ID A0A1S3W218_ERIEU Unreviewed; 706 AA.
AC A0A1S3W218;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Amyloid-like protein 2 isoform X3 {ECO:0000313|RefSeq:XP_016040493.1};
GN Name=APLP2 {ECO:0000313|RefSeq:XP_016040493.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016040493.1};
RN [1] {ECO:0000313|RefSeq:XP_016040493.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_016040493.1; XM_016185007.1.
DR AlphaFoldDB; A0A1S3W218; -.
DR GeneID; 103128663; -.
DR CTD; 334; -.
DR OrthoDB; 2907766at2759; -.
DR Proteomes; UP000079721; 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; cd21709; JMTM_APLP2; 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; 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; 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:UP000079721};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..706
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010171860"
FT TRANSMEM 637..659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 47..206
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 316..507
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 47..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 214..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..235
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..269
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 117..124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
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 706 AA; 80342 MW; 863ED09F6EDEC72B CRC64;
MAAMGTVVAV ATGRLLVLLL LLGLTVPAAA LAGYIEALAA NAGTGFAVAE PQIAMFCGKL
NMHVNIQTGK WEPDPTGTKS CLGTKEEVLQ YCQEMYPELQ ITNVVEANQA VSVDNWCQKD
KKQCKSHIVI PLKCLVGEFV SDVLLVPEKC QFFHKEQMDV CENHQHWHTV VKEACLTRGM
ALYSYGMLLP CGVDQFHGME YVCCPQTKVI ESAISKEEEE EEDEEEEEEE DYDIYKSEFP
TEAELEDFTE AAADEEDEDD EEGEEVVEDR DYYYDTFKGD DYNEENPTEP SNGGPISEKE
IIHDVKVPPT PLPTNDVDVY FETSADDNEH ARFQKAKEQL EIRHRNRMDR VKKEWEEAEL
QAKNLPKVER QTLIQHFQAM VKALEKEAAS EKQQLVETHL ARVEAMLNDR RRMALENYLS
ALQSDPPRPH RILQALRRYV RAENKDRLHT IRHYQHVLAV DPEKAAQMKP QVMTHLHVIE
ERRNQSLSLL YKVPYVAQEI QEEIDELLQE QRADMDQFTA SISETPVDVR VSSEESDEIP
PFHPFHPFPS LPENEDTQPE LYRPMKKGSG VGEQDGGLIG AEEKVINSKN KVDENMVIDE
TLDVKEMIFN AERVGGLEEE PESVGPLRED FSLSSSALIG LLVISVAIAT VIVISLVMLR
KRQYGTISHG IVEVDPMLTP EERHLNKMQN HGYENPTYKY LEQMQI
//
