ID W5KBA0_ASTMX Unreviewed; 1085 AA.
AC W5KBA0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=ferroxidase {ECO:0000256|ARBA:ARBA00013107};
DE EC=1.16.3.1 {ECO:0000256|ARBA:ARBA00013107};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000004861.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000004861.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001830};
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR AlphaFoldDB; W5KBA0; -.
DR STRING; 7994.ENSAMXP00000004861; -.
DR Ensembl; ENSAMXT00000004861.2; ENSAMXP00000004861.2; ENSAMXG00000004739.2.
DR eggNOG; KOG1263; Eukaryota.
DR GeneTree; ENSGT00940000155866; -.
DR HOGENOM; CLU_005569_0_0_1; -.
DR InParanoid; W5KBA0; -.
DR OrthoDB; 537265at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000004739; Expressed in ovary and 8 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR CDD; cd11021; CuRO_2_ceruloplasmin; 1.
DR CDD; cd04225; CuRO_5_ceruloplasmin; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 4.
DR InterPro; IPR048236; Ceruloplasmin-like_CuRO_5.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR024715; Factor_5/8-like.
DR PANTHER; PTHR46806:SF7; COAGULATION FACTOR VIII; 1.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07731; Cu-oxidase_2; 2.
DR Pfam; PF07732; Cu-oxidase_3; 3.
DR PIRSF; PIRSF000354; Factors_V_VIII; 3.
DR SUPFAM; SSF49503; Cupredoxins; 6.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000354-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1085
FT /note="ferroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017274627"
FT DOMAIN 95..205
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 309..356
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT DOMAIN 449..492
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 820..879
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 969..1073
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 131..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 177..203
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 279..360
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 548..574
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 650..731
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ SEQUENCE 1085 AA; 123698 MW; 85C53C71B3CA78DC CRC64;
MGALRWSVIG FLCCVGSVSG VFREYFIGIK EIQWDYAPSG MNMIQNKTLK EDAHARTFLE
KGEQRIGRVY KKAVYLQYTD ATFRQEIEKP KWMGYLGPLI TAEEGDTVVV HLKNMASRPY
SIHPHGMSYN KSNEGALYPD QSDPAEKRDD SVAPGKAYSY IWPLESSHAP GKDDPNCLTR
VYHSHVTAPK DIATGLIGPL IICKKGSLDV HGEKSGDYLY ALMFTVSDEN LSWYLDDNIK
THCTVPAKVK KDDEDFIESN KMHSINGYVF GNLPDLSMCM GNKIHWHLFG IGNEVDVHSA
FFHGQVLTNR QHRTDTVSLF PATFANVQME ADNPGQWLLS CQVNDHLEAG MQAFFEIKKC
FPNVHKPRPF GAVRQYYIAA EEVIWDYGPT QINQYTGIKL EDDSMADTFF DNRDDRIGGK
YKKVQYVEYT DDTFTKRKER TPEEQHLGIL GPIIRAEEED TIKVTFRNKA SRPYSIQPHG
VQYSIEMDGT LYHNVLEESY TAKKLRELKK EARVIEPLPA AMVLPDTTFK YEWVVPKAGG
PAAGDPDCIS YLYYSAVDPI RDTNSGLVGP LLICKPKTLK SGKQKNVKKE FHILATNFDE
NLSWYLDENI NRYAKNPKTV KKDDEDFELS NQMRSLNGYM YGNLKGLTMC KGDKVSWHLY
GLGSEGDIHG LYFQGNRFLY RGTRKDTISV FPHVSHTVIM EPDSMGTFEV TCKIADDNHV
GMRANYTVEK CSIFSRQTEV MLHQKKYYIA AVEMDWDYSP TRTWEEKMFN GLKDSPGNPF
LKKEGKFIGS KYRKVLYKEY TDDTFTKPKE RSEDMQHLGI MGPMIHGNVG EKVKIVFKNM
AKRTYSVHAH GIKTENPQVI PTPPGQTQTY TWYIPKTAGP TEEQEECSVG AYYSTVDVNK
DFYSGLIGPL VICKKSLLRK LGLKKEIEEF ALLFTVFDEN QSWYLDDNIK THVKNTPSKL
KEDPDFIESN KMHGINGLVY GNLPGLNMQV GDKVYWYLMG MGKEMDVHTA HFHGHSFEYK
QNGVHRADVF DLFPGTFQTV VMRPQYPGTW LLHCHVTDHV MSGMEATYTV QDKEGRKGFL
GLFPG
//
