HEPHL_ACRMI
ID HEPHL_ACRMI Reviewed; 1114 AA.
AC B3EWZ9;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Hephaestin-like protein {ECO:0000303|PubMed:23765379};
DE EC=1.-.-.- {ECO:0000250|UniProtKB:Q9BQS7};
DE Flags: Precursor;
OS Acropora millepora (Staghorn coral) (Heteropora millepora).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Acroporidae; Acropora.
OX NCBI_TaxID=45264;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=22490231; DOI=10.1111/j.1365-294x.2012.05554.x;
RA Moya A., Huisman L., Ball E.E., Hayward D.C., Grasso L.C., Chua C.M.,
RA Woo H.N., Gattuso J.P., Foret S., Miller D.J.;
RT "Whole transcriptome analysis of the coral Acropora millepora reveals
RT complex responses to CO(2)-driven acidification during the initiation of
RT calcification.";
RL Mol. Ecol. 21:2440-2454(2012).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 29-39; 54-68; 82-92; 97-108; 319-336; 431-442; 460-473;
RP 506-532; 765-775; 785-797; 868-876 AND 902-917, TISSUE SPECIFICITY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23765379; DOI=10.1093/molbev/mst109;
RA Ramos-Silva P., Kaandorp J., Huisman L., Marie B., Zanella-Cleon I.,
RA Guichard N., Miller D.J., Marin F.;
RT "The skeletal proteome of the coral Acropora millepora: the evolution of
RT calcification by co-option and domain shuffling.";
RL Mol. Biol. Evol. 30:2099-2112(2013).
CC -!- FUNCTION: May function as a ferroxidase and may be involved in copper
CC transport and homeostasis. {ECO:0000250|UniProtKB:Q9BQS7}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q9BQS7};
CC Note=Binds 6 Cu cations per monomer. {ECO:0000250|UniProtKB:Q9BQS7};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Note=Presence in the organic matrix of the
CC skeleton may be due to shedding of a soluble peptide. {ECO:0000255,
CC ECO:0000303|PubMed:23765379}.
CC -!- TISSUE SPECIFICITY: Component of the acid-insoluble and acid-soluble
CC organic matrix of the aragonitic skeleton (at protein level).
CC {ECO:0000269|PubMed:23765379}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000255}.
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DR EMBL; JT019463; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B3EWZ9; -.
DR SMR; B3EWZ9; -.
DR PRIDE; B3EWZ9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0016021; C:integral component of 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; -; 3.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
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; PTHR11709; 4.
DR Pfam; PF07731; Cu-oxidase_2; 3.
DR Pfam; PF07732; Cu-oxidase_3; 3.
DR PIRSF; PIRSF000354; Factors_V_VIII; 1.
DR SUPFAM; SSF49503; SSF49503; 6.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Copper transport; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Ion transport; Membrane; Metal-binding; Oxidoreductase;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1114
FT /note="Hephaestin-like protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429546"
FT TOPO_DOM 27..1091
FT /note="Extracellular"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:23765379"
FT TRANSMEM 1092..1112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1113..1114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..210
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 218..365
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 380..562
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 572..719
FT /note="Plastocyanin-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 730..915
FT /note="Plastocyanin-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 924..1114
FT /note="Plastocyanin-like 6"
FT /evidence="ECO:0000255"
FT BINDING 129
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 131
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 189
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 191
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 303
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 346
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 351
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 657
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 700
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 705
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 710
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 1014
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 1017
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 1019
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 1059
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 1060
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 1061
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 1065
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT BINDING 1070
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 831
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 183..209
FT /evidence="ECO:0000250|UniProtKB:Q9BQS7, ECO:0000255"
FT DISULFID 284..365
FT /evidence="ECO:0000250|UniProtKB:Q9BQS7, ECO:0000255"
FT DISULFID 536..562
FT /evidence="ECO:0000250|UniProtKB:Q9BQS7, ECO:0000255"
FT DISULFID 638..719
FT /evidence="ECO:0000250|UniProtKB:Q9BQS7, ECO:0000255"
FT DISULFID 889..915
FT /evidence="ECO:0000250|UniProtKB:Q9BQS7, ECO:0000255"
SQ SEQUENCE 1114 AA; 124798 MW; 40E23EA1CBB77FF3 CRC64;
MMDRSNAAFV LTACFIFSQL ICHVAAITRT YYIAAVEKEW DYAPSGYNKI KGVKLEDDSD
ATVFATKGAH RIGRIYDKVL YREYEDASFT KEKPHPKYLG FLGPILKGEI GDTIVVHFKN
NGSRVYSMHP HGVFYSKDSE GALYEDNTKG KFKKDDKVPP GGTHTYSWHL TQSHAPADQE
DKCITWIYHS HVVPSKDINT GLLGIMLICR KGALNQGQQS GVDKEFVALF TVLDENESWL
LSKNIERCSD PTRVNPDDED FKESNKMHAI NGYFYGNLPG LDMCYGDSVK WHLAGIGNEV
DIHTAYFHGQ SFTIDGHRKD VASLLPATFV TASMKALNPG KWMLNCLVND HYNAGMYTLF
NVTKCPGKVG VAPSVSGGKK RTYFIAANEV EWNYGPTGVN GMDGQSLIAP GSDSAVFFAQ
NAQRIGGTYL KAIYEQYTDA RFSTKVPKPE HLGFLGPVIR AEVNDIIEVV FKNNARFNFS
IQPHGVFFNK SNEGALYEDG TSRAQKADDN VQPGQTFTYR WTVPEEVGPT KSDAACITWV
YHSSVDPVKD TYSGLFGPLL TCKKGTLNND NTRKDTDKEF VLLFTVTDES ESWYHEKNKE
MKANAILIND DDEDYKESNK MHGINGFLYA NLPGLEMCLG DTISWHVIGL GNEVDMHTAY
FYGNTFTHQG SVKDTVSLLP GVFGTLTMTP DNAGDWALVC RTNDHYSAGM QAKYKVNTCN
RNPELKTSGK TRDYYIAAFE MEWDYAPTGL DALDGKKLDQ SEEAKVFTVT SDKRIGRKYV
KAVYREFTND QFNQQKLRTP AEEHLGILGP MLHAEVGDTI KVVFKNNANR NYSVHPHGLY
YSKAHEGSDY NDGTSGADKL DNAIQPGKTY TYIWKVPERA GPGKDGPACA TWAYYSDVNP
IKDTNSGLIG PLIICKKGKL KEGTEERSDV DREFVLMFTV LDENESWYLD ENIKKYCKNP
GDKETLKADD DFMESNKMHG INGFVFGNLK GLKMYQDEKV DWLLLGIGNE VDMHTVHFHG
QSFLRKQVSY HREDVYDLFP GVFATVEMVP DSTGDWLLHC HVNDHMVAGM ETLYSVLDKS
LKTTPKPITA ASSFVTSSIF IYLSFPVLAM LLKA
