ID A0A3Q3S6H1_9TELE Unreviewed; 891 AA.
AC A0A3Q3S6H1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Lysyl oxidase homolog 4-like {ECO:0000313|Ensembl:ENSMAMP00000018335.1};
GN Name=LOXL4 {ECO:0000313|Ensembl:ENSMAMP00000018335.1};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000018335.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000018335.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SIMILARITY: Belongs to the lysyl oxidase family.
CC {ECO:0000256|ARBA:ARBA00007492}.
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; A0A3Q3S6H1; -.
DR STRING; 205130.ENSMAMP00000018335; -.
DR Ensembl; ENSMAMT00000018813.2; ENSMAMP00000018335.1; ENSMAMG00000012383.2.
DR GeneTree; ENSGT00940000157042; -.
DR InParanoid; A0A3Q3S6H1; -.
DR OrthoDB; 3035117at2759; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IEA:UniProtKB-EC.
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:SF5; LYSYL OXIDASE HOMOLOG 4; 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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; LTQ {ECO:0000256|ARBA:ARBA00022477};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..891
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018540149"
FT DOMAIN 30..132
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 302..425
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 446..546
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 556..664
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT REGION 138..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 57..121
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 70..131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 101..111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 391..401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 471..535
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 484..545
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 515..525
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 632..642
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 891 AA; 99192 MW; C2D09D5E1E8E90E9 CRC64;
MLGLRSLSTL LLLLLLSLSP PPLSAQEVLV RLAGVGRRGA NEGRVEVFYN GAWGTVCDDE
VDIHLATVVC RQLGYQSSFS WAHSAKFGQG QGAIWLDNVR CRGTEHSIAE CQSNGWGISD
CTHAEDLGVI CSPARRPGFA PVDESNSSPG RQPRQRNPQS VSPPSPPAAQ TSSLHGRGHE
IALHRSPTSR RSSISPQENG HEIQILRRNR DSPRVNQQLN TALPQGHELP SRLANGALYR
QTQAETNRQP YPQYQSEPRS DRHQQISGNH IEPDPVYPDN GLETNGHYTQ GSDRIQLQEA
RLRPVLSSNH GGLVTEGVLE VKNAGKWRHV CSHGWDLSSS RVICGMLGFP AAEEFDQNAY
RKLWDSKLSD PSSRLRTQIS KKAYWVEKVQ CQGVEASLSQ CRVQTSLPRS DVPCRGGMHA
VVRCVPGSQF TRYGRVPAPP AVPPVVRLKS GPRIGEGRVE VLREGKWGTV CDHLWDMTAA
SVACRELGFG TAKEALTKAQ LGQGTGPIHM NSVQCTGRER SITECQYRPV PLYSCKHNQD
VAVRCNVPNT GIQTTVRLAG GRDQAEGRVE VLMEVGGVRR WGSICSENWG LNEAMVVCRQ
LGLGFASRAH QETWYWSGSP DARDVVLSGT HCIGTEMSIQ QCRKNTHVYC PRGGDGRAAG
VTCVEAAPDL VLDAQLVQET AYLEDRPLHL LTCANEENCL SSSAARMNWP YGHRRLLRFS
SRIMNLGRAD FQPRASREDW IWHQCHRHYH SIEVFTHYDL LTFNGTKVAE GHKASFCLED
TYCPDGVHKR YACYNMGHQG ISVGCWDTYR HDIDCQWVDI TDVRPGEYIF QVEVNPSLDM
AESDFQNNVM RCRCKYDGAR VYMFGCHAGD AYSAEVEDLF DHHRQISNNF L
//
