ID A0A091UJX4_NIPNI Unreviewed; 646 AA.
AC A0A091UJX4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
DE Flags: Fragment;
GN ORFNames=Y956_14823 {ECO:0000313|EMBL:KFQ90652.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFQ90652.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFQ90652.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFQ90652.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL409578; KFQ90652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091UJX4; -.
DR eggNOG; KOG3698; Eukaryota.
DR Proteomes; UP000053283; Unassembled WGS sequence.
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:UP000053283};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..646
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001880887"
FT DOMAIN 43..144
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 167..280
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 305..405
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 415..525
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT REGION 290..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 69..133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 82..143
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 113..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 246..256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 330..394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 343..404
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 374..384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 492..502
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT NON_TER 646
FT /evidence="ECO:0000313|EMBL:KFQ90652.1"
SQ SEQUENCE 646 AA; 71796 MW; 35F5E771DA896618 CRC64;
MGSCGTWAWQ ELLVLLSSVW LWVGSAQPTP PGPTHTPGSQ LKFRLAGYPR KHNEGRVEVF
YNDEWGTICD DDFTLANAHV LCRHLGFVAA TGWAHSAKYG KGVGRIWLDN VNCAGGEKSI
GDCKHRGWGN SDCSHEEDAG VICKDERIPG FKDSNVIETE QSHVEEVRLR SVVSGARRQL
PVTEGIVEVR YKDSWAQICD EGWDSQNSRV ICGMMGFPAE KKVNRNFYKL FTERQQLNYR
LHSVSCMGTE VHLSMCAFEF YRGNASAACR AGMPAVVSCL PGPLFTTGNA HKKKQRQQQQ
GQPRIRLKGG AKVGEGRVEV LRSSEWGTIC DDHWNLLSAS VVCRELGFGS AKEALTGARM
GQGTGPIHMN EVQCLGTEKS LWSCPFKNIT QDDCKHTEDA AVRCNIPYMG YENLIRLSGG
RSRFEGRVEV AVGAGDGDQP RWGLVCGEGW GTLEAMVACR QLGLGFANHG LQETWYWDAS
NVTEMVLSGV KCAGHEMSLS HCQHHGTSLN CRNTGTRFAA GVICSETASD LLLHAPLVQE
TAYIEDRPLH MLYCAAEENC LSSSARLANW PYGHRRLLRF SSQIHNNGRA DFRPKAGRHS
WVWHECHRHY HSMDIFTHYD ILTPNGTKVA EGHKASFCLE DTECEE
//
