ID A0A1S3A0T5_ERIEU Unreviewed; 376 AA.
AC A0A1S3A0T5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
GN Name=LOX {ECO:0000313|RefSeq:XP_007527591.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007527591.1};
RN [1] {ECO:0000313|RefSeq:XP_007527591.1}
RP IDENTIFICATION.
RG RefSeq;
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|ARBA:ARBA00036237,
CC ECO:0000256|RuleBase:RU367046};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935,
CC ECO:0000256|RuleBase:RU367046};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239, 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|ARBA:ARBA00007492, ECO:0000256|RuleBase:RU367046}.
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DR RefSeq; XP_007527591.1; XM_007527529.2.
DR AlphaFoldDB; A0A1S3A0T5; -.
DR CTD; 4015; -.
DR OrthoDB; 3035117at2759; -.
DR Proteomes; UP000079721; 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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001695; Lysyl_oxidase.
DR InterPro; IPR019828; Lysyl_oxidase_CS.
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.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU367046};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW LTQ {ECO:0000256|ARBA:ARBA00022477, ECO:0000256|RuleBase:RU367046};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367046};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367046};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU367046};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|RuleBase:RU367046}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..376
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010298964"
FT REGION 24..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 376 AA; 42430 MW; 3FFE18F0A96EA120 CRC64;
MRFALTALLL GPLQLCALLR CTPPAAGQQQ PPRSPPAAPS ASTAAQPRTR ILLLRNNRTG
AAERTRTPGP SGAVAGRPRP TARHWFQAGY SSGARDAGAP RSGNWTAPAE RPVLSNLRPP
SRVEGMVGDD PYNPYKYSDD NPYYNYYDTY ERPRPGSRYR PGYGTGYFQY GLPDLVPDPY
YIQASTYVQR MSMYNLRCAA EENCLASSAY RSDVRDYDHR VLLRFPQRVK NQGTSDFLPS
RPRYSWEWHS CHQHYHSMDE FSHYDLLDAN TQRRVAEGHK ASFCLEDTSC DYGYHRRFAC
TAHTQGLSPG CYDTYNADID CQWIDITDVQ PGNYILKVSV NPSYLVPESD YTNNVVRCDI
RYTGHHAYAS GCTISP
//
