HEPH_HUMAN
ID HEPH_HUMAN Reviewed; 1158 AA.
AC Q9BQS7; B1AJX8; D3DVT7; E9PHN8; O75180; Q6UW45; Q9C058;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Hephaestin;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=HEPH; Synonyms=KIAA0698; ORFNames=UNQ2562/PRO6242;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11932491; DOI=10.1093/protein/15.3.205;
RA Syed B.A., Beaumont N.J., Patel A., Naylor C.E., Bayele H.K., Joannou C.L.,
RA Rowe P.S.N., Evans R.W., Srai S.K.S.;
RT "Analysis of the human hephaestin gene and protein: comparative modelling
RT of the N-terminus ecto-domain based upon ceruloplasmin.";
RL Protein Eng. 15:205-214(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhao K.W.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-1158 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [8]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145 AND SER-1150, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May function as a ferroxidase for ferrous (II) to ferric ion
CC (III) conversion and may be involved in copper transport and
CC homeostasis. Implicated in iron homeostasis and may mediate iron efflux
CC associated to ferroportin 1.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 6 Cu cations per monomer. {ECO:0000250};
CC -!- INTERACTION:
CC Q9BQS7-3; O76003: GLRX3; NbExp=3; IntAct=EBI-22734368, EBI-374781;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BQS7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQS7-2; Sequence=VSP_011627;
CC Name=3;
CC IsoId=Q9BQS7-3; Sequence=VSP_047331;
CC Name=4;
CC IsoId=Q9BQS7-4; Sequence=VSP_047332;
CC -!- TISSUE SPECIFICITY: Detected in breast, colon, bone trabecular cells
CC and fibroblasts.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ89349.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAX05385.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAX05388.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Hephaestin entry;
CC URL="https://en.wikipedia.org/wiki/Hephaestin";
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DR EMBL; AJ296162; CAC35365.2; -; mRNA.
DR EMBL; AF148860; AAK08131.1; -; mRNA.
DR EMBL; AY358990; AAQ89349.1; ALT_INIT; mRNA.
DR EMBL; AL030998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05384.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05385.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471132; EAX05386.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05388.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC011561; AAH11561.1; -; mRNA.
DR EMBL; AB014598; BAA31673.2; -; mRNA.
DR CCDS; CCDS14384.3; -. [Q9BQS7-1]
DR CCDS; CCDS14385.1; -. [Q9BQS7-4]
DR CCDS; CCDS48133.1; -. [Q9BQS7-2]
DR RefSeq; NP_001124332.1; NM_001130860.3. [Q9BQS7-2]
DR RefSeq; NP_001269070.1; NM_001282141.1.
DR RefSeq; NP_055614.1; NM_014799.3. [Q9BQS7-4]
DR RefSeq; NP_620074.3; NM_138737.4. [Q9BQS7-3]
DR RefSeq; XP_006724785.1; XM_006724722.1.
DR AlphaFoldDB; Q9BQS7; -.
DR SMR; Q9BQS7; -.
DR BioGRID; 115179; 5.
DR IntAct; Q9BQS7; 2.
DR STRING; 9606.ENSP00000430620; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB13257; Ferrous sulfate anhydrous.
DR TCDB; 8.A.105.1.1; the multi-copper-containing ferroxidase (mcfo) family.
DR GlyGen; Q9BQS7; 8 sites.
DR iPTMnet; Q9BQS7; -.
DR PhosphoSitePlus; Q9BQS7; -.
DR BioMuta; HEPH; -.
DR DMDM; 52782976; -.
DR EPD; Q9BQS7; -.
DR jPOST; Q9BQS7; -.
DR MassIVE; Q9BQS7; -.
DR MaxQB; Q9BQS7; -.
DR PaxDb; Q9BQS7; -.
DR PeptideAtlas; Q9BQS7; -.
DR PRIDE; Q9BQS7; -.
DR ProteomicsDB; 20574; -.
