LOXL4_MOUSE
ID LOXL4_MOUSE Reviewed; 757 AA.
AC Q924C6; E9PXI3;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Lysyl oxidase homolog 4;
DE EC=1.4.3.-;
DE AltName: Full=Lysyl oxidase-like protein 4;
DE AltName: Full=Lysyl oxidase-related protein C;
DE Flags: Precursor;
GN Name=Loxl4; Synonyms=Loxc;
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].
RX PubMed=11292829; DOI=10.1074/jbc.m100861200;
RA Ito H., Akiyama H., Iguchi H., Iyama K., Miyamoto M., Ohsawa K.,
RA Nakamura T.;
RT "Molecular cloning and biological activity of a novel lysyl oxidase-related
RT gene expressed in cartilage.";
RL J. Biol. Chem. 276:24023-24029(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: May modulate the formation of a collagenous extracellular
CC matrix.
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 -!- 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; AF338440; AAK71933.1; -; mRNA.
DR EMBL; AC124552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS29830.1; -.
DR RefSeq; NP_444313.3; NM_053083.3.
DR AlphaFoldDB; Q924C6; -.
DR SMR; Q924C6; -.
DR BioGRID; 212283; 6.
DR IntAct; Q924C6; 1.
DR MINT; Q924C6; -.
DR STRING; 10090.ENSMUSP00000125803; -.
DR GlyGen; Q924C6; 2 sites.
DR iPTMnet; Q924C6; -.
DR PhosphoSitePlus; Q924C6; -.
DR MaxQB; Q924C6; -.
DR PaxDb; Q924C6; -.
DR PRIDE; Q924C6; -.
DR ProteomicsDB; 292353; -.
DR Antibodypedia; 31028; 225 antibodies from 23 providers.
DR DNASU; 67573; -.
DR Ensembl; ENSMUST00000026190; ENSMUSP00000026190; ENSMUSG00000025185.
DR Ensembl; ENSMUST00000171432; ENSMUSP00000126686; ENSMUSG00000025185.
DR GeneID; 67573; -.
DR KEGG; mmu:67573; -.
DR UCSC; uc008hns.2; mouse.
DR CTD; 84171; -.
DR MGI; MGI:1914823; Loxl4.
DR VEuPathDB; HostDB:ENSMUSG00000025185; -.
DR eggNOG; ENOG502QSX8; Eukaryota.
DR GeneTree; ENSGT00940000157042; -.
DR HOGENOM; CLU_002555_3_0_1; -.
DR InParanoid; Q924C6; -.
DR Reactome; R-MMU-1566948; Elastic fibre formation.
DR Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
DR BioGRID-ORCS; 67573; 0 hits in 70 CRISPR screens.
DR PRO; PR:Q924C6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q924C6; protein.
DR Bgee; ENSMUSG00000025185; Expressed in intramembranous bone and 94 other tissues.
DR ExpressionAtlas; Q924C6; baseline and differential.
DR Genevisible; Q924C6; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IDA:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR GO; GO:0018057; P:peptidyl-lysine oxidation; IBA:GO_Central.
DR Gene3D; 3.10.250.10; -; 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 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; SSF56487; 4.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 4.
PE 2: Evidence at transcript level;
KW Copper; Disulfide bond; Glycoprotein; LTQ; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Secreted; Signal; TPQ.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..757
FT /note="Lysyl oxidase homolog 4"
FT /id="PRO_0000018536"
FT DOMAIN 33..134
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 160..288
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 312..412
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 422..530
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 534..737
FT /note="Lysyl-oxidase like"
FT BINDING 612
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 614
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 616
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT MOD_RES 675
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 72..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 103..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 192..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 205..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 252..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 337..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 350..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 381..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 451..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 464..529
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 498..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 559..565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 611..659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 643..649
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 671..681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 718..732
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT CROSSLNK 639..675
FT /note="Lysine tyrosylquinone (Lys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CONFLICT 39
FT /note="T -> A (in Ref. 1; AAK71933)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="V -> I (in Ref. 1; AAK71933)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="L -> F (in Ref. 1; AAK71933)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="V -> G (in Ref. 1; AAK71933)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="Y -> N (in Ref. 1; AAK71933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 84779 MW; 45E698867160955C CRC64;
MMWPQPPTFS LFLLLLLSQA PSSRPQSSGT KKLRLVGPTD RPEEGRLEVL HQGQWGTVCD
DDFALQEATV ACRQLGFESA LTWAHSAKYG QGEGPIWLDN VRCLGTEKTL DQCGSNGWGV
SDCRHSEDVG VVCHPRRQHG YHSEKVSNAL GPQGRRLEEV RLKPILASAK RHSPVTEGAV
EVRYDGHWRQ VCDQGWTMNN SRVVCGMLGF PSQTSVNSHY YRKVWNLKMK DPKSRLNSLT
KKNSFWIHRV DCLGTEPHLA KCQVQVAPGR GKLRPACPGG MHAVVSCVAG PHFRRQKPKP
TRKESHAEEL KVRLRSGAQV GEGRVEVLMN RQWGTVCDHR WNLISASVVC RQLGFGSARE
ALFGAQLGQG LGPIHLSEVR CRGYERTLGD CLALEGSQNG CQHANDAAVR CNIPDMGFQN
KVRLAGGRNS EEGVVEVQVE VNGVPRWGTV CSDHWGLTEA MVTCRQLGLG FANFALKDTW
YWQGTPEAKE VVMSGVRCSG TEMALQQCQR HGPVHCSHGP GRFSAGVACM NSAPDLVMNA
QLVQETAYLE DRPLSMLYCA HEENCLSKSA DHMDWPYGYR RLLRFSSQIY NLGRADFRPK
AGRHSWIWHQ CHRHYHSIEV FTHYDLLTLN GSKVAEGHKA SFCLEDTNCP SGVQRRYACA
NFGEQGVAVG CWDTYRHDID CQWVDITDVG PGDYIFQVVV NPTNDVAESD FSNNMIRCRC
KYDGQRVWLH NCHTGDSYRA NAELSLEQEQ RLRNNLI
