ID L8J2B5_9CETA Unreviewed; 763 AA.
AC L8J2B5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Amyloid-like protein 2 {ECO:0000313|EMBL:ELR62373.1};
GN ORFNames=M91_09773 {ECO:0000313|EMBL:ELR62373.1};
OS Bos mutus (wild yak).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR62373.1, ECO:0000313|Proteomes:UP000011080};
RN [1] {ECO:0000313|EMBL:ELR62373.1, ECO:0000313|Proteomes:UP000011080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX PubMed=22751099; DOI=10.1038/ng.2343;
RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA Wang J., Liu J.;
RT "The yak genome and adaptation to life at high altitude.";
RL Nat. Genet. 44:946-949(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane 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 EMBL; JH880348; ELR62373.1; -; Genomic_DNA.
DR RefSeq; XP_005887592.1; XM_005887530.2.
DR AlphaFoldDB; L8J2B5; -.
DR STRING; 72004.ENSBMUP00000034376; -.
DR MEROPS; I02.016; -.
DR Ensembl; ENSBMUT00000039543; ENSBMUP00000034376; ENSBMUG00000025583.
DR GeneID; 102277640; -.
DR KEGG; bom:102277640; -.
DR CTD; 334; -.
DR OrthoDB; 2907766at2759; -.
DR Proteomes; UP000011080; Unassembled WGS sequence.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0004867; F:serine-type endopeptidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR CDD; cd22607; Kunitz_ABPP-like; 1.
DR Gene3D; 6.10.250.1670; -; 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 Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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 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; ALZHEIMER'S DISEASE BETA-AMYLOID RELATED; 1.
DR PANTHER; PTHR23103:SF14; AMYLOID-LIKE PROTEIN 2; 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; 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; SSF56491; A heparin-binding domain; 1.
DR SUPFAM; SSF89811; Amyloid beta a4 protein copper binding domain (domain 2); 1.
DR SUPFAM; SSF57362; BPTI-like; 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.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011080};
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..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..763
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003992591"
FT TRANSMEM 697..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..205
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 313..363
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 376..567
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 46..139
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 147..205
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 212..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 116..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 149..203
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 160..190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 174..202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 763 AA; 86797 MW; D8B5E023899CB8DA CRC64;
MAATGTAATA ATGKLLVLLL LGLTAPAAAL AGYIEALAAS AGTGFAVAEP QIAMFCGKLN
MHVNIQTGRW EPDPSGTQSC FGTKEEVLQY CQEMYPELQI TNVMEANQPV SVDNWCRRDK
KQCKSHIVIP FKCLVGEFVS DVLLVPEKCL FFHKERMEVC ENHQRWHTVV KEACLTQEMT
LYSYSMLLPC GVDQFHGTEY VCCPQTKVVQ TAVSKEDEED DDDNDDEDQE EDYDVYKSEF
PTEADLEDFT EATADEEDDD EEEEEGEEEV VEDRDYYYDT FKGDDYNEES PTEPSSYRAA
AEEEITHDVR AVCSQEALTG PCRAVMPRWY FDLSKGKCVR FIYGGCGGNR NNFESEDYCM
AVCKAMIPPT PLPTNDVDVY FETSADDNEH ARFQKAKEQL EIRHRNRMDR VKKEWEEAEL
QAKNLPKAER QTLIQHFQAM VKALEKEAAS EKQQLVETHL ARVEAMLNDR RRVALENYLA
ALQSDPPRPH RILQALRRYV RAENKDRLHT LRHYQHVLAV DPEKAAQMRS QVMTHLHVIE
ERRNQSLSLL YKVPYVAQEI QEEIDELLQE QRADMDQFSS SFSETPVDVR VSSEESDEIP
PFHSLHPFPS LPENEDSQPE LFHPMKKGSA LGEQDGGLIG AEEKVINSKK KVDENMVIDE
TLDVKEMIFN AERVGGLEEE PESVGPLRED FSLSSSALIG LLVVAVAIAT IIVISLVMLR
RRQYGSISHG IVEVDPMQER HLSKMQNHGY ENPTYKYLEQ MQI
//