ID A0A3Q1FYC6_9TELE Unreviewed; 760 AA.
AC A0A3Q1FYC6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000023371.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000023371.1}
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}.
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; A0A3Q1FYC6; -.
DR Ensembl; ENSAPOT00000011431.1; ENSAPOP00000023371.1; ENSAPOG00000005233.1.
DR GeneTree; ENSGT00940000158157; -.
DR Proteomes; UP000257200; 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:UP000257200};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..760
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018665224"
FT DOMAIN 54..155
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 180..293
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 314..414
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 424..532
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT REGION 29..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 80..144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 93..154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 124..134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 259..269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 339..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 352..413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 383..393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 500..510
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 760 AA; 84909 MW; 039445A019DA5CA4 CRC64;
MEKSRRQQRL AFILLFGLWL PCCFTQTTPS NSATPTPTPS PSPSPQPRTE KLKVRLAGYP
RKHNEGRIEL FYKGEWGTIC DDDFSLANAN VLCRQLGFVS ATGWTHSAKY GKGQGKIWLD
NVLCGGGEKS IELCKSRGWG NSDCTHDEDA GVVCKDERIP GFVDSNVIDA HVDENKIEEV
RLRPVVAMAK KKLPITEGVV EVKYKDGWAQ ICDIGWTIKN TRVVCGMLGF PHERKVNKNF
YKLYLERQKN YFHIHSVACL GTEVHLAACP LEFSKANATS ACTGGMPAVV SCMPGPLFMQ
NSGLKKKLKI SSNVRLKGGS RVGEGRVEVL KDNEWGTVCD DRWNLQSASV VCRELGFGSA
KEALTGGRLG QGMGPIYMNE VKCVGQERSI WNCPFKNITS EDCHHMEDAA VRCNIPYMGL
ENTIRITGGR TRYEGRVEVL SVDSNGTQSW GLICGESWTT KEAMVACRQL GLGYANQGLQ
ETWYWDSSNV TEMVMSGVKC TGSEMSLSQC QHHKTVSCQK AAAKFAAGVI CSETASDLVL
NASLVQQTVY IEDRPLHMLY CAAEEDCLSK SAAKANWPYG HRRLLRFSSQ IHNIGRADFK
PKAGRHSWVW HACHGHYHSM DIFTHYDLLN ANGTKVAEGH KASFCLEDTD CQEGVSKRYE
CANFGDQGIT VGCWDLYRHD IDCQWIDITD VKPGNYILQI VINPNYEVAE SDFTNNAMKC
NCKYDGHRIW LHNCHIGDAF SEEAERRFEK YPGQLNNRIS
//
