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LYOX_RAT
ID   LYOX_RAT                Reviewed;         411 AA.
AC   P16636;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Protein-lysine 6-oxidase {ECO:0000305};
DE            EC=1.4.3.13 {ECO:0000305|PubMed:16432278};
DE   AltName: Full=Lysyl oxidase;
DE   Contains:
DE     RecName: Full=Protein-lysine 6-oxidase, long form {ECO:0000250|UniProtKB:P28300};
DE   Contains:
DE     RecName: Full=Protein-lysine 6-oxidase, short form {ECO:0000250|UniProtKB:P28300};
DE   Flags: Precursor;
GN   Name=Lox {ECO:0000312|RGD:3015};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Aorta;
RX   PubMed=1973052; DOI=10.1021/bi00472a016;
RA   Trackman P.C., Pratt A.M., Wolanski A., Tang S.-S., Offner G.D.,
RA   Troxler R.F., Kagan H.M.;
RT   "Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted
RT   amino acid sequence.";
RL   Biochemistry 29:4863-4870(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION.
RX   PubMed=1678281; DOI=10.1021/bi00247a025;
RA   Trackman P.C., Pratt A.M., Wolanski A., Tang S.-S., Offner G.D.,
RA   Troxler R.F., Kagan H.M.;
RT   "Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted
RT   amino acid sequence.";
RL   Biochemistry 30:8282-8282(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [4]
RP   PROTEIN SEQUENCE OF 163-167, AND PROTEOLYTIC PROCESSING OF N-TERMINUS.
RX   PubMed=8636146; DOI=10.1074/jbc.271.12.7113;
RA   Panchenko M.V., Stetler-Stevenson W.G., Trubetskoy O.V., Gacheru S.N.,
RA   Kagan H.M.;
RT   "Metalloproteinase activity secreted by fibrogenic cells in the processing
RT   of prolysyl oxidase. Potential role of procollagen C-proteinase.";
RL   J. Biol. Chem. 271:7113-7119(1996).
RN   [5]
RP   FUNCTION, AND COFACTOR.
RX   PubMed=16432278; DOI=10.1093/toxsci/kfj112;
RA   Zhao Y., Gao S., Chou I.N., Toselli P., Stone P., Li W.;
RT   "Inhibition of the expression of lysyl oxidase and its substrates in
RT   cadmium-resistant rat fetal lung fibroblasts.";
RL   Toxicol. Sci. 90:478-489(2006).
RN   [6]
RP   PROTEOLYTIC PROCESSING OF N-TERMINUS.
RX   PubMed=1349020; DOI=10.1016/s0021-9258(18)42494-5;
RA   Trackman P.C., Bedell-Hogan D., Tang J., Kagan H.M.;
RT   "Post-translational glycosylation and proteolytic processing of a lysyl
RT   oxidase precursor.";
RL   J. Biol. Chem. 267:8666-8671(1992).
RN   [7]
RP   CLEAVAGE OF SIGNAL PEPTIDE AFTER CYS-21, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA   Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT   "Peptidomics for studying limited proteolysis.";
RL   J. Proteome Res. 14:4921-4931(2015).
CC   -!- FUNCTION: Responsible for the post-translational oxidative deamination
CC       of peptidyl lysine residues in precursors to fibrous collagen and
CC       elastin (PubMed:16432278). Regulator of Ras expression. May play a role
CC       in tumor suppression. Plays a role in the aortic wall architecture (By
CC       similarity). {ECO:0000250|UniProtKB:P28301,
CC       ECO:0000269|PubMed:16432278}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-lysyl-[protein] + O2 = (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:0000305|PubMed:16432278};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000269|PubMed:16432278};
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};
CC   -!- SUBUNIT: Interacts with MFAP4. Interacts (via propeptide) with EFEMP2;
CC       this interaction is strong and facilitates formation of ternary
CC       complexes with ELN during elastic fiber assembly; this interaction
CC       limits interaction of EFEMP2 with FBLN5.
CC       {ECO:0000250|UniProtKB:P28300}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P28301}.
CC       Secreted, extracellular space.
CC   -!- TISSUE SPECIFICITY: Aorta and lung. {ECO:0000269|PubMed:1973052}.
