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Database: UniProt
Entry: A0A3B3TGB6_9TELE
LinkDB: A0A3B3TGB6_9TELE
Original site: A0A3B3TGB6_9TELE 
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
//
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