ID V9KDA3_CALMI Unreviewed; 753 AA. AC V9KDA3; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 12-AUG-2020, entry version 25. DE RecName: Full=ABPP {ECO:0000256|ARBA:ARBA00018220}; DE AltName: Full=Amyloid precursor protein {ECO:0000256|ARBA:ARBA00017734}; DE AltName: Full=Amyloid-beta A4 protein {ECO:0000256|ARBA:ARBA00016844}; DE AltName: Full=Amyloid-beta precursor protein {ECO:0000256|ARBA:ARBA00021782}; OS Callorhinchus milii (Ghost shark). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus. OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO96226.1}; RN [1] {ECO:0000313|EMBL:AFO96226.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Liver {ECO:0000313|EMBL:AFO96226.1}; RX PubMed=24402279; DOI=10.1038/nature12826; RG International Elephant Shark Genome Sequencing Consortium; RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B., RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W., RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S., RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T., RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T., RA Wilson R.K., Brenner S., Warren W.C.; RT "Elephant shark genome provides unique insights into gnathostome RT evolution."; RL Nature 505:174-179(2014). 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|ARBA:ARBA00009449}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JW863709; AFO96226.1; -; mRNA. DR MEROPS; I02.015; -. 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; 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; 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; 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; APP_CUBD; 1. DR PROSITE; PS00320; APP_INTRA; 1. DR PROSITE; PS00280; BPTI_KUNITZ_1; 1. DR PROSITE; PS50279; BPTI_KUNITZ_2; 1. PE 2: Evidence at transcript level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690}; KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}; 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..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..753 FT /note="ABPP" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004778687" FT TRANSMEM 684..706 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 293..343 FT /note="BPTI/Kunitz inhibitor" FT /evidence="ECO:0000259|PROSITE:PS50279" FT REGION 237..283 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 382..442 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 538..558 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 237..269 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 753 AA; 85057 MW; A31797CD026019F0 CRC64; MFLQPAARLL LLSAIGTVTV SPSALTALEV PTDGGTGLLA AEPQIAMFCD KLNMHMNVQT GKWISDPSGT NSCFGTKEGI LQYCQEVYPD LQITNVVEAN QPVTIQNWCK KGRKQCKGHP HIVIPYRCLV GEFVSDALLV PDKCKFLHRE KMDTCENHLY WHTVAKEACG DKTMNLKDYG MLLPCGIDQF RGVEFVCCPI SEENEKVDSV DVDEEDSYIW WGGADAEYSD GGDKVIEEEP MDEEEEVDIE DDDDEEEDED DEDDDQYEDP TEHTTSSTTT TTEAIEEVVR EVCSEQAETG PCRAMIPRWY FDIGEGKCAQ FIYGGCGGNR NNFDSEEYCL SVCSSVIPAT AASTPDAIDQ YLETPGDENE HAYFQKAKER QEARHRERMS QIMREWEEAE RQARNLHKAD KKAVIQRFQE MVESLEQEAA SERQQLVETH MARVEAMLND RRRIALENYL AALQADPPRP RHVLNALKKY IRAEQKDRQH TLKHFEHVRM VDPKKAAQIK SQVMTHLRVI DERMNQSLSL LYKVPAVAEE IQDEVDELLQ KEQSYIDDMV ANSVSDTRVS YGNDALVPSL SETKTTIELL PDQGEFTLDD LQPLHPFVVD SIPVNTENEV EPVDARPAAD RGLTTRPGSG LTGIKTQEIA EVKMETKFRQ DSGYEVHHQK LVFFPEDVGS NKGAIIGLMV GGVVIATVIV ITLVMLKKKQ YTSIHHGVIE VDAAVTPEER HLSKMQQNGY ENPTYKFFEQ MQN //