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Amyloid-like protein 1 (APLP) (APLP-1) [Cleaved into: C30]

 APLP1_HUMAN             Reviewed;         650 AA.
P51693; O00113; Q96A92;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
22-FEB-2003, sequence version 3.
25-APR-2018, entry version 171.
RecName: Full=Amyloid-like protein 1;
Short=APLP;
Short=APLP-1;
Contains:
RecName: Full=C30;
Flags: Precursor;
Name=APLP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9428684; DOI=10.1111/j.1432-1033.1997.0354a.x;
Paliga K., Peraus G., Kreger S., Duwrrwang U., Hesse L., Multhaup G.,
Masters C.L., Beyreuther K., Weidemann A.;
"Human amyloid precursor-like protein 1 -- cDNA cloning, ectopic
expression in COS-7 cells and identification of soluble forms in the
cerebrospinal fluid.";
Eur. J. Biochem. 250:354-363(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=9521588; DOI=10.1007/s004390050676;
Lenkkeri U., Kestila M., Lamerdin J.E., McCready P., Adamson A.,
Olsen A., Tryggvason K.;
"Structure of the human amyloid-precursor-like protein gene APLP1 at
19q13.1.";
Hum. Genet. 102:192-196(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
PubMed=7494461; DOI=10.1016/0169-328X(95)00328-P;
Kim T.-W., Wu K., Xu J.-L., McAuliffe G., Tanzi R.E., Wasco W.,
Black I.B.;
"Selective localization of amyloid precursor-like protein 1 in the
cerebral cortex postsynaptic density.";
Brain Res. Mol. Brain Res. 32:36-44(1995).
[6]
HEPARIN AND ZINC-BINDING.
PubMed=7929392;
Bush A.I., Pettingell W.H. Jr., de Paradis M., Tanzi R.E., Wasco W.;
"The amyloid beta-protein precursor and its mammalian homologues.
Evidence for a zinc-modulated heparin-binding superfamily.";
J. Biol. Chem. 269:26618-26621(1994).
[7]
INTERACTION WITH APBA2.
PubMed=9890987; DOI=10.1074/jbc.274.4.2243;
Tomita S., Ozaki T., Taru H., Oguchi S., Takeda S., Yagi Y.,
Sakiyama S., Kirino Y., Suzuki T.;
"Interaction of a neuron-specific protein containing PDZ domains with
Alzheimer's amyloid precursor protein.";
J. Biol. Chem. 274:2243-2254(1999).
[8]
EXTRACELLULAR COPPER-BINDING.
PubMed=12135352; DOI=10.1021/bi0258647;
Simons A., Ruppert T., Schmidt C., Schlicksupp A., Pipkorn R.,
Reed J., Masters C.L., White A.R., Cappai R., Beyreuther K.,
Bayer T.A., Multhaup G.;
"Evidence for a copper-binding superfamily of the amyloid precursor
protein.";
Biochemistry 41:9310-9320(2002).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-215; SER-227 AND THR-228,
AND STRUCTURE OF CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[10]
GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[11]
X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 285-499, HEPARIN-BINDING,
MUTAGENESIS OF HIS-426; ARG-429 AND HIS-433, AND SUBUNIT.
PubMed=21574595; DOI=10.1021/bi101846x;
Lee S., Xue Y., Hu J., Wang Y., Liu X., Demeler B., Ha Y.;
"The E2 Domains of APP and APLP1 Share a Conserved Mode of
Dimerization.";
Biochemistry 50:5453-5464(2011).
-!- FUNCTION: May play a role in postsynaptic function. The C-terminal
gamma-secretase processed fragment, ALID1, activates transcription
activation through APBB1 (Fe65) binding (By similarity). Couples
to JIP signal transduction through C-terminal binding. May
interact with cellular G-protein signaling pathways. Can regulate
neurite outgrowth through binding to components of the
extracellular matrix such as heparin and collagen I.
{ECO:0000250}.
-!- FUNCTION: The gamma-CTF peptide, C30, is a potent enhancer of
neuronal apoptosis. {ECO:0000250}.
