ID A0A2U4BWN7_TURTR Unreviewed; 702 AA.
AC A0A2U4BWN7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Amyloid-like protein 2 isoform X4 {ECO:0000313|RefSeq:XP_019797617.1};
GN Name=APLP2 {ECO:0000313|RefSeq:XP_019797617.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019797617.1};
RN [1] {ECO:0000313|RefSeq:XP_019797617.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019797617.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_019797617.1; XM_019942058.2.
DR AlphaFoldDB; A0A2U4BWN7; -.
DR GeneID; 101336246; -.
DR OrthoDB; 2907766at2759; -.
DR Proteomes; UP000245320; Chromosome 8.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
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 CDD; cd21709; JMTM_APLP2; 1.
DR Gene3D; 6.10.250.1670; -; 1.
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; IPR019745; Amyloid_glyco_intracell_CS.
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:SF14; AMYLOID BETA PRECURSOR LIKE PROTEIN 2; 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 Copper {ECO:0000256|ARBA:ARBA00023008};
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:UP000245320};
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..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..702
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015564542"
FT TRANSMEM 633..655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..205
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 312..503
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 46..139
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 147..205
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 211..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 116..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 149..203
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 160..190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 174..202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 702 AA; 79522 MW; D7AE66A96C457781 CRC64;
MAATGTAAAA ATGKLLVLLL LGLTAPAAAL AGYIEALAAN AGTGFAVAEP QIAMFCGKLN
MHVNIQTGKW EPDPTGTQSC FGTKEEVLQY CQEMYPELQI TNVMEANQPV SVDNWCRRDK
KQCKTHIVIP FKCLVGEFVS DVLLVPEKCQ FFHKERMEVC ENHQHWHTVV KEACLTQGMT
LYSYGMLLPC GVDQFHGTEY VCCPQTKVVE SAVSKEEEED DEEDDEEDDE EEDYDIYKSE
FPTEADLEDF TEAAVDEGEE EVVEDRNYYY DAFKGDGRHE ESPTQSSRHG TAAEKEISYG
VRVPPTPLPT NDVDVYFETS ADDNEHARFQ KAKEQLEIRH RNRMDRVKKE WEEAELQAKN
LPKAERQTLI QHFQAMVKAL EKEAASEKQQ LVETHLARVE AMLNDRRRVA LENYLAALQS
DPPRPHRILQ ALRRYVRAEN KDRLHTIRHY QHVLAVDPEK AAQMKSQVMT HLHVIEERRN
QSLSLLYKVP YVAQEIQEEI DELLQEQRAD MDQFTASISE TPVDVRVSSE ESDEVLPFHP
LHPFPSLPEN EDTQPEVYHP MKTGSALGEQ EGGLIGAEEK VINSKKKVDE NMVIDETLDV
KEMILNAERV GGLEEGPESV GPLREDFSLS SSALIGLLVI AVAIATVIVI SLVMLRKRQY
GTISHGIVEV DPMLTPEERH LNKMQNHGYE NPTYKYLEQM QI
//
