ID A0A3B3IIZ7_ORYLA Unreviewed; 762 AA.
AC A0A3B3IIZ7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
GN Name=loxl2b {ECO:0000313|Ensembl:ENSORLP00000044065.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000044065.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000044065.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000044065.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000044065.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000044065.1};
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|ARBA:ARBA00036237,
CC 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: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Secreted, extracellular space,
CC extracellular matrix, basement membrane
CC {ECO:0000256|ARBA:ARBA00004302}.
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_004072828.1; XM_004072780.2.
DR RefSeq; XP_011477881.1; XM_011479579.1.
DR RefSeq; XP_011477882.1; XM_011479580.1.
DR RefSeq; XP_011477884.1; XM_011479582.1.
DR Ensembl; ENSORLT00000027600.1; ENSORLP00000044065.1; ENSORLG00000016197.2.
DR Ensembl; ENSORLT00000035106.1; ENSORLP00000044563.1; ENSORLG00000016197.2.
DR GeneID; 101164651; -.
DR KEGG; ola:101164651; -.
DR CTD; 791144; -.
DR GeneTree; ENSGT00940000155874; -.
DR OrthoDB; 3035117at2759; -.
DR Proteomes; UP000001038; Chromosome 9.
DR Bgee; ENSORLG00000016197; Expressed in muscle tissue and 8 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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:SF1; LYSYL OXIDASE HOMOLOG 2; 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 Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU367046};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW LTQ {ECO:0000256|ARBA:ARBA00022477, ECO:0000256|RuleBase:RU367046};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367046}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367046};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
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};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..762
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041074270"
FT DOMAIN 55..156
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 185..294
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 318..417
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 427..536
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DISULFID 81..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 94..155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 125..135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 262..272
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 387..397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 503..513
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 762 AA; 85606 MW; 9D0B933A42949892 CRC64;
MSVQTELCCT VILLVLSKLV PAQYELHGYP PGYPDPEQEQ YTPPVLDPDT PRIQLRLAGD
KRKHNEGRVE VYYNGEWGTV CDDDFNIHAA QVVCRELGYV EAVSWSPSSK YGKGEGTIWF
DNLQCTGTEK TLALCRSNGI GVSDCKHTED VGVVCSDRRI PGFKFVNLLP NHVENLDIRV
EDVRIRAILS SYRKRIPVTE GYVEVKDGGK WKQICDTEWT QFNSRVICGM FGFPGEKRYN
ARVYKMFARR RKPTYWDFSV NCTGTEAHLS SCRLGHANSS DTCTEGLPVV VSCVPGRAFA
PTPMTGYRKA FRQEQPLVRL RGGAIVGEGR VEVLKNGEWG TICDDKWNLL AATVVCRELG
FGTAKEALSG GRLGQGMGPV HMNEVQCSGF EKSITECLFN GEILGCSHEE DAAVRCNVPA
MGFQQRLRLS GGRNPYEGRV EVLMERNDSL VWGTVCSEGW GIMEAMVVCR QLGLGFASNA
FQETWYWPGE VSADQVVMSG VRCSGTEMSL SHCLHHGEHL SCPRGGGRKA AGVSCSETAP
DLVLNPQVVE QTTYMEDRPM FMLQCAYEEN CLSSTSGQVP ANTYRRLLRF SSQIHNNGQS
DFRPKAGRHE WVWHECHRHY HSMEVFTTYD LFTLNGSKVA EGHKASFCLE DSECDEGIEK
KYECANFGEQ GITVGCWDTY RHDIDCQWID ITDIKPGDYL FQIVINPNYE VPETDYTNNI
TKCRCRYDGH RIWMYNCHNG GSLSAELEQT FPGLLNNQVT HR
//