-!- SUBUNIT: Monomer and homodimer. Heparin binding promotes
homodimerization. Binds, via its C-terminus, to the PID domain of
several cytoplasmic proteins, including APBB and APBA family
members, MAPK8IP1 and Dab1 (By similarity). Binding to Dab1
inhibits its serine phosphorylation (By similarity). Interacts
with CPEB1. Interacts (via NPXY motif) with DAB2 (via PID domain);
the interaction is impaired by tyrosine phosphorylation of the
NPXY motif. Interacts (via NPXY motif) with DAB1 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-74648, EBI-74648;
Q06481:APLP2; NbExp=2; IntAct=EBI-74648, EBI-79306;
P05067-4:APP; NbExp=2; IntAct=EBI-74648, EBI-302641;
Q93074:MED12; NbExp=2; IntAct=EBI-74648, EBI-394357;
P17028:ZNF24; NbExp=2; IntAct=EBI-74648, EBI-707773;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- SUBCELLULAR LOCATION: C30: Cytoplasm. Note=C-terminally processed
in the Golgi complex.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P51693-1; Sequence=Displayed;
Name=2;
IsoId=P51693-2; Sequence=VSP_039100;
-!- TISSUE SPECIFICITY: Expressed in the cerebral cortex where it is
localized to the postsynaptic density (PSD).
{ECO:0000269|PubMed:7494461}.
-!- DOMAIN: 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 NPXY site is also involved in clathrin-mediated
endocytosis.
-!- PTM: Proteolytically cleaved by caspases during neuronal
apoptosis. Cleaved, in vitro, at Asp-620 by caspase-3 (By
similarity). {ECO:0000250}.
-!- PTM: N- and O-glycosylated. O-glycosylation with core 1 or
possibly core 8 glycans. Glycosylation on Ser-227 is the preferred
site to Thr-228. {ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:23234360}.
-!- MISCELLANEOUS: Binds zinc and copper in the extracellular domain.
Zinc-binding increases heparin binding. No Cu(2+) reducing
activity with copper-binding.
-!- SIMILARITY: Belongs to the APP family. {ECO:0000305}.
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EMBL; U48437; AAB96331.1; -; mRNA.
EMBL; AD000864; AAB50173.1; -; Genomic_DNA.
EMBL; BC012889; AAH12889.1; -; mRNA.
EMBL; BC013850; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS32997.1; -. [P51693-2]
RefSeq; NP_001019978.1; NM_001024807.2. [P51693-2]
RefSeq; NP_005157.1; NM_005166.4. [P51693-1]
UniGene; Hs.74565; -.
PDB; 3PMR; X-ray; 2.11 A; A/B=285-499.
PDB; 3Q7G; X-ray; 2.30 A; A/B=285-494.
PDB; 3Q7L; X-ray; 2.20 A; A/B=285-494.
PDB; 3QMK; X-ray; 2.21 A; A/B=285-494.
PDB; 4RD9; X-ray; 2.60 A; A/B=292-494.
PDB; 4RDA; X-ray; 2.50 A; A/B=290-495.
PDBsum; 3PMR; -.
PDBsum; 3Q7G; -.
PDBsum; 3Q7L; -.
PDBsum; 3QMK; -.
PDBsum; 4RD9; -.
PDBsum; 4RDA; -.
ProteinModelPortal; P51693; -.
SMR; P51693; -.
BioGrid; 106830; 46.
DIP; DIP-30846N; -.
IntAct; P51693; 42.
MINT; P51693; -.
STRING; 9606.ENSP00000221891; -.
GlyConnect; 716; -.
iPTMnet; P51693; -.
PhosphoSitePlus; P51693; -.
BioMuta; APLP1; -.
DMDM; 28558769; -.
PaxDb; P51693; -.
PeptideAtlas; P51693; -.
PRIDE; P51693; -.
TopDownProteomics; P51693-2; -. [P51693-2]
DNASU; 333; -.
Ensembl; ENST00000221891; ENSP00000221891; ENSG00000105290. [P51693-2]
GeneID; 333; -.
KEGG; hsa:333; -.
UCSC; uc002ocf.4; human. [P51693-1]
CTD; 333; -.
DisGeNET; 333; -.
EuPathDB; HostDB:ENSG00000105290.11; -.
GeneCards; APLP1; -.
HGNC; HGNC:597; APLP1.
HPA; HPA028970; -.
HPA; HPA028971; -.
MIM; 104775; gene.
neXtProt; NX_P51693; -.
OpenTargets; ENSG00000105290; -.
PharmGKB; PA24884; -.
eggNOG; ENOG410IT8P; Eukaryota.
eggNOG; ENOG4111MXY; LUCA.
