ID A0A3B3TGB6_9TELE Unreviewed; 407 AA.
AC A0A3B3TGB6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000041453.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000041453.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B3TGB6; -.
DR STRING; 1676925.ENSPKIP00000041453; -.
DR Ensembl; ENSPKIT00000022488.1; ENSPKIP00000041453.1; ENSPKIG00000017989.1.
DR GeneTree; ENSGT00940000154779; -.
DR OrthoDB; 3035117at2759; -.
DR Proteomes; UP000261540; 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 Secreted {ECO:0000256|RuleBase:RU367046}; Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|RuleBase:RU367046}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..407
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017271993"
FT REGION 59..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 47045 MW; 288D9B345D51947B CRC64;
MRTFVFDVVV FSCAHLCLWS CILQIVHAQD ERRSDPQSGG FLRRFRWEVN GRVHSLLSRA
SQLQAPRRRE DSTGSVRSNP VVIIQSSNET EENSQVGRGD PQRARGQVRG RQWFQAGAAR
RSQQRRPDAE RSPETSDSSR ENTPQFSNLR PENTMVADDP YDPYKSLDEN NPYYNTHDTY
NRQRPDGRQR PGYGTRLFQN GLPDLVPDPY YIQTTTYIQR VPMYNLRCAA EENCLASTAY
RSSVRDWDTR VLLRFPQRVK NQGTADFLPS RPRYAWEWHS CHRHFHSMDQ FSRYDLLERG
SQRKVAEGHK ASFCLEDTSC DPGYYRRFAC TAHTQGLSPG CYDTYNADID CQWIDITDVK
PGTYILKITA NPEFQVPESD FSNNVVRCEV YYTGNYASTS GCHVSPY
//