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}.
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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
//