAEADNQ SKNLPRSERQ DLNEHFQSVL QTLEEQVAGE RQRLVETHLA
RVEAILNNNR RLALENYLTA VQSDPPQPER VLQALKRYMA AEQKDRRHTL RHYQHIVAVD
PQKAEQMKFQ VYTHLHVIEE RMNQSLALLY KDPTLAEELH SDIQELVRAE RGDISELMTT
SFSETRTTEE LLPADSEEEK DDEEEEERAF QNRPYPPRIE LQPNNKNDDE YDYTTSERGP
TYEYEEKINT SVELKQEIRP NEIARDELQP DALETFNRGA MVGLLVVAVA IAMVMVISLL
LVRRKPYGTI SHGIVEVDPM LTPEERQLNK MQNHGYENPT YKFFEQMN
//
