ID A0A665W3Q0_ECHNA Unreviewed; 725 AA.
AC A0A665W3Q0;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Amyloid beta precursor like protein 1 {ECO:0000313|Ensembl:ENSENLP00000038744.1};
GN Name=aplp1 {ECO:0000313|Ensembl:ENSENLP00000038744.1};
OS Echeneis naucrates (Live sharksucker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Echeneidae; Echeneis.
OX NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000038744.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000038744.1}
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 AlphaFoldDB; A0A665W3Q0; -.
DR Ensembl; ENSENLT00000039766.1; ENSENLP00000038744.1; ENSENLG00000016719.1.
DR InParanoid; A0A665W3Q0; -.
DR OMA; CLRDPQH; -.
DR Proteomes; UP000472264; Unplaced.
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:UP000472264};
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 657..679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 47..207
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 352..543
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 47..142
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 150..207
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 209..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..301
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 92..136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 117..124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 163..193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 725 AA; 83242 MW; AA71E93893F3238B CRC64;
IMSQYCLPLC YVQSVKWYQL LFISLPSLPP CAVQALAMAE VNGPGPQIPE PQIAVFCGRQ
LLHMNLQTGQ WEPDSQGRQG CFKEPSEVLS YCQEVYPALS ISHIEESKRP VTIHGWCKKG
WGRCQTRPFI VIPYRCLEGE YVSEALLVPD RCKFLHQEQM DACKSYIYWH NIAKEVCTAD
NLELHSYGML LPCGDHFRGV KYVCCPGRGS SSGKGETDER DVPVGPQTFT SQASGKLNSI
TKVTAPTPSP SPDTDMDEAD MEEEDDEVVE EEEEEEDEED EEEVDEEEAE EEEEEEEAMA
VKDQEYENPI DSGPYRTSDY LDPFFYKKSH KPTTPTPLTK GDSLTTPRPT DGVDVYFEKP
VDDTEHANFL RAKTDLEERR MKRINEIMKE WAEADNQSKN LPKSERQGLN EHFQSVLQTL
EEQVAGERQR LVETHLARVE AILNNNRRLA LENYLTAAQS DPPQPERVLQ ALKRYMAAEQ
KDRRHTLRHY QHIVAVDPQK AEQMKFQVYT HLHVIEERMN QSLALLYKDP TLAEELHNDI
QELVKAERGD ISELMTTSFS ETRTTEELLP AASEEEKDDE EEEERAFQNR PYPPRIEPQS
NKKVDEYDYT TSERGPTYEY EEKINTSAEL KQVVNKPPEI ERDELQPDAL ETFNRGAMVG
LLVVAVAIAM VMVISLLLVR RKPYGTISHG IVEVDPMLTP EERQLNKMQN HGYENPTYKF
FEQMN
//
