LOXL1_BOVIN
ID LOXL1_BOVIN Reviewed; 591 AA.
AC Q95L39;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Lysyl oxidase homolog 1;
DE EC=1.4.3.-;
DE AltName: Full=Lysyl oxidase-like protein 1;
DE Flags: Precursor;
GN Name=LOXL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEOLYTIC PROCESSING, AND FUNCTION.
RC TISSUE=Skin;
RX PubMed=11684696; DOI=10.1074/jbc.m109499200;
RA Borel A., Eichenberger D., Farjanel J., Kessler E., Gleyzal C.,
RA Hulmes D.J.S., Sommer P., Font B.;
RT "Lysyl oxidase-like protein from bovine aorta. Isolation and maturation to
RT an active form by bone morphogenetic protein-1.";
RL J. Biol. Chem. 276:48944-48949(2001).
CC -!- FUNCTION: Active on elastin and collagen substrates.
CC {ECO:0000269|PubMed:11684696}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P16636};
CC -!- COFACTOR:
CC Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489;
CC Evidence={ECO:0000250|UniProtKB:P33072};
CC Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072};
CC -!- SUBUNIT: Interacts (via propeptide) with EFEMP2.
CC {ECO:0000250|UniProtKB:Q08397}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}.
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:0000250|UniProtKB:P33072}.
CC -!- SIMILARITY: Belongs to the lysyl oxidase family. {ECO:0000305}.
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DR EMBL; AF421185; AAL13312.1; -; mRNA.
DR RefSeq; NP_776808.1; NM_174383.2.
DR AlphaFoldDB; Q95L39; -.
DR SMR; Q95L39; -.
DR STRING; 9913.ENSBTAP00000011978; -.
DR PaxDb; Q95L39; -.
DR GeneID; 281903; -.
DR KEGG; bta:281903; -.
DR CTD; 4016; -.
DR eggNOG; ENOG502QWET; Eukaryota.
DR InParanoid; Q95L39; -.
DR OrthoDB; 815466at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IBA:GO_Central.
DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR GO; GO:0018057; P:peptidyl-lysine oxidation; IBA:GO_Central.
DR InterPro; IPR001695; Lysyl_oxidase.
DR InterPro; IPR019828; Lysyl_oxidase_CS.
DR Pfam; PF01186; Lysyl_oxidase; 1.
DR PRINTS; PR00074; LYSYLOXIDASE.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Copper; Disulfide bond; LTQ;
KW Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal; TPQ.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..91
FT /id="PRO_0000045438"
FT CHAIN 92..591
FT /note="Lysyl oxidase homolog 1"
FT /id="PRO_0000045439"
FT REGION 77..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..591
FT /note="Lysyl-oxidase like"
FT COMPBIAS 324..354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 466
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 468
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 470
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT MOD_RES 529
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 412..418
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 465..514
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 498..504
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 525..535
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 572..586
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CROSSLNK 494..529
FT /note="Lysine tyrosylquinone (Lys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P33072"
SQ SEQUENCE 591 AA; 64496 MW; 337A344E64F0FC73 CRC64;
MALALTGWQL VWGACVCVLV HGQQAPPGQG SDPGRWRQLI QWENNGQVYS LLNSGAEYVP
PGPQGSEANS RVLLAGAPQA PPRRRGGLRR RQAPSLPLPG RVGSDTVRGQ ARHPFGFGQV
PDNWREVAVG DSTGMARART SVSQQRHGGS ASSVSASASA FASTYRQPSS FPQQQFPYPQ
APFVSQYETY DPSTRTYDQG YVYYRSASGG LGAAAVASAG VVYPFQPRAR YEEYGGGGGE
EQPEYPPQGF YPAAPERPYA PQPADGLDRR YSHSLYHEGT AGLEPAYPDP GPDAAQPNGG
GGGGTYGGGG GDPRLGWYPP YGNMPPEAYS PPRVVEPQPP FRVLEPPYLP VRSSDAPPPG
SERNGAQQGR LSVGSVYRPN QNGRGLPDLV PDPNYVQAST YVQRAHLYSL RCAAEEKCLA
STAYAPEATD YDVRVLLRFP QRVKNQGTAD FLPNRPRHTW EWHSCHQHYH SMDEFSHYDL
LDAATGKKVA EGHKASFCLE DSTCDFGNLK RYACTSHTQG LSPGCYDTYN ADIDCQWIDI
TDVQPGNYIL KVHVNPKYIV LESDFTNNVV RCNIHYTGRY VSTTNCKIVQ S