GeneTree; ENSGT00530000063252; -.
HOGENOM; HOG000232190; -.
HOVERGEN; HBG000051; -.
InParanoid; P51693; -.
KO; K05639; -.
OMA; THLQVIE; -.
OrthoDB; EOG091G0UW4; -.
PhylomeDB; P51693; -.
TreeFam; TF317274; -.
ChiTaRS; APLP1; human.
EvolutionaryTrace; P51693; -.
GeneWiki; APLP1; -.
GenomeRNAi; 333; -.
PRO; PR:P51693; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105290; -.
CleanEx; HS_APLP1; -.
ExpressionAtlas; P51693; baseline and differential.
Genevisible; P51693; HS.
GO; GO:0005604; C:basement membrane; TAS:ProtInc.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0031694; F:alpha-2A adrenergic receptor binding; IPI:BHF-UCL.
GO; GO:0031695; F:alpha-2B adrenergic receptor binding; IPI:BHF-UCL.
GO; GO:0031696; F:alpha-2C adrenergic receptor binding; IPI:BHF-UCL.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0071874; P:cellular response to norepinephrine stimulus; IDA:BHF-UCL.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
Gene3D; 1.20.120.770; -; 1.
Gene3D; 3.30.1490.140; -; 1.
Gene3D; 3.90.570.10; -; 1.
InterPro; IPR036669; Amyloid_Cu-bd_sf.
InterPro; IPR008155; Amyloid_glyco.
InterPro; IPR011178; Amyloid_glyco_Cu-bd.
InterPro; IPR024329; Amyloid_glyco_E2_domain.
InterPro; IPR008154; Amyloid_glyco_extra.
InterPro; IPR019744; Amyloid_glyco_extracell_CS.
InterPro; IPR015849; Amyloid_glyco_heparin-bd.
InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
InterPro; IPR019745; Amyloid_glyco_intracell_CS.
InterPro; IPR019543; APP_amyloid_C.
InterPro; IPR036176; E2_sf.
PANTHER; PTHR23103; PTHR23103; 1.
Pfam; PF10515; APP_amyloid; 1.
Pfam; PF12924; APP_Cu_bd; 1.
Pfam; PF12925; APP_E2; 1.
Pfam; PF02177; APP_N; 1.
PRINTS; PR00203; AMYLOIDA4.
SMART; SM00006; A4_EXTRA; 1.
SUPFAM; SSF109843; SSF109843; 1.
SUPFAM; SSF56491; SSF56491; 1.
SUPFAM; SSF89811; SSF89811; 1.
PROSITE; PS00319; A4_EXTRA; 1.
PROSITE; PS00320; A4_INTRA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Cell adhesion;
Cell membrane; Complete proteome; Copper; Cytoplasm; Endocytosis;
Glycoprotein; Heparin-binding; Membrane; Metal-binding;
Neurodegeneration; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Zinc.
SIGNAL 1 38 {ECO:0000255}.
CHAIN 39 650 Amyloid-like protein 1.
/FTId=PRO_0000000203.
PEPTIDE 621 650 C30. {ECO:0000250}.
/FTId=PRO_0000000204.
TOPO_DOM 39 580 Extracellular. {ECO:0000255}.
TRANSMEM 581 603 Helical. {ECO:0000255}.
TOPO_DOM 604 650 Cytoplasmic. {ECO:0000255}.
REGION 158 178 Copper-binding. {ECO:0000250}.
REGION 204 211 Zinc-binding.
REGION 285 305 O-glycosylated at three sites.
REGION 310 342 Heparin-binding. {ECO:0000250}.
REGION 410 441 Heparin-binding. {ECO:0000250}.
REGION 442 459 Collagen-binding. {ECO:0000250}.
REGION 632 649 Interaction with DAB1. {ECO:0000250}.
REGION 636 650 Interaction with DAB2. {ECO:0000250}.
MOTIF 604 615 Basolateral sorting signal.
{ECO:0000250}.
MOTIF 640 643 Clathrin-binding. {ECO:0000255}.
MOTIF 640 643 NPXY motif; contains endocytosis signal.
COMPBIAS 241 247 Poly-Glu.
COMPBIAS 264 268 Poly-Glu.
SITE 167 167 Required for Cu(2+) reduction.
{ECO:0000250}.
SITE 620 621 Cleavage; by caspase-3. {ECO:0000250}.
CARBOHYD 215 215 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:19838169}.
