ID A0A0N5BLB4_STREA Unreviewed; 737 AA.
AC A0A0N5BLB4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE SubName: Full=A4_EXTRA domain-containing protein {ECO:0000313|WBParaSite:SPAL_0000671300.1};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000671300.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0000671300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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; A0A0N5BLB4; -.
DR STRING; 174720.A0A0N5BLB4; -.
DR WBParaSite; SPAL_0000671300.1; SPAL_0000671300.1; SPAL_0000671300.
DR Proteomes; UP000046392; Unplaced.
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 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..737
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005894481"
FT TRANSMEM 663..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..203
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 253..454
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 38..131
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 139..203
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 512..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 261..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 512..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..594
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 48..71
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 107..114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 737 AA; 85584 MW; 150A15E87E33B2C5 CRC64;
MLPGSIFIFL LQIIFSFASP KDGIYASIDT PIPTKLHSKF IPMVAFLCGY RNKFSNENGG
WTTDTNKFAT CLTGKLDILK YCRKVYPNLN ITNIVEYSHE ETIDKWCRED TPNCKFSHTV
RPYKCIDGEF VAQALQVPNG CMFGHMSSRS MCSDYSQLNN KAFNECIKMK DNNGKSMVLR
SFSVLQPCAI DLFRGVEYVC CPTIIKNKSN EFLTNDINEI TEGNDFDDDV FGSDDLLNII
ENDDNGTLLD KGEQDPYFKE ITNANNEHEK FREAEKRLEQ RHRSEVSRII NVWSELYDKY
KNMKDNDTNE AEKYKKDMVR KFRKTVANIE EENKEMKKEI ETVHEERLKN IFNERKRKAT
HEFREALARH VEKDNKIEVL RTLKACIRSE EKDRYHMLNR YRHLLRTDAV EAEKYKTELL
HNLKYIDLRI NGTIAMLDDF PQLAEAIGPI VKSFWREYRK EHTPEIESDV LSNAIGENDN
VKLVNLYKTH YEKLHEAEKN IRKKYFSKGN IKKATTTPKP TTTTTTSTIP PATEINKNSI
YNELEKADLE KGDNDKSNEV NDIEYVKFNK NQTDDRSDYD EDEDDNDDDD SDTSEEGNNN
KKQETFNDSE EDNVPVEIEP IISGPIMDST FDENPSYVKL SKMDHNRQLY SYNKSQSYLS
SNFIIYGFIG TLCCVFFVAA ITLYSKNRHS GFVEVDVCTP EERHVNSMQI NGYENPTYTY
FDANAPVKSQ NEESLKQ
//
