LOXL4_BOVIN
ID LOXL4_BOVIN Reviewed; 757 AA.
AC Q8MJ24;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Lysyl oxidase homolog 4;
DE EC=1.4.3.-;
DE AltName: Full=Lysyl oxidase-like protein 4;
DE Flags: Precursor;
GN Name=LOXL4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tepsiri N., Grant M.E., Boot-Handford R.P., Wallis G.A.;
RT "The investigation of the lysyl oxidase related gene in the bovine growth
RT plate cartilage.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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; AF529202; AAM94335.1; -; mRNA.
DR RefSeq; NP_776809.1; NM_174384.2.
DR AlphaFoldDB; Q8MJ24; -.
DR SMR; Q8MJ24; -.
DR STRING; 9913.ENSBTAP00000027838; -.
DR PaxDb; Q8MJ24; -.
DR PRIDE; Q8MJ24; -.
DR GeneID; 281904; -.
DR KEGG; bta:281904; -.
DR CTD; 84171; -.
DR eggNOG; ENOG502QSX8; Eukaryota.
DR HOGENOM; CLU_002555_3_0_1; -.
DR InParanoid; Q8MJ24; -.
DR OrthoDB; 815466at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
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; 2.
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_0000045441"
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 /evidence="ECO:0000250"
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"
SQ SEQUENCE 757 AA; 84050 MW; 0A17A02C2D793984 CRC64;
MWFLPAALPL LPLLLLLGQA PPSRPQSLGT MKLRLVGPGS GPEEGRLEVL HQGQWGTVCD
DDFALQEATV ACRQLGFEGA LTWAHSAKYG SGEGPIWLDN VHCVGTESSL DQCGSNGWGV
SDCTHSEDVG VVCNPQRHRG SVSERVSNAL GPQDRRLEEV RLKPILASAK RQSPVTEGAV
EVKYEGHWRQ VCDQGWTRNN SRVVCGMLGF PSEAPVDSHH YRKVWDSKMK DPNSRLKSLT
KKNSFWIHRV NCLGTEPHMA NCQVQVAPAQ GKLRPACPGG MHAVVSCVAG PRFRPPKAKP
GRKESRAEEM KVRLRSGAQV GEGRVEVLMN RQWGTVCDHG WNLISASVVC RQLGFGSARE
ALFGAQLGQA LGPIHLSEVR CRGYERTLSD CPSLEGSQNG CQHDNDAAVR CNIPNMGFQD
QVRLAGGRSP EEGVVEVQVE VNGVQRWGAV CSDHWGLSEA MVACRQLGLG FASHAIKDTW
YWQGTPGARE VVMSGVHCSG TELALQQCQR HGPVHCSHGT GRFSAGVSCT DSAPDLVMNA
QLVQETAYLE DRPLSLLYCA HEENCLSQSA DRMDWPYGHR RLLRFSSQIH NLGRADFRPK
MGRHGWIWHQ CHRHYHSIEV FTHYDLLTLN GSKVAEGHKA SFCLEDTNCP TGMQRRYACA
NFGEQGVTVG CWDTYRHDID CQWVDITDVG PGDYIFQVVV NPKFEVAESD FSNNMMRCRC
KYDGQRVWLH NCHTGDSYRA NTELSQEQEQ RLRNNLI
