ID A0A2I3SW76_PANTR Unreviewed; 693 AA.
AC A0A2I3SW76;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:ENSPTRP00000081231.1,
GN ECO:0000313|VGNC:VGNC:57877};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000081231.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000081231.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000081231.1}
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|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 EMBL; AACZ04065674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04065675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04065676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3SW76; -.
DR Ensembl; ENSPTRT00000086106.1; ENSPTRP00000081231.1; ENSPTRG00000047037.1.
DR VGNC; VGNC:57877; LOXL2.
DR GeneTree; ENSGT00940000155874; -.
DR OMA; YCTGKEA; -.
DR Proteomes; UP000002277; Chromosome 8.
DR Bgee; ENSPTRG00000047037; Expressed in fibroblast and 18 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:UP000002277};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..693
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014185445"
FT DOMAIN 58..159
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 188..236
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 290..389
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 399..508
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
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 359..369
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 475..485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 693 AA; 77095 MW; F70BFB1493FF73B5 CRC64;
MERPLCSHLC SCLAVLALLS PLSLAQYDSW PHYPEYFQQP APEYHQPQAP ANVAKIQLRL
AGQKRKHSEG RVEVYYDGQW GTVCDDDFSI HAAHVVCREL GYVEAKSWTA SSSYGKGEGP
IWLDNLHCTG NEATLAACTS NGWGVTDCKH TEDVGVVCSD KRIPGFKFDN SLINQIENLN
IQVEDIRIRA ILSTYRKRTP VTEGYVEVKE GKTWKQICDK HWTAKNSRVV CGMFGFPGER
TYNTKVYKSR CPLNTLENSH PTPSLVIPSQ LFLPVGAKKS KPPPWQQPLV RLRGGAYIGE
GRVEVLKNGE WGTVCDDKWD LVSASVVCRE LGFGSAKEAV TGSRLGQGIG PIHLNEIQCT
GNEKSIIDCK FNAESQGCNH EEDAGVRCNT PAMGLQKKLR LNGGRNPYEG RVEVLVERNG
SLVWGMVCGQ NWGIVEAMVV CRQLGLGFAS NAFQETWYWH GDVNSNKVVM SGVKCSGTEL
SLAHCRHDGE DVACPQGGVQ YGAGVACSET APDLVLNAEM VQQTTYLEDR PMFMLQCAME
ENCLSASAAQ TDPTTGYRRL LRFSSQIHNN GQSDFRPKNG RHAWIWHDCH RHYHSMEVFT
HYDLLNLNGT KVAEGHKASF CLEDTECEGD IQKNYECANF GDQGITMGCW DMYRHDIDCQ
WVDITDVPPG DYLFQVVPSA KRRKKSLSTS AGS
//
