GenomeNet

Database: UniProt
Entry: A0A287BE80_PIG
LinkDB: A0A287BE80_PIG
Original site: A0A287BE80_PIG 
ID   A0A287BE80_PIG          Unreviewed;       702 AA.
AC   A0A287BE80; A0A481B7Z1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Amyloid beta like protein 2 {ECO:0000313|Ensembl:ENSSSCP00000054402.2};
DE   SubName: Full=Amyloid-like protein 2 isoform 3 {ECO:0000313|EMBL:HDA92355.1};
DE   SubName: Full=Amyloid-like protein 2 isoform X1 {ECO:0000313|EMBL:HDC00454.1};
GN   Name=APLP2 {ECO:0000313|Ensembl:ENSSSCP00000054402.2,
GN   ECO:0000313|VGNC:VGNC:85414};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000054402.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000054402.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000054402.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDA92355.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000054402.2}
RP   IDENTIFICATION.
RG   Ensembl;
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}.
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; DQIR01136879; HDA92355.1; -; Transcribed_RNA.
DR   EMBL; DQIR01244976; HDC00454.1; -; Transcribed_RNA.
DR   EMBL; DQIR01267986; HDC23464.1; -; Transcribed_RNA.
DR   EMBL; DQIR01297221; HDC52699.1; -; Transcribed_RNA.
DR   Ensembl; ENSSSCT00000060720.2; ENSSSCP00000054402.2; ENSSSCG00000015244.5.
DR   VGNC; VGNC:85414; APLP2.
DR   GeneTree; ENSGT00530000063252; -.
DR   Proteomes; UP000008227; Chromosome 9.
DR   Bgee; ENSSSCG00000015244; Expressed in adult mammalian kidney and 42 other cell types or tissues.
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   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|PeptideAtlas:A0A287BE80};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
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_5041082370"
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          324..515
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..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..245
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..278
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;  79889 MW;  D04C520B64455AEA CRC64;
     MAATRTAAAA ATGKFLLLLL LGLSAPAAAL AGYIEALAAN AGTGFAVAEP QIAMFCGKLN
     MHVNIQTGKW EPDPTGTKSC FGTKEEVLQY CQEMYPELQI TNVMEANQPV RVDNWCRRDK
     KQCKSHVVIP SKCLVGEFVS DVLLVPEKCQ FFHKERMEVC ENHQHWHTVV KEACLTQGMT
     LYSYGMLLPC GVDQFHGTEY VCCPQTKLVR SSVSKEEEED DDDDEEDDDD EENEEEDEEE
     DYDIYKSEFP TEADLEDFTE AAVDEDEEDE EGEEVVEDRD YYYDTFKGDE YNEEGPTEPS
     RDRAAAERVT HDVRVPPTPL PTNDVDVYFE TSADDNEHAR FQKAKEQLEI RHRNRMDRVK
     KEWEEAELQA KNLPKAERQT LIQHFQAMVK ALEKEAASEK QQLVETHLAR VEAMLNDRRR
     VALENYLAAL QADPPRPHRI LQALRRYVRA ENKDRLHTIR HYQHVLAVDP EKAAQMKSQV
     MTHLHVIEER RNQSLSLLYK VPYVAQEIQE EIDELLQEQR ADMDQFTASI SETPVDVRVS
     SEESDEMPPL YPLHPFPSLP ENEGSALGEQ DGGLIGAEEK VINSKKKVDE NMVIDETLDV
     KEMIFNAERV GGLEEAPEST GPLREDFGLS SSALIGLLVI AVAIATVIVI SLVMLRKRQY
     GTISHGIVEV DPMLTPEERH LNKMQNHGYE NPTYKYLEQM QI
//
DBGET integrated database retrieval system