ID A0A3M0JEM2_HIRRU Unreviewed; 289 AA.
AC A0A3M0JEM2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
GN ORFNames=DUI87_26423 {ECO:0000313|EMBL:RMB97139.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB97139.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMB97139.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMB97139.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMB97139.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RMB97139.1}.
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DR EMBL; QRBI01000169; RMB97139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0JEM2; -.
DR STRING; 333673.A0A3M0JEM2; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
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; 3.
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:UP000269221};
KW Secreted {ECO:0000256|RuleBase:RU367046};
KW TPQ {ECO:0000256|RuleBase:RU367046}.
SQ SEQUENCE 289 AA; 33244 MW; C8165A1073ECB451 CRC64;
MLNLLSLAKK TASLRKPFQD AFNPTVCVIK KGGRSQNPQC NKYPGIPVIP DRKERETTPY
NPYKYTDDNP YYNYYDTYER PRQGNRYRPG YGTGYFQYGL PDLVPDPYYI QASTYVQRMS
MYNLRCAAEE NCLARHYHSM DEFSHYDLLD ASSHRKVAEG HKASFCLEDT SCDYGYYRRY
ACTAHTQHLL LTTVRDMTLS FDGFVVQLTV AICTHKLGLS PGCYDTYNAD IDCQWIDITD
VKPGNYILKV SVNPSYLVPE SDYSNNIVRC DIRYTGHHAY ASGCTISPY
//
