ID W5KEB5_ASTMX Unreviewed; 733 AA.
AC W5KEB5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000005926.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000005926.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Mediates the post-translational oxidative deamination of
CC lysine residues on target proteins leading to the formation of
CC deaminated lysine (allysine). {ECO:0000256|RuleBase:RU367046}.
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:0000256|RuleBase:RU367046};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935,
CC ECO:0000256|RuleBase:RU367046};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|RuleBase:RU367046}.
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:0000256|RuleBase:RU367046}.
CC -!- SIMILARITY: Belongs to the lysyl oxidase family.
CC {ECO:0000256|ARBA:ARBA00007492, ECO:0000256|RuleBase:RU367046}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR AlphaFoldDB; W5KEB5; -.
DR STRING; 7994.ENSAMXP00000005926; -.
DR Ensembl; ENSAMXT00000005926.2; ENSAMXP00000005926.2; ENSAMXG00000005786.2.
DR eggNOG; ENOG502QSX8; Eukaryota.
DR GeneTree; ENSGT00940000158157; -.
DR HOGENOM; CLU_002555_3_0_1; -.
DR InParanoid; W5KEB5; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000005786; Expressed in zone of skin and 11 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.250.10; SRCR-like domain; 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 PANTHER; PTHR45817:SF2; LYSYL OXIDASE HOMOLOG 3; 1.
DR PANTHER; PTHR45817; LYSYL OXIDASE-LIKE-RELATED; 1.
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; SRCR-like; 4.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 4.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU367046};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196};
KW LTQ {ECO:0000256|ARBA:ARBA00022477, ECO:0000256|RuleBase:RU367046};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367046};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367046};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU367046};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|RuleBase:RU367046}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..733
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030179375"
FT DOMAIN 33..134
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 159..266
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 287..387
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 397..505
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DISULFID 59..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 72..133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 103..113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 191..255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 204..265
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 233..243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 312..376
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 325..386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 356..366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 473..483
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 733 AA; 81499 MW; 0DF726B3BC3C8188 CRC64;
MGKSQYVVVM LACLWLPSTL CQTSSPQHEQ LKFRLAGYPR KHNEGRVEVF YSGEWGTICD
DDFTLSNAHV LCRHLGFVEA LSWSHSAKYG AGTGKIWLDN VMCSGSETSI DKCLSRGWGN
SDCTHEEDAG VICKDERLPG FLDSNIIEMQ VDENRMEKVR LRPLSAAHAA RMPVTEGVVE
VKYKEGWRQI CNVGWTARNS RVVCGMMGFP SERIQAKKPN SHRSVCRIHS VACSGNEAHL
SACTMEFSTN TSSACPGGGP VVVSCVPGPQ FSNGRGRKSK LNHVSKVRLK GGAKAGEGRV
EVLKGSEWGT VCDDLWNLQS ASVVCRELGF GTAKEALTGA RMGQGMGPIH MNEVQCVGDE
KSLLKCPHKS ITAENCKHME DASVKCNIPY MGFEKTIRLT GGRTQLEGRV ELLAPNASSL
EQWGLICGDG WTSREAMVAC RQLGLGHASS GLSETWYWDS SNVTEMVMSG VKCRGDEMTL
SDCQHHHIVS CKRAGAQFSA GVICSDSASD LVLNAPLVEK SVYIEDRPLH LLYCAAEENC
LSKSAVRANW PYGHRRLLRF SSEIHNVGRA DFRPRLGRHS WVWHECHRHY HSMDIFTHYD
LLDLNGTKVA DGHKASFCLE DTDCHEGISK RYECANFGEQ GITVGCWDTY RHDIDCQWID
ITDVKPGNYI LQVVLNPNFE VAESDFTNNA MRCNCKYDGN RIWLHKCHIG DSYSEEAEKQ
FELYPGQLNN KIS
//
