ID A0A3B3D6R4_ORYME Unreviewed; 726 AA.
AC A0A3B3D6R4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:ENSOMEP00000025783.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000025783.1}
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}.
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DR AlphaFoldDB; A0A3B3D6R4; -.
DR Ensembl; ENSOMET00000006236.1; ENSOMEP00000025783.1; ENSOMEG00000007284.1.
DR GeneTree; ENSGT00940000155874; -.
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 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:SF7; LYSYL OXIDASE HOMOLOG 2A; 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..726
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017203357"
FT DOMAIN 34..135
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 159..261
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 285..384
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 394..503
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DISULFID 60..124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 73..134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 104..114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 226..236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 354..364
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 470..480
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 726 AA; 80760 MW; 002BEFC73788930A CRC64;
MLAPPGTCCL LSGLLCMLVL CSAQSNSASP VIQLRLAGEK RKHYEGRVEV FYNGEWGTVC
DDDFSIYAAH VVCRELGFLD AQAWSPSAKY GRGEGRIWLD NVHCSGSEKS LAQCESNGFG
VSDCKHSEDV GVVCSTKRIP GFKFIRNEIH NDQVEDVRIR ATYSHRKRVP ITEGFVEVKD
GGKWRQICNE GWTEMNSRVI CGMYGFPGEK KTRRLTKNYW GFGVNCTGNE ADLSDCKLGR
EIKLKGNGTC GRGMPAVISC VPGRAFAPSV SIGFRKAYRV EQPLVRLRGG AMIGEGRVEV
LRNGEWGTIC DDNWNIRAAT VVCRELGFGS AKEALSGAKM GQGIGPVHMN EVECSGFEKS
LTECSFNQQS LGCSHEEDVA VKCNVPAMGF NKKLRLSGGR NPYEGRVEVL TERNGLLTWG
SVCSDSWGTM EAMVVCRQLG LGFASHAFQE TWYWQGDAST DAVVMSGVRC SGTELTLDQC
LHHGVFVDCP KGGGRFAAGV SCTQTAPDLV LNAPVVEQTT YLEDRPLYAL QCAMEENCLS
SAASKADPTS YRRLLRFSSQ IHNNGLSDFR PRAAHHSWTW HECHRHYHSM EVFTHYDLLS
LNGTKVAEGH KASFCLEDTQ CDEGIQKRYE CANFGSQGIT VGCWDTYRHD IDCQWIDITD
VKPGDYIFQV VINPNYEVAE SDYTNNVMKC QTRYDGHRIW TYNCHIGETF KIKPAAFHDY
VKKLQF
//
