ID A0A0K0E4K2_STRER Unreviewed; 743 AA.
AC A0A0K0E4K2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=A4_EXTRA domain-containing protein {ECO:0000313|WBParaSite:SSTP_0000442200.1};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000442200.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000442200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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; A0A0K0E4K2; -.
DR STRING; 6248.A0A0K0E4K2; -.
DR WBParaSite; SSTP_0000442200.1; SSTP_0000442200.1; SSTP_0000442200.
DR Proteomes; UP000035681; 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:UP000035681};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..743
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005327431"
FT TRANSMEM 669..690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..201
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 252..453
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 37..130
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 138..201
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 568..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 318..348
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 573..597
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 47..70
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 106..113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 743 AA; 86514 MW; 2D4E961A4DB870C7 CRC64;
MLPGSIFIFL LQILFSFASP KDGISVSVDS HITKIHSKFV PMVAFLCGYR NKYTNDNGGW
TTDKNKFATC LTGKLDILKY CRKVYPNLNI TNIVEYSHEE KIDRWCDEDA TTCKYSHTVR
PYRCIDGEFV AQALQVPNGC TFGHISSRSM CNDYSQLNNK AFAECSKMND SGRPMVLRSF
SVLQPCAIDL FRGVEYVCCP SIKKTKTNEI LTNDINEITE GNEFEEDEEF DTDDLINTIE
SDDNDTLIEK SEQDPYFKEI TNANNEHEKY REAEKRLEQR HRSEVSKIIN VWSELYDKYK
TMKESNINEA EKYKKEMVGK FRKTVANIEE ENKEIKKQIE TVHEERLKNI FNERKRKATH
EFREALARHV EKDNKAEIVR TLKACIRSEE KDRYHMLNRY RHLLRTDGNE AEKYRSELLH
NLKYIDLRIN GTIAMLDDFP ELAEAVGPIV KTFWREYRKE HTPELDTNFL INGMEENDNI
KLVNLYKTHY EKLHEAEKNM RKKYFLKTNI RRVSTTSTTT TTTTLSPTTN AIKKDIMNEL
EKTDLDSVEN NKSKEVKVIE YVKFNKSKTD DESGYDEDED EDDYDDDDDD DDDDTSDEED
KKNKKKDSLT DSSDSDEDNV PVEIEPIISG PIMDSFIDES PSYVRLSKMD HNRHLYNHSK
SQSYLSSNFI IYGFIGTLCS VFLVAAITLY SRNRHSGFVE VDVCTPEERH VNNMQVNGYE
NPTYTYYDAS VIVKPSNEET TKQ
//
