ID A0A3B3XDN8_9TELE Unreviewed; 755 AA.
AC A0A3B3XDN8;
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 Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000013162.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000013162.1}
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 RefSeq; XP_014845092.1; XM_014989606.1.
DR AlphaFoldDB; A0A3B3XDN8; -.
DR STRING; 48701.ENSPMEP00000013162; -.
DR Ensembl; ENSPMET00000020816.1; ENSPMEP00000013162.1; ENSPMEG00000015493.1.
DR GeneID; 106919325; -.
DR CTD; 336266; -.
DR OrthoDB; 3035117at2759; -.
DR Proteomes; UP000261480; 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: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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..755
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017258138"
FT DOMAIN 49..150
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 177..288
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 309..409
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 419..527
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DISULFID 75..139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 88..149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 119..129
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 254..264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 334..398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 347..408
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 378..388
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 495..505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 755 AA; 84099 MW; DB64EB736EC36790 CRC64;
MMEKSRHTRQ LAVSLLFGLW FPCCLSQTTA PSRASVALTP SAAPQQLKVR LAGYPRKHNE
GRIELFYKGE WGTICDDDFS IANANVLCRQ LGFVSATGWT HSAKYGNGQG KIWLDNVLCN
GGEKSIDLCK SRGWGNSDCT HDEDAGVVCK DERIPGFVDS NIIDAQVDEK KVEEVRLRPV
VGTARRKLPI TEGVVEVKHK DGWAQICDVG WTVKNTRVVC GMLGFPHERK VNKNFYKLYL
ERQKNLYLLR SVACLGSEVH LAACPLEFNR PNATATCAGG MPVVVSCMPG PLFMQNSSLK
KKVKVSSNVR LKGGARLGEG RVEVLKDNEW GTVCDDRWSL LSASVVCREL GFGSAKEALT
GARMGQGMGP IYMNEVKCVG NEKSIWNCPF KNITAEDCQH MEDAAVRCNI PYMGLENSIR
ITGGRSRFEG RVEVLSSDAN GTESWGLICG ETWTTREAMV ACRQLGLGYA NQGLQETWYW
DSSNVTEMVM SGVKCTGSEM ALSQCQHHKT VNCQKAAAKF SAGVICSETA SDLVLNASLV
EQTVYIEDRP LHMLYCAAEE DCLSKSAAKA NWPYGHRRLL RFSSQIHNIG RADFKPKAGR
HSWVWHACHG HYHSMDVFTH YDLLNANGSK VAEGHKASFC LEDTECQEGV SKRYECANFG
DQGITVGCWD LYRHDIDCQW LDITDVKPGN YIMQVVINPN YEVAESDFTN NGMKCNCKYD
GHRIWLHNCH IGDAFSEEAE KRFEKYPGQI NNRIS
//
