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
//