ID A0A3B3BT81_ORYME Unreviewed; 753 AA.
AC A0A3B3BT81;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000008278.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000008278.1}
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|ARBA:ARBA00001935,
CC 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|ARBA:ARBA00007492, ECO:0000256|RuleBase:RU367046}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B3BT81; -.
DR STRING; 30732.ENSOMEP00000008278; -.
DR PaxDb; 30732-ENSOMEP00000008278; -.
DR Ensembl; ENSOMET00000002716.1; ENSOMEP00000008278.1; ENSOMEG00000009459.1.
DR GeneTree; ENSGT00940000158157; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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 GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR Gene3D; 3.10.250.10; SRCR-like domain; 4.
DR InterPro; IPR001695; Lysyl_oxidase.
DR InterPro; IPR019828; Lysyl_oxidase_CS.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR45817:SF2; LYSYL OXIDASE HOMOLOG 3; 1.
DR PANTHER; PTHR45817; LYSYL OXIDASE-LIKE-RELATED; 1.
DR Pfam; PF01186; Lysyl_oxidase; 1.
DR Pfam; PF00530; SRCR; 4.
DR PRINTS; PR00074; LYSYLOXIDASE.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 4.
DR SUPFAM; SSF56487; SRCR-like; 4.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 4.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU367046};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196};
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU367046};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|RuleBase:RU367046}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..753
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017275815"
FT DOMAIN 47..148
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 175..286
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 307..407
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 417..525
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DISULFID 73..137
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 86..147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 117..127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 252..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 332..396
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 345..406
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 376..386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 493..503
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 753 AA; 83930 MW; 75E95557078C24C7 CRC64;
METSERRKQL AFSLLFGLCF PCCLAQTTTT APTRDTPTPS SQARIKVRLA GYPRKHNEGR
VELFYRGEWG TICDDDFSLA NANVLCRQLG FVSATGWTHS AKYGKGQGKI WLDNVLCNGG
EKSIDSCKSR GWGNSDCTHD EDAGVICKDE RIPGFVDSNI IDAQVDEFKV EEVRLRPVVG
TTRKKMPITE GVVEVKHRNG WAHICDLGWT VQNTRVICGM LGFPHERKVN KNFYKLYLER
QKNHILVHSV SCTGTEVHLA ACPLEYAKPN STSSCLGGMP AVVSCMPGPL FLQNSSLKKK
VKVSANVRLK GGSRVGEGRV EVLRDRDWGT VCDDRWNLQS ASVVCRELGF GTAKEALTGA
RMGQGIGPIH MNEVKCVGHE RSIWTCPYKN ITAEDCQHTE DAAVRCNVPY MGLENSIRIT
GGRTRYEGRV ELLIPDSNGT QGWGLICGET WTTKEASVAC RQLGLGYANQ GLQETWYWDS
SNVTQMVLSG VRCTGEEMSL SQCQHHKTVS CQKSAAKFAA GVICSETASD LVLNAPLVQE
TVYIEDRPLH MLYCAAEEDC LSKSAAKANW PYGHRRLLRF SSEIRNIGRA DFKPKAGRHS
WVWHACHGHY HSMDVFTHYD LLNANGTRVA EGHKASFCLE DTDCQGGVSK RYECANFGDQ
GITVGCWDLY RHDIDCQWID ITDVKPGNYI FQVVINPNYE VAESDFSNNA MKCNCKYDGH
RIWLHNCHLG GALSEEAERL FEKYPGQLNN KVS
//
