ID F7FA83_MONDO Unreviewed; 800 AA.
AC F7FA83;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN Name=AOC1 {ECO:0000313|Ensembl:ENSMODP00000004538.4};
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000004538.4, ECO:0000313|Proteomes:UP000002280};
RN [1] {ECO:0000313|Ensembl:ENSMODP00000004538.4, ECO:0000313|Proteomes:UP000002280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17495919; DOI=10.1038/nature05805;
RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT coding sequences.";
RL Nature 447:167-177(2007).
RN [2] {ECO:0000313|Ensembl:ENSMODP00000004538.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU000672};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000256|RuleBase:RU000672};
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51,
CC ECO:0000256|RuleBase:RU000672}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
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 AlphaFoldDB; F7FA83; -.
DR STRING; 13616.ENSMODP00000004538; -.
DR Ensembl; ENSMODT00000004638.4; ENSMODP00000004538.4; ENSMODG00000003706.4.
DR eggNOG; KOG1186; Eukaryota.
DR GeneTree; ENSGT00950000183207; -.
DR HOGENOM; CLU_015739_1_0_1; -.
DR InParanoid; F7FA83; -.
DR OMA; PYNSQDV; -.
DR TreeFam; TF314750; -.
DR Proteomes; UP000002280; Chromosome 8.
DR Bgee; ENSMODG00000003706; Expressed in blood and 7 other cell types or tissues.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0052597; F:diamine oxidase activity; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0008131; F:primary amine oxidase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0048038; F:quinone binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0097185; P:cellular response to azide; IEA:Ensembl.
DR GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
DR GO; GO:0035874; P:cellular response to copper ion starvation; IEA:Ensembl.
DR GO; GO:0071420; P:cellular response to histamine; IEA:Ensembl.
DR GO; GO:0009445; P:putrescine metabolic process; IEA:Ensembl.
DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
DR Gene3D; 3.10.450.40; -; 2.
DR Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638:SF3; AMILORIDE-SENSITIVE AMINE OXIDASE [COPPER-CONTAINING]; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR PRINTS; PR00766; CUDAOXIDASE.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000672};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000672};
KW Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..173
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 189..288
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 348..756
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 509
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 509
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 800 AA; 91209 MW; 3784E4A8CEA2ED58 CRC64;
MQLNTYSFPY FLSAPMYVEL APAMCTSTSS SRWTSLESIL PRTMAQRTLG FAWLLGGLLL
LLTVAIAEHS SWNLRSKATV FADLSPEELR VVQSFLLSKK DLKLAPSKDG TMNKNSIFLI
EMLLPKKHQV LKFLDEGGNR PVREARVIIF FGAQEHPNIT EFAVGPLPWP SYMRMLPPKP
GHSPSWGSRP ITSTEYYLLY HFLQDATEPL YRFFRDTTGF WLHNCTDHCL TFTDVSPRGL
ASGQRSSWFI MQRFVEGYFL HPTGMEILVD HKSSDPQEWR VERVWYNGQF YESPEDLARK
YEQGKVNVVI LEDLPPKGKM GAGTEEQPLF SSYQPRGDFP TPTARPGPHL VEPQGPRYKL
EGNAVLYGGW SFAFRLRSSS GLQILNLRFG GERIAYEVSV QEAVALYGGH TPAGMQTKYI
DVGWGLGSVT HELAPGIDCP KTATFLDAHH FYDANAPTHY PNALCLFEMP TGVPLRRHFD
SDFSGGFNFY AGLEGQVLVL RTTSTVYNYD YLWDFVFHHN GVMEAKMHAT GYVHATFFTP
EGLRHGTRLH THLLGNIHTH LIHYRVDLDV AGTNNGFETM GTKLENITNP WNSHYHVVQP
VLERNPRHRE RHAAFRFGRK LPKFLLFTSP KKNLWGHPRS YRIQLHSMAD QVLPPGWQEE
RTVTWARYPL AVTKYRESEL VSSSIYNQND PWDPPVVFEE FLRNNENIEN EDLVAWVTVG
FLHIPHSEDI PNTATPGNSV GFLLRPFNFF SEDPSLASKE TVIVRSQAKG PNHIERWTSD
NIEGCWKASP FNYNGTYRPV
//