APP

Functionⁱ

Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP (By similarity). Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu²⁺-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu²⁺ ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity).By similarity

Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron (By similarity).By similarity

The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.By similarity

N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).By similarity

Miscellaneous

Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between amyloid-beta molecules resulting in amyloid-beta-metal aggregates. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	147	Copper 1PROSITE-ProRule annotation	1
Metal bindingⁱ	151	Copper 1PROSITE-ProRule annotation	1
Metal bindingⁱ	168	Copper 1PROSITE-ProRule annotation	1
Siteⁱ	170	Required for Cu(2+) reductionPROSITE-ProRule annotation	1
Siteⁱ	301 – 302	Reactive bondBy similarity	2
Metal bindingⁱ	677	Copper or zinc 2By similarity	1
Metal bindingⁱ	681	Copper or zinc 2By similarity	1
Metal bindingⁱ	684	Copper or zinc 2By similarity	1
Metal bindingⁱ	685	Copper or zinc 2By similarity	1
Siteⁱ	704	Implicated in free radical propagationBy similarity	1
Siteⁱ	706	Susceptible to oxidationBy similarity	1

GO - Molecular functionⁱ

DNA binding Source: UniProtKB
enzyme binding Source: Ensembl
heparin binding Source: UniProtKB-KW
identical protein binding Source: Ensembl
PTB domain binding Source: Ensembl
serine-type endopeptidase inhibitor activity Source: UniProtKB-KW
signaling receptor activator activity Source: Ensembl
signaling receptor binding Source: Ensembl
transition metal ion binding Source: InterPro

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

adult locomotory behavior Source: UniProtKB
amyloid fibril formation Source: Ensembl
astrocyte activation involved in immune response Source: Ensembl
axo-dendritic transport Source: UniProtKB
axon midline choice point recognition Source: UniProtKB
axonogenesis Source: UniProtKB
cell adhesion Source: UniProtKB-KW
cellular copper ion homeostasis Source: UniProtKB
cellular response to amyloid-beta Source: Ensembl
cholesterol metabolic process Source: Ensembl
cognition Source: UniProtKB
collateral sprouting in absence of injury Source: UniProtKB
dendrite development Source: UniProtKB
endocytosis Source: UniProtKB
extracellular matrix organization Source: UniProtKB
forebrain development Source: Ensembl
ionotropic glutamate receptor signaling pathway Source: UniProtKB
locomotory behavior Source: UniProtKB
mating behavior Source: UniProtKB
microglia development Source: Ensembl
modulation of age-related behavioral decline Source: Ensembl
modulation of excitatory postsynaptic potential Source: Ensembl
mRNA polyadenylation Source: UniProtKB
negative regulation of cell population proliferation Source: Ensembl
negative regulation of gene expression Source: Ensembl
negative regulation of long-term synaptic potentiation Source: Ensembl
negative regulation of neuron differentiation Source: Ensembl
neuromuscular process controlling balance Source: Ensembl
neuron apoptotic process Source: Ensembl
neuron projection development Source: UniProtKB
neuron projection maintenance Source: Ensembl
neuron remodeling Source: UniProtKB
Notch signaling pathway Source: UniProtKB-KW
positive regulation of amyloid-beta formation Source: Ensembl
positive regulation of amyloid fibril formation Source: Ensembl
positive regulation of astrocyte activation Source: Ensembl
positive regulation of chemokine biosynthetic process Source: Ensembl
positive regulation of ERK1 and ERK2 cascade Source: Ensembl
positive regulation of G2/M transition of mitotic cell cycle Source: Ensembl
positive regulation of glycolytic process Source: Ensembl
positive regulation of interleukin-1 beta biosynthetic process Source: Ensembl
positive regulation of interleukin-6 biosynthetic process Source: Ensembl
positive regulation of JNK cascade Source: Ensembl
positive regulation of long-term synaptic potentiation Source: Ensembl
positive regulation of microglial cell activation Source: Ensembl
positive regulation of mitotic cell cycle Source: UniProtKB
positive regulation of NF-kappaB transcription factor activity Source: Ensembl
positive regulation of NIK/NF-kappaB signaling Source: Ensembl
positive regulation of peptidyl-serine phosphorylation Source: Ensembl
positive regulation of peptidyl-threonine phosphorylation Source: Ensembl
positive regulation of protein binding Source: Ensembl
positive regulation of T cell migration Source: Ensembl
positive regulation of transcription by RNA polymerase II Source: Ensembl
positive regulation of tumor necrosis factor biosynthetic process Source: Ensembl
protein phosphorylation Source: UniProtKB
regulation of epidermal growth factor-activated receptor activity Source: UniProtKB
regulation of long-term neuronal synaptic plasticity Source: Ensembl
regulation of multicellular organism growth Source: UniProtKB
regulation of presynapse assembly Source: Ensembl
regulation of spontaneous synaptic transmission Source: Ensembl
regulation of synapse structure or activity Source: UniProtKB
regulation of translation Source: UniProtKB
response to oxidative stress Source: Ensembl
smooth endoplasmic reticulum calcium ion homeostasis Source: Ensembl
suckling behavior Source: Ensembl
synaptic growth at neuromuscular junction Source: Ensembl
tumor necrosis factor production Source: Ensembl
visual learning Source: UniProtKB

