ID A0A2K5WP61_MACFA Unreviewed; 646 AA.
AC A0A2K5WP61;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Amyloid beta precursor like protein 1 {ECO:0000313|Ensembl:ENSMFAP00000038804.1};
GN Name=APLP1 {ECO:0000313|Ensembl:ENSMFAP00000038804.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000038804.1, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000038804.1, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000038804.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
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}.
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; A0A2K5WP61; -.
DR Ensembl; ENSMFAT00000013061.2; ENSMFAP00000038804.1; ENSMFAG00000038687.2.
DR VEuPathDB; HostDB:ENSMFAG00000038687; -.
DR GeneTree; ENSGT00530000063252; -.
DR Proteomes; UP000233100; Chromosome 19.
DR Bgee; ENSMFAG00000038687; Expressed in frontal cortex and 4 other cell types or tissues.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0005886; C:plasma 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; 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 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 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:UP000233100};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 577..599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..206
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 289..480
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 44..140
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 148..206
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 208..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 150..204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 161..191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 175..203
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 646 AA; 72016 MW; D556B4DFAF322413 CRC64;
MEAVCGAWGR GLVLGVSVLG SKEPGDPHAN APRALIIPST SIQAQGSAQV AGLCGRLTLH
RDLRTGRWEP DPQRSRRCLR DPQRVLEYCR QMYPELQIAR VEQATQAIPM ERWCGGARSG
SCTHPHHQVV PFRCLPGEFV SEALLVPEGC RFLHQERMDQ CESSTRRHQE AQEACSSQGL
ILHGSGMLLP CGSDRFRGVE YVCCPPPGTP DPSGTAVGDP STRSWPPGSR VEGAEDEEEE
ESFPQPVDDY FVEPPQAEEE EKEERVPPPS SHTLAVVSKV TPTPRPTDGV DIYFGMPGEI
SEHEGFLRAK MDLEERRMRQ INEVMREWAM ADNQSKNLPK ADRQALNEHF QSILQTLEEQ
VSGERQRLVE THATRVIALI NDQRRAALEG FLAALQGDPP QAERVLTALR HYLRAEQKEQ
RHTLRHYQHV AAVDPEKAQQ MRFQVQTHLQ VIEERVNQSL GLLDQNPHLA QELRPQIQEL
LHSEYLGPSE LEAPAPGGSS EDKGGLQPPD SKDDTPMTLP KGSTEQDAAS PEKEKMSPLE
QYEQKVNASV PRGFPFHSSE IQRDELAPAG TGVSREAVSG LLIMGAGGGS LIVLSMLLLR
RKKPYGAISH GVVEVDPMLT LEEQQLRELQ RHGYENPTYR FLEERP
//
