LOCUS       NP_001400932             411 aa            linear   ROD 01-MAY-2025
DEFINITION  protein-lysine 6-oxidase precursor [Rattus norvegicus].
ACCESSION   NP_001400932 XP_006254775
VERSION     NP_001400932.1
DBSOURCE    REFSEQ: accession NM_001414003.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Jiang,T., Xiao,H., Li,B., He,H., Wang,H. and Chen,L.
  TITLE     LOX overexpression programming mediates the osteoclast mechanism of
            low peak bone mass in female offspring rats caused by pregnant
            dexamethasone exposure
  JOURNAL   Cell Commun Signal 21 (1), 84 (2023)
   PUBMED   37095518
  REMARK    GeneRIF: LOX overexpression programming mediates the osteoclast
            mechanism of low peak bone mass in female offspring rats caused by
            pregnant dexamethasone exposure.
            Erratum:[Cell Commun Signal. 2024 Mar 26;22(1):192. doi:
            10.1186/s12964-024-01579-w. PMID: 38532448]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 411)
  AUTHORS   McEnaney,R.M., McCreary,D.D., Skirtich,N.O., Andraska,E.A.,
            Sachdev,U. and Tzeng,E.
  TITLE     Elastic Laminar Reorganization Occurs with Outward Diameter
            Expansion during Collateral Artery Growth and Requires Lysyl
            Oxidase for Stabilization
  JOURNAL   Cells 11 (1), 7 (2021)
   PUBMED   35011567
  REMARK    GeneRIF: Elastic Laminar Reorganization Occurs with Outward
            Diameter Expansion during Collateral Artery Growth and Requires
            Lysyl Oxidase for Stabilization.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Zhao,R., Liu,W., Wang,M., Zhang,Y., Pan,L., Feng,F., Xia,T. and
            Yang,L.
  TITLE     Lysyl oxidase inhibits TNF-alpha induced rat nucleus pulposus cell
            apoptosis via regulating Fas/FasL pathway and the p53 pathways
  JOURNAL   Life Sci 260, 118483 (2020)
   PUBMED   32979358
  REMARK    GeneRIF: Lysyl oxidase inhibits TNF-alpha induced rat nucleus
            pulposus cell apoptosis via regulating Fas/FasL pathway and the p53
            pathways.
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Rosell-Garcia,T., Paradela,A., Bravo,G., Dupont,L., Bekhouche,M.,
            Colige,A. and Rodriguez-Pascual,F.
  TITLE     Differential cleavage of lysyl oxidase by the metalloproteinases
            BMP1 and ADAMTS2/14 regulates collagen binding through a tyrosine
            sulfate domain
  JOURNAL   J Biol Chem 294 (29), 11087-11100 (2019)
   PUBMED   31152061
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Wan,Z.H., Li,G.H., Guo,Y.L., Li,W.Z., Chen,L. and Zhang,Y.J.
  TITLE     Amelioration of Cavernosal Fibrosis and Erectile Function by Lysyl
            Oxidase Inhibition in a Rat Model of Cavernous Nerve Injury
  JOURNAL   J Sex Med 15 (3), 304-313 (2018)
   PUBMED   29502979
  REMARK    GeneRIF: LOX over-activation contributes to penile fibrosis and LOX
            inhibition could be a promising strategy in preventing the
            progression of cavernous nerve injury-induced erectile dysfunction.
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Trackman,P.C., Pratt,A.M., Wolanski,A., Tang,S.S., Offner,G.D.,
            Troxler,R.F. and Kagan,H.M.
  TITLE     Cloning of rat aorta lysyl oxidase cDNA: complete codons and
            predicted amino acid sequence
  JOURNAL   Biochemistry 30 (33), 8282 (1991)
   PUBMED   1678281
  REMARK    Correction to:[Biochemistry. 1990 May 22;29(20):4863-70. doi:
            10.1021/bi00472a016. PMID: 1973052]
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Trackman,P.C., Pratt,A.M., Wolanski,A., Tang,S.S., Offner,G.D.,
            Troxler,R.F. and Kagan,H.M.