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Heparin-binding, Protease inhibitor, Serine protease inhibitor
Biological process	Apoptosis, Cell adhesion, Endocytosis, Notch signaling pathway
Ligand	Copper, Iron, Metal-binding, Zinc

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	I02.015

MEROPSⁱ

I02.015

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Amyloid-beta A4 protein Alternative name(s): ABPP Short name: APP Alzheimer disease amyloid A4 protein homolog Amyloid precursor proteinCurated Amyloid-beta precursor proteinCurated Cleaved into the following 14 chains: N-APP Soluble APP-alpha Short name: S-APP-alpha Soluble APP-beta Short name: S-APP-beta C99 Alternative name(s): Beta-secretase C-terminal fragment Short name: Beta-CTF Amyloid-beta protein 42 Short name: Abeta42 Alternative name(s): Beta-APP42 amyloid-beta protein 40 Short name: Abeta40 Alternative name(s): Beta-APP40 C83 Alternative name(s): Alpha-secretase C-terminal fragment Short name: Alpha-CTF P3(42) P3(40) C80 Gamma-secretase C-terminal fragment 59 Alternative name(s): Gamma-CTF(59) Gamma-secretase C-terminal fragment 57 Alternative name(s): Gamma-CTF(57) Gamma-secretase C-terminal fragment 50 Alternative name(s): Gamma-CTF(50) C31
Gene namesⁱ	Name:APP
Organismⁱ	Sus scrofa (Pig)
Taxonomic identifierⁱ	9823 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus
Proteomesⁱ	UP000008227 Componentⁱ: Chromosome 13

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	18 – 701	ExtracellularCuratedAdd BLAST	684
Transmembraneⁱ	702 – 722	HelicalBy similarityAdd BLAST	21
Topological domainⁱ	723 – 770	CytoplasmicCuratedAdd BLAST	48

Keywords - Cellular componentⁱ

Amyloid, Cell membrane, Cell projection, Coated pit, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane, Nucleus, Secreted

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 17	By similarityAdd BLAST	17
ChainⁱPRO_0000000140	18 – 770	Amyloid-beta A4 proteinAdd BLAST	753
ChainⁱPRO_0000000141	18 – 687	Soluble APP-alphaSequence analysisAdd BLAST	670
ChainⁱPRO_0000000142	18 – 671	Soluble APP-betaSequence analysisAdd BLAST	654
ChainⁱPRO_0000381970	18 – 286	N-APPBy similarityAdd BLAST	269
ChainⁱPRO_0000000143	672 – 770	C99By similarityAdd BLAST	99
ChainⁱPRO_0000000144	672 – 713	Amyloid-beta protein 42By similarityAdd BLAST	42
ChainⁱPRO_0000000145	672 – 711	amyloid-beta protein 40By similarityAdd BLAST	40
ChainⁱPRO_0000000146	688 – 770	C83By similarityAdd BLAST	83
PeptideⁱPRO_0000000147	688 – 713	P3(42)By similarityAdd BLAST	26
PeptideⁱPRO_0000000148	688 – 711	P3(40)By similarityAdd BLAST	24
ChainⁱPRO_0000384578	691 – 770	C80Add BLAST	80
ChainⁱPRO_0000000149	712 – 770	Gamma-secretase C-terminal fragment 59Add BLAST	59
ChainⁱPRO_0000000150	714 – 770	Gamma-secretase C-terminal fragment 57Add BLAST	57
ChainⁱPRO_0000000151	721 – 770	Gamma-secretase C-terminal fragment 50By similarityAdd BLAST	50
ChainⁱPRO_0000000152	740 – 770	C31By similarityAdd BLAST	31

