ID F6YGE3_CALJA Unreviewed; 774 AA.
AC F6YGE3; U3E1S0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
GN Name=LOXL2 {ECO:0000313|Ensembl:ENSCJAP00000037386.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000037386.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000037386.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000037386.4}
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|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 AlphaFoldDB; F6YGE3; -.
DR Ensembl; ENSCJAT00000039495.5; ENSCJAP00000037386.4; ENSCJAG00000020099.5.
DR eggNOG; ENOG502QSX8; Eukaryota.
DR GeneTree; ENSGT00940000155874; -.
DR HOGENOM; CLU_002555_3_0_1; -.
DR OrthoDB; 3035117at2759; -.
DR TreeFam; TF326061; -.
DR Proteomes; UP000008225; Chromosome 13.
DR Bgee; ENSCJAG00000020099; Expressed in heart and 6 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
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:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070492; F:oligosaccharide binding; IEA:Ensembl.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0070828; P:heterochromatin organization; IEA:Ensembl.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0036211; P:protein modification process; IEA:Ensembl.
DR GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0002040; P:sprouting angiogenesis; IEA:Ensembl.
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:UP000008225};
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 84..148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 97..158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 128..138
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 265..275
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 395..405
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 511..521
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 774 AA; 86618 MW; F3C0BDE12192BE9D CRC64;
MERPLCSPLC SCLAMLALLS TLSLAQYDSW PYYPEYFQQP APEYHQPQVP ANVAKIQLRL
AGQKRKHSEG RVEVYYDGQW GTVCDDDFSI HAAHVVCREL GYVEAKSWTA SSSYGKGEGP
IWLDNLHCTG KEATLAACSS NGWGVTDCKH TEDVGVVCSD KRIPGFKFDN SLINQIENLN
IQVEDIRIRA ILSAYRKRTP VMEGYVEVKE GKTWKQICDK HWTAKNSRVV CGMFGFPGER
TYNTKVYKMF ASRRKQRYWP FSMDCTGTEA HISSCKLGPQ VSLDPMKNVT CENGLPAVVS
CVPGPVFSPD GPSRFRKAYK PEQPLVRLRG GASIGEGRVE VLKNGEWGTV CDDKWDLVSA
SVVCRELGFG SAKEAVTGSR LGQGIGPIHL NEIQCTGNEK SIIDCKFNAE SQGCNHEEDA
GVRCNIPAMG LQKKLRLNGG RNPYEGRVEV LVERNGSLVW GTVCGQNWGI VEAMVVCRQL
GLGFASNAFQ ETWYWHGDVY ANKVVMSGVK CSGTELSLAH CRHDGEDVAC PQGGVQYGAG
VACSETAPDL VLNAEIVQQT TYLEDRPMFM LQCAMEENCL SASAAQTNPT TGYRRLLRFS
SQIHNNGQSD FRPKNGRHAW IWHDCHRHYH SMEVFTHYDL LNLNGTKVAE GHKASFCLED
TECEGDIQKN YECANFGDQG ITMGCWDMYR HDIDCQWVDI TDVPPGDYLF QVVINPNYEV
AESDYSNNIM KCRSRYDGHR IWMYNCHIGG SFSEETEKKF EHFSGLLNNQ LSPQ
//
