ID   E9PG40_HUMAN            Unreviewed;       714 AA.
AC   E9PG40;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   13-FEB-2019, entry version 68.
DE   SubName: Full=Amyloid-beta precursor protein {ECO:0000313|Ensembl:ENSP00000398879};
GN   Name=APP {ECO:0000313|Ensembl:ENSP00000398879};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000398879, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000398879, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RG   Chromosome 21 mapping and sequencing consortium;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA   Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA   Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA   Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA   Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA   Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA   Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA   Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA   Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA   Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA   Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA   Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [2] {ECO:0000213|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [3] {ECO:0000313|Ensembl:ENSP00000398879}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [4] {ECO:0000213|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
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DR   EMBL; AP001442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF457122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF457123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF457130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF510514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001129602.1; NM_001136130.2.
DR   UniGene; Hs.434980; -.
DR   ProteinModelPortal; E9PG40; -.
DR   SMR; E9PG40; -.
DR   jPOST; E9PG40; -.
DR   MaxQB; E9PG40; -.
DR   PeptideAtlas; E9PG40; -.
DR   PRIDE; E9PG40; -.
DR   DNASU; 351; -.
DR   Ensembl; ENST00000439274; ENSP00000398879; ENSG00000142192.
DR   GeneID; 351; -.
DR   UCSC; uc011ach.3; human.
DR   CTD; 351; -.
DR   EuPathDB; HostDB:ENSG00000142192.20; -.
DR   HGNC; HGNC:620; APP.
DR   OpenTargets; ENSG00000142192; -.
DR   eggNOG; KOG3540; Eukaryota.
DR   eggNOG; ENOG410ZW2A; LUCA.
DR   GeneTree; ENSGT00530000063252; -.
DR   OrthoDB; 953529at2759; -.
DR   ChiTaRS; APP; human.
DR   GenomeRNAi; 351; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   Bgee; ENSG00000142192; Expressed in 242 organ(s), highest expression level in frontal cortex.
DR   ExpressionAtlas; E9PG40; baseline and differential.
DR   Genevisible; E9PG40; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; IEA:InterPro.
DR   CDD; cd00109; KU; 1.
DR   Gene3D; 1.20.120.770; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.30.1490.140; -; 1.
DR   Gene3D; 3.90.570.10; -; 1.
DR   Gene3D; 4.10.230.10; -; 1.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR036669; Amyloid_Cu-bd_sf.
DR   InterPro; IPR008155; Amyloid_glyco.
DR   InterPro; IPR013803; Amyloid_glyco_Abeta.
DR   InterPro; IPR037071; Amyloid_glyco_Abeta_sf.
DR   InterPro; IPR011178; Amyloid_glyco_Cu-bd.
DR   InterPro; IPR024329; Amyloid_glyco_E2_domain.
DR   InterPro; IPR008154; Amyloid_glyco_extra.
DR   InterPro; IPR019744; Amyloid_glyco_extracell_CS.
DR   InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR   InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
DR   InterPro; IPR019745; Amyloid_glyco_intracell_CS.
DR   InterPro; IPR028866; APP.
DR   InterPro; IPR019543; APP_amyloid_C.
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; PTHR23103; 1.
DR   PANTHER; PTHR23103:SF7; PTHR23103:SF7; 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; PF03494; Beta-APP; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   PRINTS; PR00203; AMYLOIDA4.
DR   PRINTS; PR00759; BASICPTASE.
DR   PRINTS; PR00204; BETAAMYLOID.
DR   SMART; SM00006; A4_EXTRA; 1.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF109843; SSF109843; 1.
DR   SUPFAM; SSF56491; SSF56491; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   SUPFAM; SSF89811; SSF89811; 1.
DR   PROSITE; PS00319; A4_EXTRA; 1.
DR   PROSITE; PS00320; A4_INTRA; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0000213|EPD:E9PG40,
KW   ECO:0000213|MaxQB:E9PG40, ECO:0000213|PeptideAtlas:E9PG40};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    714       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003242798.
FT   TRANSMEM    645    667       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      235    285       BPTI/Kunitz inhibitor.
FT                                {ECO:0000259|PROSITE:PS50279}.
FT   COILED      172    192       {ECO:0000256|SAM:Coils}.
FT   COILED      343    363       {ECO:0000256|SAM:Coils}.
FT   COILED      369    403       {ECO:0000256|SAM:Coils}.
FT   COILED      499    519       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   714 AA;  80833 MW;  68CC52E6F29B777B CRC64;
     MLPGLALLLL AAWTARALEV YPELQITNVV EANQPVTIQN WCKRGRKQCK THPHFVIPYR
     CLVGEFVSDA LLVPDKCKFL HQERMDVCET HLHWHTVAKE TCSEKSTNLH DYGMLLPCGI
     DKFRGVEFVC CPLAEESDNV DSADAEEDDS DVWWGGADTD YADGSEDKVV EVAEEEEVAE
     VEEEEADDDE DDEDGDEVEE EAEEPYEEAT ERTTSIATTT TTTTESVEEV VREVCSEQAE
     TGPCRAMISR WYFDVTEGKC APFFYGGCGG NRNNFDTEEY CMAVCGSAMS QSLLKTTQEP
     LARDPVKLPT TAASTPDAVD KYLETPGDEN EHAHFQKAKE RLEAKHRERM SQVMREWEEA
     ERQAKNLPKA DKKAVIQHFQ EKVESLEQEA ANERQQLVET HMARVEAMLN DRRRLALENY
     ITALQAVPPR PRHVFNMLKK YVRAEQKDRQ HTLKHFEHVR MVDPKKAAQI RSQVMTHLRV
     IYERMNQSLS LLYNVPAVAE EIQDEVDELL QKEQNYSDDV LANMISEPRI SYGNDALMPS
     LTETKTTVEL LPVNGEFSLD DLQPWHSFGA DSVPANTENE VEPVDARPAA DRGLTTRPGS
     GLTNIKTEEI SEVKMDAEFR HDSGYEVHHQ KLVFFAEDVG SNKGAIIGLM VGGVVIATVI
     VITLVMLKKK QYTSIHHGVV EVDAAVTPEE RHLSKMQQNG YENPTYKFFE QMQN
//