LOXL1_MOUSE
ID LOXL1_MOUSE Reviewed; 607 AA.
AC P97873; Q91ZY4; Q99KX3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Lysyl oxidase homolog 1;
DE EC=1.4.3.-;
DE AltName: Full=Lysyl oxidase 2;
DE AltName: Full=Lysyl oxidase-like protein 1;
DE Flags: Precursor;
GN Name=Loxl1; Synonyms=Lox2, Loxl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seve S., Borel A., Gleyzal C., Farjanel J., Eichenberger D., Font B.,
RA Sommer P.;
RT "Identification of the recombinant and natural forms of mature lysyl
RT oxidase-like 1.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 498-607.
RX PubMed=9250877; DOI=10.1007/s003359900520;
RA Tchernev V.T., Yang T.P., Kingsmore S.F.;
RT "Genetic mapping of lysyl oxidase-2 (Loxl) on mouse chromosome 9.";
RL Mamm. Genome 8:621-622(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 526-540.
RC STRAIN=C57BL/6J;
RX PubMed=9119402; DOI=10.1006/geno.1996.4574;
RA Wydner K.S., Kim Y., Csiszar K., Boyd C.D., Passmore H.C.;
RT "An intron capture strategy used to identify and map a lysyl oxidase-like
RT gene on chromosome 9 in the mouse.";
RL Genomics 40:342-345(1997).
CC -!- FUNCTION: Active on elastin and collagen substrates. {ECO:0000250}.
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; AF357006; AAK97375.1; -; mRNA.
DR EMBL; BC003973; AAH03973.1; -; mRNA.
DR EMBL; BC037999; AAH37999.1; -; mRNA.
DR EMBL; AH006767; AAC53067.1; -; Genomic_DNA.
DR EMBL; U79144; AAB86802.1; -; mRNA.
DR CCDS; CCDS52813.1; -.
DR RefSeq; NP_034859.2; NM_010729.3.
DR AlphaFoldDB; P97873; -.
DR SMR; P97873; -.
DR BioGRID; 201192; 4.
DR IntAct; P97873; 4.
DR MINT; P97873; -.
DR STRING; 10090.ENSMUSP00000057406; -.
DR iPTMnet; P97873; -.
DR PhosphoSitePlus; P97873; -.
DR MaxQB; P97873; -.
DR PaxDb; P97873; -.
DR PeptideAtlas; P97873; -.
DR PRIDE; P97873; -.
DR ProteomicsDB; 286230; -.
DR DNASU; 16949; -.
DR GeneID; 16949; -.
DR KEGG; mmu:16949; -.
DR UCSC; uc009pwv.2; mouse.
DR CTD; 4016; -.
DR MGI; MGI:106096; Loxl1.
DR eggNOG; ENOG502QWET; Eukaryota.
DR InParanoid; P97873; -.
DR OrthoDB; 815466at2759; -.
DR PhylomeDB; P97873; -.
DR TreeFam; TF326061; -.
DR Reactome; R-MMU-1566948; Elastic fibre formation.
DR Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
DR BioGRID-ORCS; 16949; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Loxl1; mouse.
DR PRO; PR:P97873; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97873; protein.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016641; F:oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor; IDA:MGI.
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 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Copper; Disulfide bond; LTQ;
KW Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal; TPQ.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..94
FT /evidence="ECO:0000250"
FT /id="PRO_0000018530"
FT CHAIN 95..607
FT /note="Lysyl oxidase homolog 1"
FT /id="PRO_0000018531"
FT REGION 63..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..607
FT /note="Lysyl-oxidase like"
FT COMPBIAS 76..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..279
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 482
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 484
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 486
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT MOD_RES 545
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 428..434
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 481..530
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 514..520
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 541..551
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 588..602
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CROSSLNK 510..545
FT /note="Lysine tyrosylquinone (Lys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CONFLICT 173
FT /note="P -> S (in Ref. 2; AAH37999)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..210
FT /note="GAG -> HAS (in Ref. 2; AAH03973)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="T -> I (in Ref. 2; AAH03973)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="S -> A (in Ref. 3; AAB86802)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 66506 MW; 7BA8144F09E96C94 CRC64;
MALAGAGSQL RTLVWSACLC VLVHGQQAQP GQGSDPGRWR QLIQWENNGQ VYSLLNSGSE
YVPAGPQRGE TSSRVLLAGA PQTSQRRSQG GPRRRQAPSL PLPGRVGSDT VRGQTRHPFG
FGQVPDNWRE VAVGDSTGMA RARTSVSQQR HGGSASSSVS ASAFATTYRQ PSPYPQQFPY
PQAPFVNQYE NYDPASRTYE QGYVYYRGAG GGMGAGAAAV ASAGVIYPFQ PRARYEDYGG
GGGEEQPEYP AQGFYPAPER PYVPQPQPQP QPQPQPQPQP SDGLDRRYSH SLYNEGTPGF
EQAYPDPSTD VSQAPAGAGG TYGGAGDPRL GWYPPYAANV PPEAYVPPRA VEPQPPFRVL
EPPYLPVRSS DAPSQGGERN GAQQGRLSVG SVYRPNQNGR GLPDLVPDPN YVQASTYVQR
AHLYSLRCAA EEKCLASTAY APEATDYDLR VLLRFPQRVK NQGTADFLPN RPRHTWEWHS
CHQHYHSMDE FSHYDLLDAS TGKKVAEGHK ASFCLEDSTC DFGNLKRYAC TSHTQGLSPG
CYDTYNADID CQWIDITDVQ PGNYILKVHV NPKYIVLESD FTNNVVRCNI HYTGRYVSTT
NCKIVQS
