GenomeNet

Database: UniProt
Entry: A0A0A0MUW3_PAPAN
LinkDB: A0A0A0MUW3_PAPAN
Original site: A0A0A0MUW3_PAPAN 
ID   A0A0A0MUW3_PAPAN        Unreviewed;       653 AA.
AC   A0A0A0MUW3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Amyloid beta precursor like protein 1 {ECO:0000313|Ensembl:ENSPANP00000003895.2};
GN   Name=APLP1 {ECO:0000313|Ensembl:ENSPANP00000003895.2};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000003895.2, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000003895.2, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000003895.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       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   RefSeq; XP_003915417.1; XM_003915368.2.
DR   AlphaFoldDB; A0A0A0MUW3; -.
DR   Ensembl; ENSPANT00000007410.3; ENSPANP00000003895.2; ENSPANG00000007946.3.
DR   GeneID; 101013794; -.
DR   KEGG; panu:101013794; -.
DR   CTD; 333; -.
DR   eggNOG; KOG3540; Eukaryota.
DR   GeneTree; ENSGT00530000063252; -.
DR   HOGENOM; CLU_014607_2_0_1; -.
DR   OMA; CLRDPQH; -.
DR   OrthoDB; 2907766at2759; -.
DR   Proteomes; UP000028761; Chromosome 20.
DR   Bgee; ENSPANG00000007946; Expressed in lateral globus pallidus and 56 other cell types or tissues.
DR   ExpressionAtlas; A0A0A0MUW3; baseline.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031694; F:alpha-2A adrenergic receptor binding; IEA:Ensembl.
DR   GO; GO:0031695; F:alpha-2B adrenergic receptor binding; IEA:Ensembl.
DR   GO; GO:0031696; F:alpha-2C adrenergic receptor binding; IEA:Ensembl.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0071874; P:cellular response to norepinephrine stimulus; IEA:Ensembl.
DR   GO; GO:0180011; P:cytoplasmic polyadenylation; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0006417; P:regulation of translation; IEA:Ensembl.
DR   CDD; cd21708; JMTM_APLP1; 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   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   PANTHER; PTHR23103; ALZHEIMER'S DISEASE BETA-AMYLOID RELATED; 1.
DR   PANTHER; PTHR23103:SF13; AMYLOID BETA PRECURSOR LIKE PROTEIN 1; 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   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000028761};
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..38
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           39..653
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014136985"
FT   TRANSMEM        584..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          50..212
FT                   /note="E1"
FT                   /evidence="ECO:0000259|PROSITE:PS51869"
FT   DOMAIN          295..486
FT                   /note="E2"
FT                   /evidence="ECO:0000259|PROSITE:PS51870"
FT   REGION          50..146
FT                   /note="GFLD subdomain"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT   REGION          154..212
FT                   /note="CuBD subdomain"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT   REGION          214..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        156..210
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT   DISULFID        167..197
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT   DISULFID        181..209
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ   SEQUENCE   653 AA;  72572 MW;  77BE1E4A67B8D52E CRC64;
     MGPASPAARG LSRRPGQPPL PLLLPLLLLL LRAQPAIGSL AGGSPGAAEA PGSAQVAGLC
     GRLTLHRDLR TGRWEPDPQR SRRCLRDPQR VLEYCRQMYP ELQIARVEQA TQAIPMERWC
     GGARSGSCTH PHHQVVPFRC LPGEFVSEAL LVPEGCRFLH QERMDQCESS TRRHQEAQEA
     CSSQGFILHG SGMLLPCGSD RFRGVEYVCC PPPGTPDPSG TAVGDPSTRS WPLGSRVEGA
     EDEEEEESFP QPVDDYFVEP PQAEEEEEEE RVPPPSSHTL AVVSKVTPTP RPTDGVDIYF
     GMPGEISEHE GFLRAKMDLE ERRMRQINEV MREWAMADNQ SKNLPKADRQ ALNEHFQSIL
     QTLEEQVSGE RQRLVETHAT RVIALINDQR RAALEGFLAA LQGDPPQAER VLTALRHYLR
     AEQKEQRHTL RHYQHVAAVD PEKAQQMRFQ VQTHLQVIEE RVNQSLGLLD QNPHLAQELR
     PQIQELLHSE YLGPSELEAP APGGSSEDKG GLQPPDSKDA DTPMTLPKGS TEQDAASPEK
     EKMSPLEQYE QKVNASVPRG FPFHSSEIQR DELAPAGTGV SREAVSGLLI MGAGGGSLIV
     LSMLLLRRKK PYGAISHGVV EVDPMLTLEE QQLRELQRHG YENPTYRFLE ERP
//
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