ID A0A3Q4APD1_MOLML Unreviewed; 769 AA.
AC A0A3Q4APD1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Lysyl oxidase homolog {ECO:0000256|RuleBase:RU367046};
DE EC=1.4.3.13 {ECO:0000256|RuleBase:RU367046};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000006285.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000006285.1}
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; A0A3Q4APD1; -.
DR STRING; 94237.ENSMMOP00000006285; -.
DR Ensembl; ENSMMOT00000006397.1; ENSMMOP00000006285.1; ENSMMOG00000004914.1.
DR OMA; VVCPKGG; -.
DR Proteomes; UP000261620; 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:SF7; LYSYL OXIDASE HOMOLOG 2A; 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:UP000261620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU367046};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|RuleBase:RU367046}.
FT DOMAIN 61..162
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 190..301
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 325..424
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 434..543
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DISULFID 87..151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 100..161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 131..141
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 266..276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 394..404
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 510..520
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 769 AA; 85995 MW; 65F5CE3795A9B49F CRC64;
MLYFRCPWFH YLIVPPSRSL SFPSSCIMLK PGALQVLLSV FLCTWMLCQA QPQSGTPVIQ
LRLVGEKKKH NEGRVEVFYN GVWGTVCDDD FSISAAQVVC RELGFMDAVS WSPSAKYGRG
DGQIWLDNVH CNGGEKSLAQ CHSNGFGVTD CKHSEDVGVV CTQNRIPGFK FIQNRDSAEG
LTVQVEDVRI RATYSHRKRI PITDGFLEVK DGGKWRQICN EDWTEMNSRV ICGMYGFPGE
KRVNLRPYKL LAKRRKKNYW GFSVNCTGNE ADLSDCKMGH EIEMKGNQTC KHGMPVVVSC
VPGRSFAPSV SAGFRKAYRV EQPLVRLRGG AMIGEGRVEV LKNGEWGTVC DDHWNIRAAT
VVCRELGFGS AKEALMDARL GQGIGPVHMN EVECSGFENS LTECRFNRDA LGCSHEEDAA
VRCNVPAMGF QNRLRLSGGR NPYEGRVEVL AERNGSLVWG TVCSESWGTM EAMVVCRQLG
LGFASHAFQE TSYWQGDASA DAVLMSGVRC SGTELTLDQC LHHGKHVQCP KGGGRFAAGV
SCTQTAPDLV LNAQVVEQTT YLEDRPMYIL QCAQEESCLS SSAEKADPSS YRRLLRFSSQ
IQNNGQSDFR PRTAYHSWVW HECHRHYHSM EVFTHYDLLS LNGTKVAEGH KASFCLEDTH
CDEGIQKKYE CANFGAQGIS VGCSDTYRHD IDCQWIDITD LKPGDYIFQV VINPNYEVAE
SDYTNNIMKC RSRYDGQRIW TYNCHIGGSR SLETESSFPG LLTNELSHR
//
