ID A0A3Q1J7K2_ANATE Unreviewed; 753 AA.
AC A0A3Q1J7K2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000027219.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000027219.2}
RP IDENTIFICATION.
RG Ensembl;
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|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; A0A3Q1J7K2; -.
DR STRING; 64144.ENSATEP00000027219; -.
DR Ensembl; ENSATET00000027649.2; ENSATEP00000027219.2; ENSATEG00000018763.2.
DR GeneTree; ENSGT00940000158157; -.
DR Proteomes; UP000265040; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW 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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..753
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030080276"
FT DOMAIN 45..146
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 169..282
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 71..135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 84..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 115..125
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 248..258
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; 84223 MW; 56348F65D4ACF854 CRC64;
CFGKITLLFG LWLPCCLTQT TTPNPATVTP KPSPSSQSQT ERLKVRLAGY PRKHNEGRIE
LFYKGEWGTI CDDDFSISNA NVLCRQLGFV SATGWTHSAK YGKGQGKIWL DNVLCNGGEK
SIEFCKSRGW GNSDCTHDED AGVVCKDERI PGFVDSNIID VDESKIEEVR LRPVVAMAKK
KLPITEGVVE VKYKDGWAQI CDLGWTIKNT RVVCGMLGFP HERKVNKNFY KLYLERQKNY
FHVHSVACTG MEVHLAACPL EFSKPNATSS CEGGMAAVVS CMPGPQFMQN SGLKKKLKNS
FQSFSNVRLK GGARLGEGRV EVLKDNEWGT MCDDRWNLLS ASVVCRELGY GSAKEALTGA
RMGQGMGPIY MNEVKCLGHE KSIWNCPFKN ITSEDCQHTE DAAVRCNVPY MGLENSIRIT
GGRTRYEGRV EVLSTDSNGT QSWGLICGEN WSTTEAMVAC RQLGLGYANQ GLQETWYWDS
SNVTEMVMSG VKCTGNEMAL SHCQHHKTVS CQRAAAKFAA GVICSETASD LVLNAPLVQQ
TVYIEDRPLH MLYCAAEEDC LSKSAAKANW PYGHRRLLRF SSQIHNIGRA DFKPKAGRHS
WVWHACHGHY HSMDVFTHYD LLNANGTKVA EGHKASFCLE DTDCQEGVSK RYECANFGDQ
GITVGCWDLY RHDIDCQWLD ITDVKPGNYI MQVVINPNHE VAESDFTNNA MKCNCKYDGH
RIWLHNCHIG DAFSEEAERR FEKYPGQLNN QVY
//