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	38 ↔ 62	PROSITE-ProRule annotation
Disulfide bondⁱ	73 ↔ 117	PROSITE-ProRule annotation
Disulfide bondⁱ	98 ↔ 105	PROSITE-ProRule annotation
Disulfide bondⁱ	133 ↔ 187	PROSITE-ProRule annotation
Disulfide bondⁱ	144 ↔ 174	PROSITE-ProRule annotation
Disulfide bondⁱ	158 ↔ 186	PROSITE-ProRule annotation
Modified residueⁱ	198	Phosphoserine; by CK2By similarity	1
Modified residueⁱ	206	Phosphoserine; by CK1By similarity	1
Disulfide bondⁱ	291 ↔ 341	PROSITE-ProRule annotation
Disulfide bondⁱ	300 ↔ 324	PROSITE-ProRule annotation
Disulfide bondⁱ	316 ↔ 337	PROSITE-ProRule annotation
Modified residueⁱ	441	PhosphoserineBy similarity	1
Modified residueⁱ	497	PhosphotyrosineBy similarity	1
Glycosylationⁱ	542	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	571	N-linked (GlcNAc...) asparagineSequence analysis	1
Modified residueⁱ	729	PhosphothreonineBy similarity	1
Modified residueⁱ	730	Phosphoserine; by APP-kinase IBy similarity	1
Modified residueⁱ	743	Phosphothreonine; by CDK5 and MAPK10By similarity	1
Modified residueⁱ	757	Phosphotyrosine; by ABL1By similarity	1
Cross-linkⁱ	763	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationⁱ

Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro).By similarity

Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-3, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides.By similarity

N- and O-glycosylated.By similarity

Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins (By similarity).By similarity

Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond.By similarity

Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP).By similarity

Amyloid-beta peptides are degraded by IDE.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	197 – 198	Cleavage; by caspasesBy similarity	2
Siteⁱ	219 – 220	Cleavage; by caspasesBy similarity	2
Siteⁱ	671 – 672	Cleavage; by beta-secretaseBy similarity	2
Siteⁱ	687 – 688	Cleavage; by alpha-secretaseBy similarity	2
Siteⁱ	690 – 691	Cleavage; by theta-secretaseBy similarity	2
Siteⁱ	711 – 712	Cleavage; by gamma-secretase; site 1By similarity	2
Siteⁱ	713 – 714	Cleavage; by gamma-secretase; site 2By similarity	2
Siteⁱ	720 – 721	Cleavage; by gamma-secretase; site 3By similarity	2
Siteⁱ	739 – 740	Cleavage; by a caspaseBy similarity	2

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbⁱ	P79307
PeptideAtlas More...PeptideAtlasⁱ	P79307
PRIDEⁱ	P79307

Expressionⁱ

Gene expression databases

ExpressionAtlasⁱ	P79307 baseline and differential

ExpressionAtlasⁱ

P79307 baseline and differential

Interactionⁱ

Subunit structureⁱ

Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity).

Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif.

Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity).

Interacts, through a C-terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons (By similarity). Amyloid-beta associates with HADH2 (By similarity).

Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity).

Interacts with ITM2B.

Interacts with ITM2C.

Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu²⁺ ions. Can form homodimers; this is promoted by heparin binding (By similarity). Amyloid-beta protein 40 interacts with S100A9 (By similarity). CTF-alpha product of APP interacts with GSAP (By similarity).

Interacts with SORL1 (By similarity).

Interacts with PLD3 (By similarity).

Interacts with VDAC1 (By similarity).

Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2 (By similarity).

Interacts (via transmembrane region) with PSEN1; the interaction is direct (By similarity).

By similarity

GO - Molecular functionⁱ

enzyme binding Source: Ensembl
identical protein binding Source: Ensembl
PTB domain binding Source: Ensembl
signaling receptor binding Source: Ensembl

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRINGⁱ	9823.ENSSSCP00000012805

STRINGⁱ

9823.ENSSSCP00000012805

Structureⁱ

3D structure databases

SMRⁱ	P79307
ModBaseⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	28 – 189	E1PROSITE-ProRule annotationAdd BLAST	162
Domainⁱ	291 – 341	BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd BLAST	51
Domainⁱ	374 – 565	E2PROSITE-ProRule annotationAdd BLAST	192

