ID A0A1V4J7Q9_PATFA Unreviewed; 740 AA.
AC A0A1V4J7Q9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Amyloid-like protein 2 isoform B {ECO:0000313|EMBL:OPJ68186.1};
GN Name=APLP2 {ECO:0000313|EMBL:OPJ68186.1};
GN ORFNames=AV530_013698 {ECO:0000313|EMBL:OPJ68186.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ68186.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ68186.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ68186.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ68186.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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:OPJ68186.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSYS01008642; OPJ68186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4J7Q9; -.
DR STRING; 372326.A0A1V4J7Q9; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR CDD; cd21709; JMTM_APLP2; 1.
DR CDD; cd22607; Kunitz_ABPP-like; 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; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz 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; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
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 Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00203; AMYLOIDA4.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00006; A4_EXTRA; 1.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF56491; A heparin-binding domain; 1.
DR SUPFAM; SSF89811; Amyloid beta a4 protein copper binding domain (domain 2); 1.
DR SUPFAM; SSF57362; BPTI-like; 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.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
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..740
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012257409"
FT TRANSMEM 671..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..197
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 299..349
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 357..548
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 36..131
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 139..197
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 204..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..260
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 81..125
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 106..113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 141..195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 152..182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 166..194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 740 AA; 84308 MW; 89D33E6126550CB9 CRC64;
MGSGSAFLLL LGLAGPAVTL AGYIEALAAN AGTGFAVAEP QIAMFCGKLN MHVNIQTGKW
EPDTSGTKSC FGRKEEILQY CQEMYPDLQI TNVVEANQPV SIDSWCKRGK KQCKDHTHIV
VPYKCLVGEF VSDVLLVPEK CRFFHKERMD MCESHQHWHT VAKEACLTEG MILHSYGMLL
PCGVDQFHGT EYVCCPQTKV VDEALSKEEE DEDEDEDYNL YKSEFPTEAG VEDFTGTAVE
EDEDEDDEGE EEEEDVVEDR DYYYDSYKVD DYNEETTTEP TSEKAASEKE VSSDMKSVCS
QEAMTGPCRA VMPRWYFDPN KRKCIRFIYG GCGGNRNNFE SEEYCMAVCK KMMPTDDVDV
YFETPADDNE HARFQKAKEQ LEVRHHNRMD RVKKEWEEAE HQAVNLPKAE RQTLIQHFQA
MVKSLEKEAA SEKQQLVETH LARVEAMLND RRRIALENYL AALQADPPRP HRILQALKRY
VRAENKDRLH TIRHYQHVLA VDPEKAAQMK SQVMTHLHVI EERMNQSLSL LYKVPYVAEE
IQDEIDELLQ EQRADMDQFT SSISESQVDV RVSSEESEEI PLDGKPFRPF QVKTFPALPE
SEGSGMTELD GLIGAEEKVI NSKNKVDENV VIDETLDVKE MIFNAERVGG LVDEPDNDNS
LRDDFSFSSS ALIGLLVIAV AIATVIVISL VMLRKRQYGT ISHGIVEVDP MLTPEERHLS
KMQNHGYENP TYKYLEQMQI
//
