ID A0A1L8GRT8_XENLA Unreviewed; 767 AA.
AC A0A1L8GRT8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
GN Name=loxl2.S {ECO:0000313|RefSeq:XP_018110586.1,
GN ECO:0000313|Xenbase:XB-GENE-17337011};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018110586.1};
RN [1] {ECO:0000313|RefSeq:XP_018110586.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018110586.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018110586.1};
RG RefSeq;
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_018110586.1; XM_018255097.2.
DR AlphaFoldDB; A0A1L8GRT8; -.
DR STRING; 8355.A0A1L8GRT8; -.
DR PaxDb; 8355-A0A1L8GRT8; -.
DR GeneID; 108712720; -.
DR KEGG; xla:108712720; -.
DR AGR; Xenbase:XB-GENE-17337011; -.
DR CTD; 108712720; -.
DR Xenbase; XB-GENE-17337011; loxl2.S.
DR OMA; HIHMSEI; -.
DR OrthoDB; 3035117at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 108712720; Expressed in internal ear and 6 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:UP000186698};
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};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|RuleBase:RU367046};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DISULFID 77..141
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 90..151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 121..131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 258..268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 388..398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 504..514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 767 AA; 85800 MW; 7DCEEA27AED51499 CRC64;
MLVTHVFLLT LSLSVPSLGQ YEHWPYYPEY QEPQAPEPPP TEPKTGPQIH VRLAGEKRKH
NEGRVEVYYE GEWGTVCDDD FSMYAAHIVC RELGYQDAVS WSPSSKYGKG EGRIWLDNVN
CNGRERSIAS CSSNGWGVTD CKHSEDVGVQ CSDRRIPGFK VSNELPGQLE GLNIQVEDVR
IRAILSALRK RVPVMEGFVE VKVQGNWRQV CDTEWSSKNS RVVCGMFGFP AEKKYNTKVY
KIFSSRRTHT YWQFSANCTG NEPHLSSCKV GGVLLSDPKT NQTCSDGAPV VVSCTPGQAF
APSPGTGFRK AFRQEQPLIR LRGGANIGEG RVEVLKNGEW GTVCDDKWNL VTASVVCREL
GFGSAKEALV GAQLGQGMGQ IHMSEIQCNG FEKTLIDCKF NVHSQGCNHE EDAAVRCNVP
AMGFENQIRL SGGRHPTEGR VEVLMERNGT LHWGTVCSET WGTMEAMIVC RQLGLGFASH
AFQETWYWQG DVNADDVVMS GVKCSGTEMS LSHCRHDGVN INCPRGGGRF AAGVSCVETA
PDLVLNAALV EQTTYLEDRP MFMLQCAHEE QCLASSADHT SPTTGFRRLL RFSSQIHNNG
QADFRPKTGR HAWIWHDCHR HYHSMEVFTH YDLLSLNGTK IAEGHKASFC LEDSECEADI
QKQYACANFG EQGITVGCWD LYRHDIDCQW VDITDVAPGD YFFQVVVNPN QEVAESDYTN
NIMKCRCRYD GHRIWMYNCH IGGSYSTETE EKFEHFSGLL NNQLSTR
//