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	28 – 123	GFLD subdomainPROSITE-ProRule annotationAdd BLAST	96
Regionⁱ	96 – 110	Heparin-bindingBy similarityAdd BLAST	15
Regionⁱ	131 – 189	CuBD subdomainPROSITE-ProRule annotationAdd BLAST	59
Regionⁱ	135 – 155	Copper-bindingBy similarityAdd BLAST	21
Regionⁱ	181 – 188	Zinc-bindingBy similarity	8
Regionⁱ	391 – 423	Heparin-bindingBy similarityAdd BLAST	33
Regionⁱ	491 – 522	Heparin-bindingBy similarityAdd BLAST	32
Regionⁱ	523 – 540	Collagen-bindingBy similarityAdd BLAST	18
Regionⁱ	695 – 722	Interaction with PSEN1By similarityAdd BLAST	28
Regionⁱ	732 – 751	Interaction with G(o)-alphaBy similarityAdd BLAST	20

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	724 – 734	Basolateral sorting signalAdd BLAST		11
Motifⁱ	757 – 762	YENPXY motif; contains endocytosis signalBy similarity		6

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	230 – 260	Asp/Glu-rich (acidic)Add BLAST		31
Compositional biasⁱ	274 – 280	Poly-Thr		7

Domainⁱ

The transmembrane helix undergoes a conformation change and unravels partially when bound to PSEN1, facilitating cleavage by PSEN1.By similarity

The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells.By similarity

The GFLD subdomain binds Cu²⁺ ions; this promotes homodimerization.By similarity

The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The YENPXY site is also involved in clathrin-mediated endocytosis.By similarity

The C-terminal region can bind zinc ions; this favors dimerization and formation of higher oligomers.By similarity

Sequence similaritiesⁱ

Belongs to the APP family.PROSITE-ProRule annotation

Keywords - Domainⁱ

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3540 Eukaryota ENOG410ZTKC LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063252
HOGENOMⁱ	HOG000232190
InParanoidⁱ	P79307
KEGG Orthology (KO) More...KOⁱ	K04520
OMAⁱ	KQCKTHA
Database of Orthologous Groups More...OrthoDBⁱ	953529at2759

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00109 KU, 1 hit
Gene3Dⁱ	1.20.120.770, 1 hit 2.30.29.30, 1 hit 3.30.1490.140, 1 hit 3.90.570.10, 1 hit 4.10.230.10, 1 hit 4.10.410.10, 1 hit
InterProⁱ	View protein in InterPro IPR036669 Amyloid_Cu-bd_sf IPR008155 Amyloid_glyco IPR013803 Amyloid_glyco_Abeta IPR037071 Amyloid_glyco_Abeta_sf IPR011178 Amyloid_glyco_Cu-bd IPR024329 Amyloid_glyco_E2_domain IPR008154 Amyloid_glyco_extra IPR015849 Amyloid_glyco_heparin-bd IPR036454 Amyloid_glyco_heparin-bd_sf IPR019745 Amyloid_glyco_intracell_CS IPR028866 APP IPR019543 APP_amyloid_C IPR019744 APP_CUBD_CS IPR036176 E2_sf IPR002223 Kunitz_BPTI IPR036880 Kunitz_BPTI_sf IPR011993 PH-like_dom_sf IPR020901 Prtase_inh_Kunz-CS
PANTHERⁱ	PTHR23103 PTHR23103, 1 hit PTHR23103:SF7 PTHR23103:SF7, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF10515 APP_amyloid, 1 hit PF12924 APP_Cu_bd, 1 hit PF12925 APP_E2, 1 hit PF02177 APP_N, 1 hit PF03494 Beta-APP, 1 hit PF00014 Kunitz_BPTI, 1 hit
PRINTSⁱ	PR00203 AMYLOIDA4 PR00759 BASICPTASE PR00204 BETAAMYLOID
SMARTⁱ	View protein in SMART SM00006 A4_EXTRA, 1 hit SM00131 KU, 1 hit
SUPFAMⁱ	SSF109843 SSF109843, 1 hit SSF56491 SSF56491, 1 hit SSF57362 SSF57362, 1 hit SSF89811 SSF89811, 1 hit
PROSITEⁱ	View protein in PROSITE PS00319 APP_CUBD, 1 hit PS51869 APP_E1, 1 hit PS51870 APP_E2, 1 hit PS00320 APP_INTRA, 1 hit PS00280 BPTI_KUNITZ_1, 1 hit PS50279 BPTI_KUNITZ_2, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show all Align All

