ID A0A3P8YLE5_ESOLU Unreviewed; 563 AA.
AC A0A3P8YLE5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Lysyl oxidase homolog 1 {ECO:0000313|Ensembl:ENSELUP00000017369.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000017369.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000017369.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000017369.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SIMILARITY: Belongs to the lysyl oxidase family.
CC {ECO:0000256|ARBA:ARBA00007492}.
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DR RefSeq; XP_010876944.1; XM_010878642.3.
DR RefSeq; XP_019907089.1; XM_020051530.1.
DR AlphaFoldDB; A0A3P8YLE5; -.
DR STRING; 8010.ENSELUP00000017375; -.
DR Ensembl; ENSELUT00000026941.2; ENSELUP00000017369.1; ENSELUG00000017079.2.
DR GeneID; 105015456; -.
DR KEGG; els:105015456; -.
DR GeneTree; ENSGT00940000161080; -.
DR InParanoid; A0A3P8YLE5; -.
DR OMA; SATPWRQ; -.
DR OrthoDB; 3035117at2759; -.
DR Proteomes; UP000265140; LG02.
DR Bgee; ENSELUG00000017079; Expressed in nose and 12 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW LTQ {ECO:0000256|ARBA:ARBA00022477};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..563
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030079127"
FT REGION 57..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 61697 MW; 9D09845079FD1D45 CRC64;
MMMLPFVVGS LVWVLLGSGW AQVQDQTQAS TPWRQMIQWE NNGRRFSLLN SGAEYVPAGS
QDQERSHRVV VADSRSRTPR RPQGGNVRRQ APSRGGSETV RGQTRHPFGF GQVPDNWRQG
SVGTGSTSTR FRPSTGSSSS SSSSSSFSSS YNIPVQPYPQ FPFPQQPSYQ LPYDPSVVEG
AGRGYAEPPF QRATGGGYSA GAGGYVGGGG GYAGVSYGAG AGLAPVVPRS PQDYGEDGYR
YYPPYGYGPN PGAPVQPAVP ARAAQPPFSD GLDRRYTHSL YNGGEDSAAA ADTAPAAQDR
TGAVAQAPVR SPQYEQFPPF GRPQVQPQPA APVRNPNTAV ENPSVNVGSV YRPEQRGLPD
LVPDPNYVQA STYIQRAHMY SLRCAAEEKC LASTAYSAET TDYDVRVLLR FPQRVKNQGT
ADFLPNRPRH TWEWHSCHQH YHSMDEFSHY DLLEVTTGRK VAEGHKASFC LEDTTCDFGH
LKRYACTSHT QGLSPGCYDT YNADIDCQWI DITDIQPGNY ILKLQVNPKY LILESDFTNN
VVRCNIHYTG RFVTTNNCKI SQS
//