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: Proteolytically cleaved by BMP1 which removes the propeptide (By
CC       similarity). Also proteolytically cleaved by ADAMTS2 and ADAMTS14, but
CC       not by ADAMTS3, at an additional cleavage site downstream of the BMP1
CC       cleavage site (By similarity). The propeptide plays a role in directing
CC       the deposition of this enzyme to elastic fibers, via interaction with
CC       tropoelastin (By similarity). Cleavage by BMP1 to remove the propeptide
CC       does not increase enzymatic activity but increases binding to collagen
CC       (By similarity). Cleavage by ADAMTS2 produces a form with reduced
CC       collagen-binding activity (By similarity).
CC       {ECO:0000250|UniProtKB:P28300, ECO:0000250|UniProtKB:P28301}.
CC   -!- PTM: Sulfated at Tyr-181 and also at either Tyr-177 or Tyr-178 which
CC       enhances binding to collagen. {ECO:0000250|UniProtKB:P28300}.
CC   -!- SIMILARITY: Belongs to the lysyl oxidase family. {ECO:0000305}.
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DR   EMBL; U11038; AAC52176.1; -; mRNA.
DR   EMBL; J02903; AAA41537.1; -; mRNA.
DR   EMBL; BC078861; AAH78861.1; -; mRNA.
DR   PIR; B40557; OXRTL.
DR   RefSeq; NP_058757.1; NM_017061.2.
DR   RefSeq; XP_006254775.1; XM_006254713.3.
DR   RefSeq; XP_006254776.1; XM_006254714.3.
DR   AlphaFoldDB; P16636; -.
DR   SMR; P16636; -.
DR   IntAct; P16636; 2.
DR   STRING; 10116.ENSRNOP00000065314; -.
DR   GlyGen; P16636; 2 sites.
DR   PhosphoSitePlus; P16636; -.
DR   PaxDb; P16636; -.
DR   PRIDE; P16636; -.
DR   Ensembl; ENSRNOT00000019844; ENSRNOP00000019844; ENSRNOG00000014426.
DR   GeneID; 24914; -.
DR   KEGG; rno:24914; -.
DR   UCSC; RGD:3015; rat.
DR   CTD; 4015; -.
DR   RGD; 3015; Lox.
DR   eggNOG; ENOG502QWQR; Eukaryota.
DR   GeneTree; ENSGT00940000154779; -.
DR   HOGENOM; CLU_002555_2_1_1; -.
DR   InParanoid; P16636; -.
DR   OMA; GCHMSTY; -.
DR   OrthoDB; 815466at2759; -.
DR   PhylomeDB; P16636; -.
DR   TreeFam; TF326061; -.
DR   BRENDA; 1.4.3.13; 5301.
DR   BRENDA; 3.4.24.14; 5301.
DR   Reactome; R-RNO-1566948; Elastic fibre formation.
DR   Reactome; R-RNO-2243919; Crosslinking of collagen fibrils.
DR   PRO; PR:P16636; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Bgee; ENSRNOG00000014426; Expressed in lung and 19 other tissues.
DR   Genevisible; P16636; RN.
DR   GO; GO:0005581; C:collagen trimer; ISO:RGD.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IMP:RGD.
DR   GO; GO:0004720; F:protein-lysine 6-oxidase activity; IDA:RGD.
DR   GO; GO:0035904; P:aorta development; ISO:RGD.
DR   GO; GO:0035905; P:ascending aorta development; ISO:RGD.
DR   GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR   GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB.
DR   GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR   GO; GO:0060326; P:cell chemotaxis; IMP:MGI.
DR   GO; GO:1990869; P:cellular response to chemokine; ISO:RGD.
DR   GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
DR   GO; GO:0030199; P:collagen fibril organization; IDA:RGD.
DR   GO; GO:0061448; P:connective tissue development; ISO:RGD.
DR   GO; GO:0035906; P:descending aorta development; ISO:RGD.
DR   GO; GO:0071897; P:DNA biosynthetic process; ISO:RGD.
DR   GO; GO:0048251; P:elastic fiber assembly; IMP:RGD.
DR   GO; GO:0007507; P:heart development; ISO:RGD.
