ID W5NBN3_LEPOC Unreviewed; 1136 AA.
AC W5NBN3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Hephaestin {ECO:0000313|Ensembl:ENSLOCP00000018042.1};
GN Name=HEPH {ECO:0000313|Ensembl:ENSLOCP00000018042.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000018042.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000018042.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; AHAT01015630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015206780.1; XM_015351294.1.
DR RefSeq; XP_015206781.1; XM_015351295.1.
DR RefSeq; XP_015206782.1; XM_015351296.1.
DR RefSeq; XP_015206784.1; XM_015351298.1.
DR RefSeq; XP_015206785.1; XM_015351299.1.
DR AlphaFoldDB; W5NBN3; -.
DR STRING; 7918.ENSLOCP00000018042; -.
DR Ensembl; ENSLOCT00000018074.1; ENSLOCP00000018042.1; ENSLOCG00000014659.1.
DR GeneID; 102698283; -.
DR KEGG; loc:102698283; -.
DR CTD; 9843; -.
DR eggNOG; KOG1263; Eukaryota.
DR GeneTree; ENSGT00940000158517; -.
DR HOGENOM; CLU_005569_0_0_1; -.
DR InParanoid; W5NBN3; -.
DR OMA; YCQEGSH; -.
DR OrthoDB; 537265at2759; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000014659; Expressed in embryo and 5 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
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; IPR045087; Cu-oxidase_fam.
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; PTHR11709:SF233; FERROXIDASE HEPHL1; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 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 Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000354-1};
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:UP000018468};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1091..1116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..202
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 282..360
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT DOMAIN 444..551
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 802..862
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 953..1058
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT DISULFID 178..204
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 281..362
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 524..550
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 628..709
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ SEQUENCE 1136 AA; 128718 MW; AC6ADFEECAF4348B CRC64;
MKHIVSIQIM GFLSLMVCVR GATRLYYLGI REIEWNYTPT GKNKISGNNF TEDQDSIKYP
FRNSQTMGRI YKKAVYKQYS DATYAHEIPQ PPWLGFLGPI LKAELGDEII IHLKNFASRP
YSIHPHGVFY SKDSEGAFYP DQTFGKDKTD DGVPPGRTHT YIWTVTGDHA PTASDPNCLT
WAYHSHVDAP RDIASGLIGA LLTCKKGVLD GHTNRSDVDM DFLLMFMNVD ENLSWYVDDN
INRYCSDPGS VDKEDEEFKT RNRMHSINGY IYGNLPDLHM CAGASVTWHL FGMGSEADIH
NAFFHGQSVT VSHRRADVVS LFPATFVTAE MVPRNVGRWL LSCQVNEHLK DGMEALYEVK
ECFKTTPNIQ MPGKERKYFI AAKDVLWSYG PSGIDGETIQ SLMKKSSNTS KRTGGEYWKA
KYVEYTDETF TKEKVRTTSE EHLGILGPVI KAEVGDTIVV KFLNMASRPY SIQPHGVFYK
KEHEGTPYGD DVLGEGTSVQ PLHNFTYKWS VPEHVGPTLS DPPCLTRMYF SAVDPVRDTN
SGLVGPLLIC KPRTLKYDNT QKGIDKEFFL LFTVFNENLS WYLRQSLLHA SVNPNIDIDK
DDEEFKASNL MHAINGFLYS KLPGLEMCRG SNVSWHLLGL GDEFDIHGVV FQGNTVQVNG
RHKDSVTLTP HTSSTLLMQP DNIGTFGVIC LTSEHFLAGM RQQYQVLECN SDRFPSVRVP
QYRVSSVYYI AADEVEWDYS PDRTWELGIL NSSAAESYGH IFVGKEGGLI GSKYQKVVYR
EYTDGTFTKL KERKGDEEHF GILGPLIRAE VGDIIVIVFK NNGSHTHSIH AHGVQELYEG
KGHAAQPGEI VIYRWNIPER SGPGPGDSAC ITWAYYSMVH PVKDLHSGLI GPLITCRKGT
LTPERSRADL DREFSLLFFI FDENQSWYLD KNIAMYSEQN ISEINYEDER FCESNKMHAI
NGKIYANLHG LSMYEEERID WYLIGLGDEI DMHTVHFHAQ SFTFMDGKRH RADVFDLFPA
TFQTLEMKVT NPGTWLLHCH VSDHIHAGME TVYTVHPKNV PQRFDIDSGP ELHVGQIAVF
GKYLSQEEAE FVLTVLLVIG FVLFLTAFIL TGVVIVMSRK KKQNKHYPEE VSLKML
//
