ID   A0A3Q7T3P7_VULVU        Unreviewed;      1065 AA.
AC   A0A3Q7T3P7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=ferroxidase {ECO:0000256|ARBA:ARBA00013107};
DE            EC=1.16.3.1 {ECO:0000256|ARBA:ARBA00013107};
GN   Name=LOC112932803 {ECO:0000313|RefSeq:XP_025871554.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025871554.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025871554.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025871554.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025871554.1};
RG   RefSeq;
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   RefSeq; XP_025871554.1; XM_026015769.1.
DR   AlphaFoldDB; A0A3Q7T3P7; -.
DR   Ensembl; ENSVVUT00000021615; ENSVVUP00000016452; ENSVVUG00000012074.
DR   OMA; HVTDHIS; -.
DR   Proteomes; UP000286640; Unplaced.
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; cd04224; CuRO_3_ceruloplasmin; 1.
DR   CDD; cd11022; CuRO_4_ceruloplasmin; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 5.
DR   InterPro; IPR011707; Cu-oxidase-like_N.
DR   InterPro; IPR001117; Cu-oxidase_2nd.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   PANTHER; PTHR46806:SF7; COAGULATION FACTOR VIII; 1.
DR   PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00394; Cu-oxidase; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 2.
DR   SUPFAM; SSF49503; Cupredoxins; 6.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1065
FT                   /note="ferroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018739211"
FT   DOMAIN          91..202
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          223..357
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          807..865
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          954..1057
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   1065 AA;  122562 MW;  54D9E0ADDAD471A6 CRC64;
     MKILLLGIFL FLYSNSAWAK EKHYYIGIVE TTWDYASDNK EKKLISVDTE HSNIYLQNGP
     NRIGRLYKKA LYLQYTNENF KTVIEKPVWL GFLGPIIKAE IGDKVYVHLK NFASRPYTFH
     PHGITYRKEY EGAIYPDNTV GSHKADDKVL PGQQYTYILD ASQDDSPGEE DSNCVTRIYH
     SHIDAPKDIA SGLIGPLIVC RKDTLENEKE KNIDQEFVVM FSVVDENLSW YLDDNIKTYC
     SEPEKVDKDD EDFQESNRMY SVNGYTFGSL PGLSMCAEDR VKWYLFGMGN EVDVHAAFFH
     GQVLTNKNYR VDTVNLFPAT LFEAFMVAQN PGEWMLSCQN LNHLKAGLQA FFQVQDCKKP
     SSEKNIRWKY VKHYYIAAEE IIWDYAPSGL NNFTKENLTA PGSASEVFFK QGTTRIGGSY
     KKLVYRAYTD ASFTNRKERG PEEEHLGILG PVIWAEVGFI IRVTFYNKGK YPLSIEPVGV
     RVSKNYEGTY YSSRNNTRTE STPPSASHVA PGQTFTYEWT VPEEVGPTYK DPVCLSKMYY
     SAVDPTKDIF TGLIGPMKIC KKGGLQPNGK QKGVDKEFYL FPTVFDENES LLLDENIRMF
     TTAPDLVNKE DEDFQESNKM HSINGFMYGN QPGLNMCRGD SVVWYLFSAG NEADVHGIYF
     TGNTYLSKGE RRDTANLFPQ TTTTLIMQPD TPGTFDVECL TTDHYTGGMK QKYTVNKCKQ
     QSAHVGHYRS ERFYYIAAVE VEWDYSPSRE WEQELRLLQE QNVSNVFLDK KEFYIGSKYK
     KVVYRRYMDS MFRVPVKREN REEHLGILGP QLRADVGDKV KITFKNMATR PYSIHAHGVK
     TDNSTVIPTL PGKTRIYTWK IPDRAAAGIE DSACIPWAYY STVDQVKDLY SGLIGTLIVC
     RRHYTEFFHP ILKLEFSLLF FVFDENESWY IDDNIKTYSN HPEKVNKDDK EFIESNKMHA
     INGRMFGNLR GLRMNVGDEV NWYLMGMGNE IDLHSVHFHG HSFGYKHRGI YRSDVFDIFP
     GTYQTVEMFP RTPGTWLLHC HVTDHIHAGM ETTYTVLSNR DTNVR
//