P79307-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MLPGLALVLL AAWTARALEV PTDGNAGLLA EPQVAMFCGK LNMHMNVQNG 
        60         70         80         90        100
KWESDPSGTK TCIGTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR 
       110        120        130        140        150
SRKQCKTHTH IVIPYRCLVG EFVSDALLVP DKCKFLHQER MDVCETHLHW 
       160        170        180        190        200
HTVAKETCSE KSTNLHDYGM LLPCGIDKFR GVEFVCCPLA EESDNIDSAD 
       210        220        230        240        250
AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVADVEEE EAEDDEDDED 
       260        270        280        290        300
GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC 
       310        320        330        340        350
RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSVMSQSLL 
       360        370        380        390        400
KTTQEHLPQD PVKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA 
       410        420        430        440        450
KHRERMSQVM REWEEAERQA KNLPKADKKA VIQHFQEKVE SLEQEAANER 
       460        470        480        490        500
QQLVETHMAR VEAMLNDRRR LALENYITAL QAVPPRPRHV FNMLKKYVRA 
       510        520        530        540        550
EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER MNQSLSLLYN 
       560        570        580        590        600
VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET 
       610        620        630        640        650
KTTVELLPVN GEFSLDDLQP WHPFGVDSVP ANTENEVEPV DARPAADRGL 
       660        670        680        690        700
TTRPGSGLTN IKTEEISEVK MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG 
       710        720        730        740        750
AIIGLMVGGV VIATVIVITL VMLKKKQYTS IHHGVVEVDA AVTPEERHLS 
       760        770
KMQQNGYENP TYKFFEQMQN

Length:770

Mass (Da):86,961

Last modified:April 23, 2003 - v2

Checksum:ⁱ5F7A1DCB2BCC583E

GO

Computationally mapped potential isoform sequencesⁱ

There are 6 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

Q2XQ99	Q2XQ99_PIG	Amyloid protein variant 2 Amyloid protein variant 2 (Amyloid-beta A4 protein)	APP	751	Annotation score:
A0A286ZTE6	A0A286ZTE6_PIG	Amyloid-beta A4 protein Amyloid-beta A4 protein (Amyloid-beta A4 protein isoform h)	APP	752	Annotation score:
A0A288CFW8	A0A288CFW8_PIG	Amyloid-beta A4 protein Amyloid-beta A4 protein	APP	756	Annotation score:
Q2XQA0	Q2XQA0_PIG	Amyloid protein variant 1 Amyloid protein variant 1 (Amyloid-beta A4 protein)	APP	695	Annotation score:
A0A287AJD6	A0A287AJD6_PIG	Amyloid-beta A4 protein Amyloid-beta A4 protein (Amyloid-beta A4 protein isoform c)	APP	714	Annotation score:
A0A288CFW6	A0A288CFW6_PIG	Amyloid-beta A4 protein Amyloid-beta A4 protein	APP	698	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	134 – 136	KFL → SSY in CAB06313 (Ref. 2) Curated		3

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB032550 mRNA Translation: BAA84580.1 Z84022 mRNA Translation: CAB06313.1 X56127 mRNA Translation: CAA39592.1
PIRⁱ	F60045
NCBI Reference Sequences More...RefSeqⁱ	NP_999537.1, NM_214372.1

Genome annotation databases

Ensemblⁱ	ENSSSCT00000041749; ENSSSCP00000034553; ENSSSCG00000012022
GeneIDⁱ	397663
KEGGⁱ	ssc:397663

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P79307	Amyloid-beta A4 protein		PIG		770	UniRef100_P79307

Protein	Similar proteins		Species	Score	Length	Source
P79307	Amyloid-beta precursor protein	)	HUMAN		770	UniRef90_P05067
Amyloid-beta A4 protein		CAVPO		770
Amyloid-beta A4 protein	)	RAT		770
Amyloid-beta A4 protein		MACFA		770
Amyloid-beta A4 protein (Fragment)		MACMU		76
+527

Protein	Similar proteins		Species	Score	Length	Source
P79307	Amyloid-beta precursor protein	)	HUMAN		770	UniRef50_P05067
Amyloid-beta A4 protein	)	MOUSE		770
Amyloid-beta A4 protein	)	RAT		770
Amyloid-beta A4 protein		PANTR		770
Amyloid-beta A4 protein		MACFA		770
+697

