ID A0A2T7NF28_POMCA Unreviewed; 760 AA.
AC A0A2T7NF28;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=C0Q70_20280 {ECO:0000313|EMBL:PVD19789.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD19789.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD19789.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD19789.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD19789.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD19789.1}.
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DR EMBL; PZQS01000013; PVD19789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7NF28; -.
DR STRING; 400727.A0A2T7NF28; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg13.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.450.40; -; 2.
DR Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 2.
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 PANTHER; PTHR10638:SF20; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 2.
DR Pfam; PF02727; Cu_amine_oxidN2; 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:UP000245119};
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 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..175
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 347..621
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT DOMAIN 623..720
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 507
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 507
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 760 AA; 86697 MW; 0E71B811E2D76FD4 CRC64;
MKQTSAYQIL LTLSLFVNAG LIVAIIFTAL RKSDYSDIIN TDVCTTGQSD IRIVVSDNDR
EWETLSSNPS ANKKARKPKQ YENVFKDLTK EEIWAVLDYM YKVHDLGLVK PYEANVTDNS
ILFVELYVPN KAEVLAYLSG NSSRPLRQAK VVTLEPLASP PRVMEYVVTP LPNPTMHFPN
PRRVKQVPFR VRPPGNAEMA ALVTLLRSYM RPQMEELLKE LYGASFVDCA DRCLTITATP
VSTAFSLERR IWVQVLYQVE FSTLYPVGLQ FLVNSQTSNT ENWRIEKIQF TNLTFASFDD
LMEQHQKGLL PKISVHYPQP KGEASHIAGM LSLRGQFFPS EPLAKPRQYQ PNGNRFSIRE
QRVTYHQWQF SWRMSVVSGI QLFDVTYANE RVVYELSLQE VVVLYSGANP VVSFSQIMDS
YLGLGAHAHG LMPDVDCPEY ATFQDTVLLT ELFNEPHVYP SAVCLFEHNT QTPLRRHKSN
SFSSGFFYGG LVDTVLVLRT CYTLFNYDYL VDFVFHNNGV LETIVRSSGY IIGSLRSTAE
APFGFRVHDD LLGNLHQHLF NFKVDVDVVD AGNRYQTLDL QVDNRSWPWT PPGQPFYQTT
MRKNLRRTEK SAALRHDASS GLTYHSLRWA RWQLAVTRRK EQEEFSSSMY AQFDAADPVV
DFQNFIDDNE DIVDQDLVAW VTVGMHHIPH AEDVPNTATP GKELTFALIP FNFFGEDPSM
ASRDAVRVDA ETENNSLKME RYGMPPFTTV YHLPTTTQLS
//
