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   02-SEP-2026, entry version 169.
DE   RecName: Full=Lysyl oxidase homolog 1;
DE            EC=1.4.3.13 {ECO:0000269|PubMed:14745449};
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).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP   AND INTERACTION WITH FBNL5.
RX   PubMed=14745449; DOI=10.1038/ng1297;
RA   Liu X., Zhao Y., Gao J., Pawlyk B., Starcher B., Spencer J.A.,
RA   Yanagisawa H., Zuo J., Li T.;
RT   "Elastic fiber homeostasis requires lysyl oxidase-like 1 protein.";
RL   Nat. Genet. 36:178-182(2004).
CC   -!- FUNCTION: Catalyzes the oxidative deamination of lysine and
CC       hydroxylysine residues in collagen and elastin, resulting in the
CC       formation of covalent cross-linkages, and the stabilization of collagen
CC       and elastin fibers (PubMed:14745449). Essential for the elastic fiber
CC       homeostasis and for their maintenance at adult age (PubMed:14745449).
CC       {ECO:0000269|PubMed:14745449}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + O2 + H2O = (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:0000269|PubMed:14745449};
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 (By similarity).
CC       Interacts with FBLN5 (PubMed:14745449). {ECO:0000250|UniProtKB:Q08397,
CC       ECO:0000269|PubMed:14745449}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:14745449}. Secreted, extracellular space,
CC       extracellular matrix {ECO:0000269|PubMed:14745449}.
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   -!- PTM: Proteolytic processing by a furin-like protease causes removal of
CC       N-terminal propeptide resulting in an enzyme largely inactive, but
CC       further proteolytic processing by BMP1 results in enzyme activation.
CC       {ECO:0000250|UniProtKB:Q95L39}.
CC   -!- DISRUPTION PHENOTYPE: Mice do not deposit normal elastic fibers in the
CC       uterine tract post partum and develop pelvic organ prolapse, enlarged
CC       airspaces of the lung, loose skin and vascular abnormalities with
CC       concomitant tropoelastin accumulation. {ECO:0000269|PubMed:14745449}.
CC   -!- SIMILARITY: Belongs to the lysyl oxidase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 5.
DR   FunCoup; P97873; 209.
DR   IntAct; P97873; 4.
DR   MINT; P97873; -.
DR   STRING; 10090.ENSMUSP00000057406; -.
DR   GlyGen; P97873; 1 site.
DR   iPTMnet; P97873; -.
DR   PhosphoSitePlus; P97873; -.
DR   PaxDb; 10090-ENSMUSP00000057406; -.
DR   PeptideAtlas; P97873; -.
DR   ProteomicsDB; 286230; -.
DR   Pumba; P97873; -.
DR   DNASU; 16949; -.
DR   GeneID; 16949; -.
DR   KEGG; mmu:16949; -.
DR   UCSC; uc009pwv.2; mouse.
DR   AGR; MGI:106096; -.
DR   CTD; 4016; -.
DR   MGI; MGI:106096; Loxl1.
DR   eggNOG; ENOG502QWET; Eukaryota.
DR   InParanoid; P97873; -.
DR   OrthoDB; 547291at2759; -.
DR   PhylomeDB; P97873; -.
DR   Reactome; R-MMU-1566948; Elastic fibre formation.
DR   Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
DR   BioGRID-ORCS; 16949; 1 hit in 78 CRISPR screens.
DR   PRO; PR:P97873; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P97873; protein.
DR   GO; GO:0001669; C:acrosomal vesicle; ISO:GO_Central.
DR   GO; GO:0005604; C:basement membrane; ISO:GO_Central.
DR   GO; GO:0071953; C:elastic fiber; TAS:GO_Central.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR   InterPro; IPR001695; Lysyl_oxidase.
DR   InterPro; IPR019828; Lysyl_oxidase_CS.
DR   PANTHER; PTHR45817:SF8; LYSYL OXIDASE HOMOLOG 1; 1.
DR   PANTHER; PTHR45817; LYSYL OXIDASE-LIKE-RELATED; 1.
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;
KW   Extracellular matrix; LTQ; Metal-binding; Oxidoreductase;
KW   Reference proteome; Secreted; Signal; TPQ.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..95
FT                   /evidence="ECO:0000250|UniProtKB:Q95L39"
FT                   /id="PRO_0000018530"
FT   CHAIN           96..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          334..402
FT                   /note="Interaction with FBLN5"
FT                   /evidence="ECO:0000269|PubMed:14745449"
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        82..91
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..279
FT                   /note="Pro 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   SITE            95..96
FT                   /note="Cleavage; by furin-like protease"
FT                   /evidence="ECO:0000250|UniProtKB:Q95L39"
FT   SITE            134..135
FT                   /note="Cleavage; by BMP1"
FT                   /evidence="ECO:0000250|UniProtKB:Q95L39"
FT   SITE            151..152
FT                   /note="Cleavage; by BMP1"
FT                   /evidence="ECO:0000250|UniProtKB:Q08397"
FT   SITE            217..218
FT                   /note="Cleavage; by ADAMTS14"
FT                   /evidence="ECO:0000250|UniProtKB:Q08397"
FT   SITE            370..371
FT                   /note="Cleavage; by BMP1"
FT                   /evidence="ECO:0000250|UniProtKB:Q95L39"
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
//