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB032550 mRNA Translation: BAA84580.1 Z84022 mRNA Translation: CAB06313.1 X56127 mRNA Translation: CAA39592.1
PIRⁱ	F60045
RefSeqⁱ	NP_999537.1, NM_214372.1

3D structure databases

SMRⁱ	P79307
ModBaseⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	9823.ENSSSCP00000012805

STRINGⁱ

9823.ENSSSCP00000012805

Protein family/group databases

MEROPSⁱ	I02.015

MEROPSⁱ

I02.015

Proteomic databases

PaxDbⁱ	P79307
PeptideAtlasⁱ	P79307
PRIDEⁱ	P79307

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSSSCT00000041749; ENSSSCP00000034553; ENSSSCG00000012022
GeneIDⁱ	397663
KEGGⁱ	ssc:397663

Organism-specific databases

CTDⁱ	351

CTDⁱ

351

Phylogenomic databases

eggNOGⁱ	KOG3540 Eukaryota ENOG410ZTKC LUCA
GeneTreeⁱ	ENSGT00530000063252
HOGENOMⁱ	HOG000232190
InParanoidⁱ	P79307
KOⁱ	K04520
OMAⁱ	KQCKTHA
OrthoDBⁱ	953529at2759

Miscellaneous databases

ChiTaRSⁱ	APP pig

ChiTaRSⁱ

APP pig

Gene expression databases

ExpressionAtlasⁱ	P79307 baseline and differential

ExpressionAtlasⁱ

P79307 baseline and differential

Family and domain databases

CDDⁱ	cd00109 KU, 1 hit
Gene3Dⁱ	1.20.120.770, 1 hit 2.30.29.30, 1 hit 3.30.1490.140, 1 hit 3.90.570.10, 1 hit 4.10.230.10, 1 hit 4.10.410.10, 1 hit
InterProⁱ	View protein in InterPro IPR036669 Amyloid_Cu-bd_sf IPR008155 Amyloid_glyco IPR013803 Amyloid_glyco_Abeta IPR037071 Amyloid_glyco_Abeta_sf IPR011178 Amyloid_glyco_Cu-bd IPR024329 Amyloid_glyco_E2_domain IPR008154 Amyloid_glyco_extra IPR015849 Amyloid_glyco_heparin-bd IPR036454 Amyloid_glyco_heparin-bd_sf IPR019745 Amyloid_glyco_intracell_CS IPR028866 APP IPR019543 APP_amyloid_C IPR019744 APP_CUBD_CS IPR036176 E2_sf IPR002223 Kunitz_BPTI IPR036880 Kunitz_BPTI_sf IPR011993 PH-like_dom_sf IPR020901 Prtase_inh_Kunz-CS
PANTHERⁱ	PTHR23103 PTHR23103, 1 hit PTHR23103:SF7 PTHR23103:SF7, 1 hit
Pfamⁱ	View protein in Pfam PF10515 APP_amyloid, 1 hit PF12924 APP_Cu_bd, 1 hit PF12925 APP_E2, 1 hit PF02177 APP_N, 1 hit PF03494 Beta-APP, 1 hit PF00014 Kunitz_BPTI, 1 hit
PRINTSⁱ	PR00203 AMYLOIDA4 PR00759 BASICPTASE PR00204 BETAAMYLOID
SMARTⁱ	View protein in SMART SM00006 A4_EXTRA, 1 hit SM00131 KU, 1 hit
SUPFAMⁱ	SSF109843 SSF109843, 1 hit SSF56491 SSF56491, 1 hit SSF57362 SSF57362, 1 hit SSF89811 SSF89811, 1 hit
PROSITEⁱ	View protein in PROSITE PS00319 APP_CUBD, 1 hit PS51869 APP_E1, 1 hit PS51870 APP_E2, 1 hit PS00320 APP_INTRA, 1 hit PS00280 BPTI_KUNITZ_1, 1 hit PS50279 BPTI_KUNITZ_2, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	A4_PIG
Accessionⁱ	P79307Primary (citable) accession number: P79307 Secondary accession number(s): Q29023, Q9TUI0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
	Last sequence update:	April 23, 2003
	Last modified:	July 3, 2019
	This is version 148 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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UniProtKB - P79307 (A4_PIG)

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Amyloid-beta A4 protein

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Functionⁱ

GO - Molecular functionⁱ

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Names & Taxonomyⁱ

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Keywords - Cellular componentⁱ

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Keywords - PTMⁱ

Expressionⁱ

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