DR   GO; GO:0030324; P:lung development; ISO:RGD.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; ISO:RGD.
DR   GO; GO:0055001; P:muscle cell development; ISO:RGD.
DR   GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR   GO; GO:0018057; P:peptidyl-lysine oxidation; ISS:UniProtKB.
DR   GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; IMP:MGI.
DR   GO; GO:0043491; P:protein kinase B signaling; ISO:RGD.
DR   GO; GO:0018158; P:protein oxidation; IMP:MGI.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR   GO; GO:1903010; P:regulation of bone development; ISO:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR   GO; GO:0045652; P:regulation of megakaryocyte differentiation; ISO:RGD.
DR   GO; GO:2000586; P:regulation of platelet-derived growth factor receptor-beta signaling pathway; ISO:RGD.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:1900120; P:regulation of receptor binding; IMP:MGI.
DR   GO; GO:0016202; P:regulation of striated muscle tissue development; ISO:RGD.
DR   GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR   GO; GO:0009725; P:response to hormone; IDA:RGD.
DR   GO; GO:0048545; P:response to steroid hormone; IDA:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0042060; P:wound healing; IMP:RGD.
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   Copper; Direct protein sequencing; Disulfide bond; Glycoprotein; LTQ;
KW   Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal;
KW   Sulfation; TPQ.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:26479776"
FT   PROPEP          22..162
FT                   /note="Removed by BMP1"
FT                   /evidence="ECO:0000269|PubMed:8636146"
FT                   /id="PRO_0000018524"
FT   CHAIN           163..411
FT                   /note="Protein-lysine 6-oxidase, long form"
FT                   /evidence="ECO:0000269|PubMed:8636146"
FT                   /id="PRO_0000018525"
FT   CHAIN           213..411
FT                   /note="Protein-lysine 6-oxidase, short form"
FT                   /evidence="ECO:0000250|UniProtKB:P28300"
FT                   /id="PRO_0000447888"
FT   REGION          60..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..411
FT                   /note="Lysyl-oxidase like"
FT   BINDING         286
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255"
FT   BINDING         288
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255"
FT   BINDING         290
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255"
FT   SITE            212..213
FT                   /note="Cleavage; by ADAMTS2 and ADAMTS14"
FT                   /evidence="ECO:0000250|UniProtKB:P28300"
FT   MOD_RES         181
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P28300"
FT   MOD_RES         349
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:P33072"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        232..238
FT                   /evidence="ECO:0000250|UniProtKB:P33072"
FT   DISULFID        285..334
FT                   /evidence="ECO:0000250|UniProtKB:P33072"
FT   DISULFID        318..324
FT                   /evidence="ECO:0000250|UniProtKB:P33072"
FT   DISULFID        345..355
FT                   /evidence="ECO:0000250|UniProtKB:P33072"
FT   DISULFID        392..406
FT                   /evidence="ECO:0000250|UniProtKB:P33072"
FT   CROSSLNK        314..349
FT                   /note="Lysine tyrosylquinone (Lys-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:P33072"
SQ   SEQUENCE   411 AA;  46559 MW;  EE68C9C5AACDFC1A CRC64;
     MRFAWTVLFL GQLQFCPLLR CAPQAPREPP AAPGAWRQTI QWENNGQVFS LLSLGAQYQP
     QRRRDSSATA PRADGNAAAQ PRTPILLLRD NRTASARART PSPSGVAAGR PRPAARHWFQ
     VGFSPSGAGD GASRRAANRT ASPQPPQLSN LRPPSHVDRM VGDDPYNPYK YSDDNPYYNY
     YDTYERPRSG SRHRPGYGTG YFQYGLPDLV PDPYYIQAST YVQKMSMYNL RCAAEENCLA
     SSAYRADVRD YDHRVLLRFP QRVKNQGTSD FLPSRPRYSW EWHSCHQHYH SMDEFSHYDL
     LDASTQRRVA EGHKASFCLE DTSCDYGYHR RFACTAHTQG LSPGCYDTYA ADIDCQWIDI
     TDVQPGNYIL KVSVNPSYLV PESDYSNNVV RCEIRYTGHH AYASGCTISP Y
 
 
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