ID A0A3Q1G3B6_9TELE Unreviewed; 777 AA.
AC A0A3Q1G3B6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000023384.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000023384.1}
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|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; A0A3Q1G3B6; -.
DR Ensembl; ENSAPOT00000011412.1; ENSAPOP00000023384.1; ENSAPOG00000005233.1.
DR GeneTree; ENSGT00940000158157; -.
DR Proteomes; UP000257200; Unplaced.
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; 2.
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:UP000257200};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..777
FT /note="Lysyl oxidase homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018622120"
FT DOMAIN 54..155
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 180..315
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 336..436
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 446..549
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT REGION 29..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 80..144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 93..154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 124..134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 281..291
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 361..425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 374..435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 405..415
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 517..527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 777 AA; 86738 MW; 4AD22CD8A246DE53 CRC64;
MEKSRRQQRL AFILLFGLWL PCCFTQTTPS NSATPTPTPS PSPSPQPRTE KLKVRLAGYP
RKHNEGRIEL FYKGEWGTIC DDDFSLANAN VLCRQLGFVS ATGWTHSAKY GKGQGKIWLD
NVLCGGGEKS IELCKSRGWG NSDCTHDEDA GVVCKDERIP GFVDSNVIDA HVDENKIEEV
RLRPVVAMAK KKLPITEGVV EVKYKDGWAQ ICDIGWTIKN TRVVCGMLGF PHERKVNKNF
YKRLKKRAAE KLPRPKVNVS AGGRLYLERQ KNYFHIHSVA CLGTEVHLAA CPLEFSKANA
TSACTGGMPA VVSCMPGPLF MQNSGLKKKL KISSNVRLKG GSRVGEGRVE VLKDNEWGTV
CDDRWNLQSA SVVCRELGFG SAKEALTGGR LGQGMGPIYM NEVKCVGQER SIWNCPFKNI
TSEDCHHMED AAVRCNIPYM GLENTIRIVG GRSSYEGRVE VQVGSKWGTV CSTGWTTKEA
MVVCRQLGLG YSMHAVTETW YWDSSNVTEM VMSGVKCTGS EMSLSQCQHH KTVSCQKAAA
KFAAGVICSE TASDLVLNAS LVQQTVYIED RPLHMLYCAA EEDCLSKSAA KANWPYGHRR
LLRFSSQIHN IGRADFKPKA GRHSWVWHAC HGHYHSMDIF THYDLLNANG TKVAEGHKAS
FCLEDTDCQE GVSKRYECAN FGDQGITVGC WDLYRHDIDC QWIDITDVKP GNYILQIVIN
PNYEVAESDF TNNAMKCNCK YDGHRIWLHN CHIGDAFSEE AERRFEKYPG QLNNRIS
//