  TITLE     Cloning of rat aorta lysyl oxidase cDNA: complete codons and
            predicted amino acid sequence
  JOURNAL   Biochemistry 29 (20), 4863-4870 (1990)
   PUBMED   1973052
  REMARK    Erratum:[Biochemistry. 1991 Aug 20;30(33):8282. doi:
            10.1021/bi00247a025. PMID: 1678281]
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Ooshima,A. and Midorikawa,O.
  TITLE     Increased lysyl oxidase activity in blood vessels of hypertensive
            rats and effect of beta-aminopropionitrile on arteriosclerosis
  JOURNAL   Jpn Circ J 41 (12), 1337-1340 (1977)
   PUBMED   24127
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Starcher,B.C., Madaras,J.A. and Tepper,A.S.
  TITLE     Lysyl oxidase deficiency in lung and fibroblasts from mice with
            hereditary emphysema
  JOURNAL   Biochem Biophys Res Commun 78 (2), 706-712 (1977)
   PUBMED   20889
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Rowe,D.W., McGoodwin,E.B., Martin,G.R. and Grahn,D.
  TITLE     Decreased lysyl oxidase activity in the aneurysm-prone, mottled
            mouse
  JOURNAL   J Biol Chem 252 (3), 939-942 (1977)
   PUBMED   14140
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Nov 14, 2022 this sequence version replaced XP_006254775.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U11038.1, SRR26360190.2555359.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760400,
                                           SAMN12840115 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..411
                     /product="protein-lysine 6-oxidase precursor"
                     /EC_number="1.4.3.13"
                     /note="protein-lysine 6-oxidase; Lysyl oxidase (an H-rev
                     gene with its expression down-regulated in
                     HRAS-transformed rat 208F fibroblasts)"
                     /calculated_mol_wt=44034
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2543
     Region          <56..>154
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          60..168
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16636.2)"
     Site            91
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16636.2)"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16636.2)"
     mat_peptide     163..411
                     /product="Protein-lysine 6-oxidase, long form.
                     /evidence=ECO:0000269|PubMed:8636146. /id=PRO_0000018525"
                     /note="propagated from UniProtKB/Swiss-Prot (P16636.2)"
                     /calculated_mol_wt=29025
     Site            181
                     /site_type="sulfatation"
                     /note="Sulfotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P28300; propagated from
                     UniProtKB/Swiss-Prot (P16636.2)"
     Region          207..411
                     /region_name="Lysyl-oxidase like"
                     /note="propagated from UniProtKB/Swiss-Prot (P16636.2)"
     Region          207..406
                     /region_name="Lysyl_oxidase"
                     /note="Lysyl oxidase; pfam01186"
                     /db_xref="CDD:460102"
     Site            212..213
                     /site_type="cleavage"
                     /note="Cleavage, by ADAMTS2 and ADAMTS14.
                     /evidence=ECO:0000250|UniProtKB:P28300; propagated from
                     UniProtKB/Swiss-Prot (P16636.2)"
     mat_peptide     213..411
                     /product="Protein-lysine 6-oxidase, short form.
                     /evidence=ECO:0000250|UniProtKB:P28300.
                     /id=PRO_0000447888"
                     /note="propagated from UniProtKB/Swiss-Prot (P16636.2)"
                     /calculated_mol_wt=23034
     CDS             1..411
                     /gene="Lox"
                     /gene_synonym="H-rev142; Rrg1"
                     /coded_by="NM_001414003.1:273..1508"
                     /db_xref="GeneID:24914"
                     /db_xref="RGD:3015"
ORIGIN      
        1 mrfawtvlfl gqlqfcpllr capqaprepp aapgawrqti qwenngqvfs llslgaqyqp
       61 qrrrdssata pradgnaaaq prtpilllrd nrtasarart pspsgvaagr prpaarhwfq
      121 vgfspsgagd gasrraanrt aspqppqlsn lrppshvdrm vgddpynpyk ysddnpyyny
      181 ydtyerprsg srhrpgygtg yfqyglpdlv pdpyyiqast yvqkmsmynl rcaaeencla
      241 ssayradvrd ydhrvllrfp qrvknqgtsd flpsrprysw ewhschqhyh smdefshydl
      301 ldastqrrva eghkasfcle dtscdygyhr rfactahtqg lspgcydtya adidcqwidi
      361 tdvqpgnyil kvsvnpsylv pesdysnnvv rceirytghh ayasgctisp y
//
