ID A0A3Q3XLZ9_MOLML Unreviewed; 401 AA.
AC A0A3Q3XLZ9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000028269.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000028269.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Mediates the post-translational oxidative deamination of
CC lysine residues on target proteins leading to the formation of
CC deaminated lysine (allysine). {ECO:0000256|RuleBase:RU367046}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-
CC [protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:131803; EC=1.4.3.13;
CC Evidence={ECO:0000256|RuleBase:RU367046};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU367046};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|RuleBase:RU367046}.
CC -!- PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by
CC condensation of the epsilon-amino group of a lysine with a topaquinone
CC produced by oxidation of tyrosine. {ECO:0000256|RuleBase:RU367046}.
CC -!- SIMILARITY: Belongs to the lysyl oxidase family.
CC {ECO:0000256|RuleBase:RU367046}.
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DR AlphaFoldDB; A0A3Q3XLZ9; -.
DR STRING; 94237.ENSMMOP00000028269; -.
DR Ensembl; ENSMMOT00000028749.1; ENSMMOP00000028269.1; ENSMMOG00000021366.1.
DR OMA; GCHMSTY; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IEA:UniProtKB-UniRule.
DR InterPro; IPR001695; Lysyl_oxidase.
DR PANTHER; PTHR45817; LYSYL OXIDASE-LIKE-RELATED; 1.
DR PANTHER; PTHR45817:SF6; PROTEIN-LYSINE 6-OXIDASE; 1.
DR Pfam; PF01186; Lysyl_oxidase; 1.
DR PRINTS; PR00074; LYSYLOXIDASE.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|RuleBase:RU367046};
KW LTQ {ECO:0000256|RuleBase:RU367046};
KW Metal-binding {ECO:0000256|RuleBase:RU367046};
KW Oxidoreductase {ECO:0000256|RuleBase:RU367046};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW Secreted {ECO:0000256|RuleBase:RU367046};
KW TPQ {ECO:0000256|RuleBase:RU367046}.
FT REGION 32..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 46135 MW; 5A790AF1BB41AB05 CRC64;
MGLRVFGTPL YAYACLYFFV FILQAAQSQR DPATQQRGTQ RSPRQTLQWS HNGNIFSILS
HGSEYQPARR RGAPQEQVQA RPITIVRDAK ARQESTSSPP GSQQQQQQPR GREHRQHQHG
RPAERTGTHG GGRANETREK VTVSPPVPRR DDMMVGDDPY DPYKSIDQDN PYYNYHDVYE
RPRSRSRPGY GTRHHQYGLP DLVPDPYYIQ ASAYAQRAPM YNLRCAAEEN CLSSTAYRAR
DYDTRMLLRF PQRVKNQGTA DFLPNRPRYA WEWHSCHQHF HSMDEFSHYE LLDASTHHSV
AEGHKASFCL EDTSCDYGQY RRYACTAHTQ GLSPGCYDTY NADIDCQWID ITDVKPGQYI
LKVSVNPFYQ VPESDYSNNI VRCDVHYTGN YASLSGCHLS T
//