CARBOHYD 227 227 O-linked (GalNAc...) serine.
{ECO:0000305|PubMed:19838169}.
CARBOHYD 228 228 O-linked (GalNAc...) threonine.
{ECO:0000305|PubMed:19838169}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 461 461 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 551 551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 517 517 D -> DA (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_039100.
MUTAGEN 426 426 H->A: Reduced affinity for heparin.
Reduces homodimerization.
{ECO:0000269|PubMed:21574595}.
MUTAGEN 429 429 R->A: Strongly reduced affinity for
heparin. Strongly reduced
homodimerization.
{ECO:0000269|PubMed:21574595}.
MUTAGEN 433 433 H->A: Reduced affinity for heparin.
Reduces homodimerization.
{ECO:0000269|PubMed:21574595}.
CONFLICT 48 48 A -> P (in Ref. 1; AAB96331).
{ECO:0000305}.
CONFLICT 78 78 P -> S (in Ref. 4; BC013850).
{ECO:0000305}.
HELIX 293 298 {ECO:0000244|PDB:3PMR}.
STRAND 302 304 {ECO:0000244|PDB:4RDA}.
HELIX 306 337 {ECO:0000244|PDB:3PMR}.
TURN 338 341 {ECO:0000244|PDB:3PMR}.
HELIX 344 399 {ECO:0000244|PDB:3PMR}.
STRAND 401 403 {ECO:0000244|PDB:3PMR}.
HELIX 406 437 {ECO:0000244|PDB:3PMR}.
HELIX 439 442 {ECO:0000244|PDB:3PMR}.
TURN 443 445 {ECO:0000244|PDB:3PMR}.
HELIX 446 467 {ECO:0000244|PDB:3PMR}.
HELIX 471 485 {ECO:0000244|PDB:3PMR}.
SEQUENCE 650 AA; 72176 MW; B95F0F4D1C5CBAC7 CRC64;
MGPASPAARG LSRRPGQPPL PLLLPLLLLL LRAQPAIGSL AGGSPGAAEA PGSAQVAGLC
GRLTLHRDLR TGRWEPDPQR SRRCLRDPQR VLEYCRQMYP ELQIARVEQA TQAIPMERWC
GGSRSGSCAH PHHQVVPFRC LPGEFVSEAL LVPEGCRFLH QERMDQCESS TRRHQEAQEA
CSSQGLILHG SGMLLPCGSD RFRGVEYVCC PPPGTPDPSG TAVGDPSTRS WPPGSRVEGA
EDEEEEESFP QPVDDYFVEP PQAEEEEETV PPPSSHTLAV VGKVTPTPRP TDGVDIYFGM
PGEISEHEGF LRAKMDLEER RMRQINEVMR EWAMADNQSK NLPKADRQAL NEHFQSILQT
LEEQVSGERQ RLVETHATRV IALINDQRRA ALEGFLAALQ ADPPQAERVL LALRRYLRAE
QKEQRHTLRH YQHVAAVDPE KAQQMRFQVH THLQVIEERV NQSLGLLDQN PHLAQELRPQ
IQELLHSEHL GPSELEAPAP GGSSEDKGGL QPPDSKDDTP MTLPKGSTEQ DAASPEKEKM
NPLEQYERKV NASVPRGFPF HSSEIQRDEL APAGTGVSRE AVSGLLIMGA GGGSLIVLSM
LLLRRKKPYG AISHGVVEVD PMLTLEEQQL RELQRHGYEN PTYRFLEERP


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U0946h CLIA A4,ABPP,AD1,Alzheimer disease amyloid protein,Amyloid beta A4 protein,APP,APP,APPI,Cerebral vascular amyloid peptide,CVAP,Homo sapiens,Human,PN-II,PreA4,Protease nexin-II 96T
20-272-191483 beta Amyloid 1-40 - Mouse monoclonal [4H308] to beta Amyloid 1-40; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 Monoclon 0.05 ml
20-272-191484 beta amyloid 1-43 - Mouse monoclonal [4H309] to beta amyloid 1-43; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 Monoclon 0.05 ml
18-272-197116 beta Amyloid - Rabbit polyclonal to beta Amyloid; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 Polyclonal 0.1 mg
20-272-190774 beta Amyloid - Mouse monoclonal [2C8] to beta Amyloid; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 Monoclonal 0.05 mg


 

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