ID A0A2B4SWQ0_STYPI Unreviewed; 584 AA.
AC A0A2B4SWQ0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Amyloid-like protein 1 {ECO:0000313|EMBL:PFX33619.1};
GN Name=APLP1 {ECO:0000313|EMBL:PFX33619.1};
GN ORFNames=AWC38_SpisGene1512 {ECO:0000313|EMBL:PFX33619.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX33619.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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:PFX33619.1}.
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DR EMBL; LSMT01000010; PFX33619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4SWQ0; -.
DR STRING; 50429.A0A2B4SWQ0; -.
DR EnsemblMetazoa; XM_022941812.1; XP_022797547.1; LOC111335812.
DR OrthoDB; 2907766at2759; -.
DR Proteomes; UP000225706; 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 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; IPR019744; APP_CUBD_CS.
DR InterPro; IPR036176; E2_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.
DR PROSITE; PS00320; APP_INTRA; 1.
PE 3: Inferred from homology;
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:UP000225706};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..584
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012066722"
FT TRANSMEM 516..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..179
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 217..415
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 31..113
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 121..179
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 419..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 123..177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 134..164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 148..176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 584 AA; 65956 MW; 48D6503516B25E14 CRC64;
MDWSYRKTIF LCLTFVTVGS ALVENSNYDE LDYDPQVAIK CGKVTRHMDV NTGSWEADKN
STSLCATTMQ EILKYCKAIY PSQDVRNVVE GNKEVLVDGS LVTPYRCLVG PFESDALLVP
PKCRFEHMHD NSNCLSHDQW HTRASDKCQN EGMIVKDYGV LIPCGTGKFT GVEFVCCPQD
ASEEVATDAA KIVPISEVVS TSKPTSVLEH LKQAISKFAK HVEGSTIGCD RQKYHERRDK
LEETHKAKIQ KLIDTWRKSE KRYKLMKTDD EDLAAGSISE DLQTFNKMVN SFGDQAKLER
ARLKEEHHQC TQIDLNDKKN KALGDFVAAL QEEPRDDNKI LQAVQRYVRF CTQDRLHNLR
YFDYVLKHHP EKAEEARESL QNHLKRINNL VNESMVLLYK LPGIARKFQM ELPDWIPKPP
ALPTEAPTVE KSSAAKDPTD PPSHVGSKPA ATDMMAGGEG KHVDEDVPEV KKPFRKPGKT
AALKKANDND DYNDDDEDVA EDENGPFRKN HSRATFSAVI GLSCGALVIM IIIVVAMAMR
RTRLSNNTKT VLVDEDGEGT SEKSHLVNMQ ENGYENPTYR FYDY
//
