ID V9KDA3_CALMI Unreviewed; 753 AA. AC V9KDA3; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 02-JUN-2021, entry version 29. DE RecName: Full=Amyloid-beta A4 protein {ECO:0000256|RuleBase:RU367156}; 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 -!- FUNCTION: Functions as a cell surface receptor and performs CC physiological functions on the surface of neurons relevant to neurite CC growth, neuronal adhesion and axonogenesis. CC {ECO:0000256|RuleBase:RU367156}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367156}; CC Single-pass type I membrane protein {ECO:0000256|RuleBase:RU367156}. 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|ARBA:ARBA00009449, CC ECO:0000256|PROSITE-ProRule:PRU01217, ECO:0000256|RuleBase:RU367156}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01217}. 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:0005798; C:Golgi-associated vesicle; IEA:UniProtKB-UniRule. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-UniRule. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. 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; 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 2: Evidence at transcript level; KW Amyloid {ECO:0000256|RuleBase:RU367156}; KW Cell membrane {ECO:0000256|RuleBase:RU367156}; KW Coiled coil {ECO:0000256|SAM:Coils}; 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|RuleBase:RU367156}; 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, KW ECO:0000256|RuleBase:RU367156}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU367156}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..753 FT /note="Amyloid-beta A4 protein" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004778687" FT TRANSMEM 684..706 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367156" FT DOMAIN 39..200 FT /note="E1" FT /evidence="ECO:0000259|PROSITE:PS51869" FT DOMAIN 293..343 FT /note="BPTI/Kunitz inhibitor" FT /evidence="ECO:0000259|PROSITE:PS50279" FT DOMAIN 357..548 FT /note="E2" FT /evidence="ECO:0000259|PROSITE:PS51870" FT REGION 39..134 FT /note="GFLD subdomain" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" FT REGION 142..200 FT /note="CuBD subdomain" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" 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 residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 84..128 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" FT DISULFID 109..116 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" FT DISULFID 144..198 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" FT DISULFID 155..185 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" FT DISULFID 169..197 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217" 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 //