ID A0A0V0SKQ8_9BILA Unreviewed; 721 AA.
AC A0A0V0SKQ8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE SubName: Full=Beta-amyloid-like protein {ECO:0000313|EMBL:KRX27353.1};
DE Flags: Fragment;
GN Name=apl-1 {ECO:0000313|EMBL:KRX27353.1};
GN ORFNames=T07_15090 {ECO:0000313|EMBL:KRX27353.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX27353.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX27353.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX27353.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX27353.1}.
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DR EMBL; JYDL01000003; KRX27353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0SKQ8; -.
DR STRING; 6336.A0A0V0SKQ8; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
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; 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; 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:SF15; AMYLOID-BETA-LIKE PROTEIN; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000054630};
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 656..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..232
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 341..540
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 72..165
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 173..232
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 254..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 373..433
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 272..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..336
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 82..105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 141..148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX27353.1"
SQ SEQUENCE 721 AA; 82890 MW; AD959A5472708FC9 CRC64;
LCHASRSLSS LVRWLMVKML LNLAFLLLSI CLHFSVGSIE LFECVSFQLT RFQAVSGGYA
GSAASNHKTK ANAFVPQVVF RCGFRNRYMT EDGSWASDPD SRASCLTGKL DILKYCRKVY
WNLTVTNIVE SSHFVEVDNW CKDDGYPCKW SFWVKPYRCM VGEFESDALL VPKNCHFEHV
DDENICKDFD YWNQTAIKNC KRRNSYSVLS FAMLEPCGLD MFSGVEFVCC PNRDDINADV
VNVGRLSIRM QSSRDRDNEL YGPAIPNDSE EYPPAVTTTT TTTTTRTHST VPPPALLTTA
SPKTAVDDDE DEDDDEEDYE EDDDDDDDDD AENEAADTDN EKSAYLRVAD PEIEHEAYKN
ALEHLTKVHH KKVSKVMKEW SELENRYQEM KRRDPKHAES FKNEMNMRFQ KTVAALEEEN
ADERHQIEDI HQQRVMANLN EKKRLALKEF HQLYDVAGPP PAHAILRTLK AYVRAEEKDR
VHLLNHYRHM LRSKPQESIF FKSDVLNKLV DIDRRINATI SLLKFHPEID KKVRAAIEDF
FHTYRRENTP DIAETFPDGY LTSAQYHQLL NIKLTVDQII TLAPSVKVQR KEITENTIDP
VQQRQEQTIS SLPLRNIHVV EEDISLLNKK QDIVHDFVFQ EKSIGKGASK YIDHSFIFFS
IAGVSLIAAV VCGIFFMRHR ANHAGQGFIE VSACTPEERH VANMQISGYE NPAYKYFEEN
L
//
