ID Q60709_MOUSE Unreviewed; 751 AA.
AC Q60709;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 10-MAY-2017, entry version 129.
DE SubName: Full=Amyloid-like protein 2 {ECO:0000313|Ensembl:ENSMUSP00000072428};
DE SubName: Full=Amyloid-like protein 2, isoform 751 {ECO:0000313|EMBL:AAA50603.1};
GN Name=Aplp2 {ECO:0000313|Ensembl:ENSMUSP00000072428,
GN ECO:0000313|MGI:MGI:88047};
GN Synonyms=APLP2 {ECO:0000313|EMBL:AAA50603.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000313|EMBL:AAA50603.1}
RP NUCLEOTIDE SEQUENCE OF 1-229.
RC STRAIN=ICR {ECO:0000313|EMBL:AAA50603.1};
RX PubMed=8300594;
RA Slunt H.H., Thinakaran G., Von Koch C., Lo A.C., Tanzi R.E.,
RA Sisodia S.S.;
RT "Expression of a ubiquitous, cross-reactive homologue of the mouse
RT beta-amyloid precursor protein (APP).";
RL J. Biol. Chem. 269:2637-2644(1994).
RN [2] {ECO:0000313|EMBL:AAA50603.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ICR {ECO:0000313|EMBL:AAA50603.1};
RX PubMed=8071334;
RA Thinakaran G., Sisodia S.S.;
RT "Amyloid precursor-like protein 2 (APLP2) is modified by the addition
RT of chondroitin sulfate glycosaminoglycan at a single site.";
RL J. Biol. Chem. 269:22099-22104(1994).
RN [3] {ECO:0000313|EMBL:AAA50603.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ICR {ECO:0000313|EMBL:AAA50603.1};
RA Slunt H.H., Von Koch C., Sisodia S.S.;
RT "Mouse Amyloid Precursor-Like Protein 2 (APLP2) mRNA, isoform APLP2-
RT 751,complete cds.";
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000072428, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000072428,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0000213|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and
RT expression.";
RL Cell 143:1174-1189(2010).
RN [6] {ECO:0000313|Ensembl:ENSMUSP00000072428}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000072428};
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AC114542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U15571; AAA50603.1; -; mRNA.
DR PIR; A49974; A49974.
DR RefSeq; NP_001095925.1; NM_001102455.1.
DR UniGene; Mm.19133; -.
DR STRING; 10090.ENSMUSP00000072428; -.
DR MEROPS; I02.016; -.
DR Ensembl; ENSMUST00000072634; ENSMUSP00000072428; ENSMUSG00000031996.
DR GeneID; 11804; -.
DR UCSC; uc009orm.1; mouse.
DR CTD; 334; -.
DR MGI; MGI:88047; Aplp2.
DR eggNOG; KOG3540; Eukaryota.
DR eggNOG; ENOG410ZW2A; LUCA.
DR GeneTree; ENSGT00530000063252; -.
DR HOVERGEN; HBG000051; -.
DR OMA; TLYSYGM; -.
DR OrthoDB; EOG091G0UW4; -.
DR TreeFam; TF317274; -.
DR ChiTaRS; Aplp2; mouse.
DR Proteomes; UP000000589; Chromosome 9.
DR Bgee; ENSMUSG00000031996; -.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.1490.140; -; 1.
DR Gene3D; 3.90.570.10; -; 1.
DR Gene3D; 4.10.410.10; -; 1.
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; IPR019744; Amyloid_glyco_extracell_CS.
DR InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR InterPro; IPR019745; Amyloid_glyco_intracell_CS.
DR InterPro; IPR019543; APP_amyloid_C.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
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; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00203; AMYLOIDA4.
DR PRINTS; PR00759; BASICPTASE.
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 Complete proteome {ECO:0000313|Proteomes:UP000000589};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0000213|MaxQB:Q60709,
KW ECO:0000213|PeptideAtlas:Q60709};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}.
FT CHAIN 32 751 {ECO:0000256|SAM:SignalP}.
FT /FTId=PRO_5010141107.
FT TRANSMEM 682 704 Helical. {ECO:0000256|SAM:Phobius}.
FT DOMAIN 310 360 BPTI/Kunitz inhibitor.
FT {ECO:0000259|PROSITE:PS50279}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 310 360 iprf:BPTI_KUNITZ_2 [T]
FT MYHIT 366 547 ipfam:APP_E2 [T]
FT MYHIT 697 747 ipfam:APP_amyloid [T]
FT MYHIT 49 147 ipfam:APP_N [T]
FT MYHIT 338 356 ipat:BPTI_KUNITZ_1 [T]
FT MYHIT 308 361 ismart:KU [T]
FT MYHIT 42 204 ismart:A4_EXTRA [T]
FT MYHIT 148 204 ipfam:APP_Cu_bd [T]
FT MYHIT 737 744 ipat:A4_INTRA [T]
FT MYHIT 309 361 ipfam:Kunitz_BPTI [T]
FT MYHIT 197 204 ipat:A4_EXTRA [T]
SQ SEQUENCE 751 AA; 85248 MW; D183F6A4AD17BC04 CRC64;
MAATGTAAAA ATGKLLVLLL LGLTAPAAAL AGYIEALAAN AGTGFAVAEP QIAMFCGKLN
MHVNIQTGKW EPDPTGTKSC LGTKEEVLQY CQEIYPELQI TNVMEANQPV NIDSWCRRDK
RQCKSHIVIP FKCLVGEFVS DVLLVPDNCQ FFHQERMEVC EKHQRWHTLV KEACLTEGLT
LYSYGMLLPC GVDQFHGTEY VCCPQTKTVD SDSTMSKEEE EEEEDEEDEE EDYDLDKSEF
PTEADLEDFT EAAADEEEED EEEGEEVVED RDYYYDPFKG DDYNEENPTE PSSEGTISDK
EIVHDVKAVC SQEAMTGPCR AVMPRWYFDL SKGKCVRFIY GGCGGNRNNF ESEDYCMAVC
KAMIPPTPLP TNDVDVYFET SADDNEHARF QKAKEQLEIR HRNRMDRVKK EWEEAELQAK
NLPKTERQTL IQHFQAMVKA LEKEAASEKQ QLVETHLARV EAMLNDRRRI ALENYLAALQ
SDPPRPHRIL QALRRYVRAE NKDRLHTIRH YQHVLAVDPE KAAQMKSQVM THLHVIEERR
NQSLSLLYKV PYVAQEIQEE IDELLQEQRA DMDQFTSSIS ENPVDVRVSS EESEEIPPFH
PLHPFPSLSE NEGSGMAEQD GGLIGAEEKV INSKNKMDEN MVIDETLDVK EMIFNAERVG
GLEEEPESVG PLREDFSLSS NALIGLLVIA VAIATVIVIS LVMLRKRQYG TISHGIVEVD
PMLTPEERHL NKMQNHGYEN PTYKYLEQMQ I
//
|
