ID A0A2R8ZI91_PANPA Unreviewed; 471 AA.
AC A0A2R8ZI91;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
GN Name=LOXL3 {ECO:0000313|Ensembl:ENSPPAP00000004687.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000004687.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000004687.1}
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|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|RuleBase:RU367046}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJFE02031965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02031966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02031967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R8ZI91; -.
DR Ensembl; ENSPPAT00000021464.1; ENSPPAP00000004687.1; ENSPPAG00000019493.1.
DR GeneTree; ENSGT00940000158157; -.
DR Proteomes; UP000240080; Unplaced.
DR Bgee; ENSPPAG00000019493; Expressed in heart and 6 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; 3.
DR InterPro; IPR001695; Lysyl_oxidase.
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; 3.
DR PRINTS; PR00074; LYSYLOXIDASE.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 3.
DR SUPFAM; SSF56487; SRCR-like; 3.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 3.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|RuleBase:RU367046};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; LTQ {ECO:0000256|RuleBase:RU367046};
KW Metal-binding {ECO:0000256|RuleBase:RU367046};
KW Oxidoreductase {ECO:0000256|RuleBase:RU367046};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|RuleBase:RU367046};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|RuleBase:RU367046}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..471
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015333607"
FT DOMAIN 44..145
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 169..282
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 307..353
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT REGION 289..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 70..134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 83..144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 114..124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 248..258
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 471 AA; 51909 MW; FF515FCF54A0F924 CRC64;
MRPVSVWQWS PWGLLLCLLC SSCLGSPSPS TGPEKKAGSQ GLRFRLAGFP RKPYEGRVEI
QRAGEWGTIC DDDFTLQAAH VLCRELGFTE ATGWTHSAKY GPGTGRIWLD NLSCSGTEQS
VTECASRGWG NSDCTHDEDA GVICKDQRLP GFWDSNVIEV EHHLQVEEVR IRPAVGWGRR
PLPVTEGLVE VRLPDGWSQV CDKGWSAHNS HVVCGMLGFP SEKRVNAAFY RLLAQRQQHS
FGLHGVACVG TEAHLSLCSL EFYRANDTAR CPGGAPAVVS CVPGPLYAAS SGQKKQQQSK
PQGEARVRLK GGAHPGEGRV EVLKASTWGT VCDRKWDLHA ASVVCRELGF GSAQAALSGA
RMGQDVSKRY ECANFGEQGI TVGCWDLYRH DIDCQWIDIT DVKPGNYILQ VVINPNFEVA
ESDFTNNAMK CNCKYDGHRI WVHNCHIGDA FSEEANRRFE RYPGQTSNQI I
//
