ID A0A0V0Y0Y5_TRIPS Unreviewed; 681 AA.
AC A0A0V0Y0Y5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE SubName: Full=Amyloid-like protein 2 {ECO:0000313|EMBL:KRX93853.1};
DE Flags: Fragment;
GN Name=apl-1 {ECO:0000313|EMBL:KRX93853.1};
GN ORFNames=T4E_7596 {ECO:0000313|EMBL:KRX93853.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX93853.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX93853.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX93853.1};
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:KRX93853.1}.
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DR EMBL; JYDU01000081; KRX93853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0Y0Y5; -.
DR Proteomes; UP000054815; 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:UP000054815};
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 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..214
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 321..520
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 64..147
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 155..214
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 235..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 353..413
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 253..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..317
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 74..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 133..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX93853.1"
SQ SEQUENCE 681 AA; 78247 MW; DEDAD1FBD037572A CRC64;
LCHASRFLSS FVRWLMVKML LNSAFFVLSI CLHFAVGSIE LTRLQAVSGG YAGSAASNHK
TKANAFVPQV VFHCGFRNRY MTEDGSWATD PDSRASCLTG KLDILKYCRK VYWNLTVTNI
VESSHFVEVD NWCKDDGYPC KWSFWFESDA LLVPKNCHFE HVDDENICKD FDYWNQTAIK
NCKRRNSYSV LSFAMLEPCG LDMFSGVEFV CCPNRDDINA NVVNVGRLSI RMQSSRDREN
ELYGPAIPND SEEYPPTVTT TTTTTTTHST VPPPALLTTA SPKATTDDED EDDDEDYEEE
DDDDDDDDDD AENEDADTDN EKSVYLRVAD PEIEHEAYKN ALEHLTKVHH KKVSKVMKEW
SELENRYQEM KRRDPKHAES FKNEMNMRFQ KTVAALEEEN ADERHQIEDI HQQRVMANLN
EKKRLALKEF HQLYDVAGPP PAHAILRTLK AYVRAEEKDR VHLLNHYRHM LRSKPQESMF
FKSDVLNKLL DIDRRINATI SLLKLHPEID KKKISSTHTV VRIRPTLRKL SRMAISTLLI
ITLAPSVKVQ RKEITENTID TVQRQEQTIS TLPLRNIHVV EEDISLLNKK QDIVHDFVFQ
EKSIAKGASK YIDHSFIFFS IAGVSLIAAV VCGIFFMRHR ANHAGQGFIE VSACTPEERH
VANMQISGYE NPAYKYFEEN L
//
