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Database: UniProt
Entry: A0A1V4L109_PATFA
LinkDB: A0A1V4L109_PATFA
Original site: A0A1V4L109_PATFA 
ID   A0A1V4L109_PATFA        Unreviewed;      1187 AA.
AC   A0A1V4L109;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ferroxidase {ECO:0000256|ARBA:ARBA00013107};
DE            EC=1.16.3.1 {ECO:0000256|ARBA:ARBA00013107};
GN   Name=HEPHL1 {ECO:0000313|EMBL:OPJ90322.1};
GN   ORFNames=AV530_010129 {ECO:0000313|EMBL:OPJ90322.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ90322.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ90322.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ90322.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ90322.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ90322.1}.
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DR   EMBL; LSYS01000355; OPJ90322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4L109; -.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
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   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   SUPFAM; SSF49503; Cupredoxins; 6.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1142..1164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          125..234
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          341..388
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   DOMAIN          482..589
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          835..933
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          977..1092
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   1187 AA;  133336 MW;  4BA196DF19CD11B8 CRC64;
     MVQVAEGWDA MNLICFLNPV YDFKANCTPV MRGGCLRALG FLWLFAVVEA KTRTYYLGIV
     EENWDYAPSG KNLITGQNLL EDKFASVYAT RGANRIGRVY KKAIFRQFTD DTYSQEIPKP
     AWLGFLGPVL KAEQEDVFII HLKNFASRPY SVHPHGVFYD KDSEGALYPD GTGGKSKEDD
     FVVPGGNYTY TWPVRKDYSP TLADSNCLTW IYHSHIDTPR DIASGLIGPL LVCKKGTADE
     TSIEGTGAAN AFALMFSIVD ENFSWYLDEN INTFCLEPAT VDKEDKGFQT SNRMHAINGY
     IYGNLPGLEM CADTSMSWHL FGMGSEIDIH AAYFYGHTFT NRDQRADVVG LFPATFITAE
     MTPGNPGRWL ITCQVNEHLR GGMEALYDVQ ICKKNLSRPS PFSHKRRYYI AAEEVLWNYG
     PDGYDKFTGQ GLNATGSESA IYFTQGIDRI GGQYWKVRYV EYTDATFSKR KVRSEDMKHL
     GILGPVIKAE VGDTVLVTFA NKAKRSYSIM AHGVSFSKLS EGAPYLDGYL KPGAHVKPGE
     TFTYKWRVPE NGGPSEVDPP CLTYLYYSAT DAVKDTNSGL VGPLLVCRKN TLNHDGMQKG
     IDREFYLLFS IFDENDSWYL NKNIEAFTGD PSKVDENDAD FKESNKMHAV NGYLFGNLPG
     LAMCKDDRVS WHLIGLGSHY DMHGVHFQGN TIDLRGTTRD GLALFPHLSG TALMQPDRVG
     TFKVVCRTFD HFVGGMKHLY EVSSCRNTTR AQQQHGAMRL YYIAAEEVEW DYASNKSSAP
     NIYNVSSNEE SYGHVFLNQA EDLIGSKYKK VVYREYTNGN FTQRKVRSEE EEHLEILGPL
     LHAEVGDSVL IIFKNKASRP YSVSAHGVEE VGCEEQPETP ITLPGEINTY RWNVPERSGP
     GKTDPNCITW VYYSTANFVK DTYSGLIGPL VVCRKGVLDE RGVRKDIDRE FTLLFMVFDE
     NESWYLKENI ETYLHKDPDD FNSTKDFVEG NSKHAINGKI YNSLLGLMMN QGDRTNWYLI
     GMGNEVDIHT VHFHAQTFIF KTDKDHRGDV YDLFPGTFQT VELVAENPGT WLLHCHVADH
     IHAGMETTYT INKSEREAPS EGGVTTEAYN TTIAKNRTTT NDYDNIGGNF FGKALSPGEA
     SLILAVFFFI GLVLLSTVLT LCLITRQGSR IRYTALHDKS ALLADSL
//
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