DR ProteomicsDB; 78716; -. [Q9BQS7-1]
DR ProteomicsDB; 78717; -. [Q9BQS7-2]
DR Antibodypedia; 13137; 154 antibodies from 24 providers.
DR DNASU; 9843; -.
DR Ensembl; ENST00000336279.9; ENSP00000337418.5; ENSG00000089472.18. [Q9BQS7-4]
DR Ensembl; ENST00000343002.7; ENSP00000343939.2; ENSG00000089472.18. [Q9BQS7-1]
DR Ensembl; ENST00000441993.7; ENSP00000411687.3; ENSG00000089472.18. [Q9BQS7-2]
DR Ensembl; ENST00000519389.6; ENSP00000430620.2; ENSG00000089472.18. [Q9BQS7-1]
DR GeneID; 9843; -.
DR KEGG; hsa:9843; -.
DR MANE-Select; ENST00000343002.7; ENSP00000343939.2; NM_001367233.3; NP_001354162.2.
DR UCSC; uc004dwn.5; human. [Q9BQS7-1]
DR CTD; 9843; -.
DR DisGeNET; 9843; -.
DR GeneCards; HEPH; -.
DR HGNC; HGNC:4866; HEPH.
DR HPA; ENSG00000089472; Tissue enhanced (intestine, smooth muscle).
DR MIM; 300167; gene.
DR neXtProt; NX_Q9BQS7; -.
DR OpenTargets; ENSG00000089472; -.
DR PharmGKB; PA29241; -.
DR VEuPathDB; HostDB:ENSG00000089472; -.
DR eggNOG; KOG1263; Eukaryota.
DR GeneTree; ENSGT00940000158517; -.
DR HOGENOM; CLU_005569_0_0_1; -.
DR InParanoid; Q9BQS7; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; Q9BQS7; -.
DR TreeFam; TF329807; -.
DR PathwayCommons; Q9BQS7; -.
DR Reactome; R-HSA-425410; Metal ion SLC transporters.
DR Reactome; R-HSA-5655799; Defective SLC40A1 causes hemochromatosis 4 (HFE4) (duodenum).
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR SignaLink; Q9BQS7; -.
DR BioGRID-ORCS; 9843; 11 hits in 702 CRISPR screens.
DR ChiTaRS; HEPH; human.
DR GenomeRNAi; 9843; -.
DR Pharos; Q9BQS7; Tbio.
DR PRO; PR:Q9BQS7; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9BQS7; protein.
DR Bgee; ENSG00000089472; Expressed in jejunal mucosa and 174 other tissues.
DR ExpressionAtlas; Q9BQS7; baseline and differential.
DR Genevisible; Q9BQS7; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IMP:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; IMP:UniProtKB.
DR GO; GO:0004322; F:ferroxidase activity; IMP:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IMP:UniProtKB.
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; IPR027154; HEPH.
DR PANTHER; PTHR11709; PTHR11709; 5.
DR PANTHER; PTHR11709:SF221; PTHR11709:SF221; 5.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 2.
DR SUPFAM; SSF49503; SSF49503; 6.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Copper; Copper transport; Disulfide bond;
KW Glycoprotein; Ion transport; Iron; Iron transport; Membrane; Metal-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1158
FT /note="Hephaestin"
FT /id="PRO_0000002915"
FT TOPO_DOM 24..1110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1111..1131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1132..1158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..206
FT /note="Plastocyanin-like 1"
FT DOMAIN 218..366
FT /note="Plastocyanin-like 2"
FT DOMAIN 379..560
FT /note="Plastocyanin-like 3"
FT DOMAIN 570..718
FT /note="Plastocyanin-like 4"
FT DOMAIN 731..903
FT /note="Plastocyanin-like 5"
FT DOMAIN 911..1087
FT /note="Plastocyanin-like 6"
FT BINDING 126
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 699
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 704
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 709
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1000
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1003
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1005
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1045
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1046
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1047
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1051
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1056
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0Z4"
FT CARBOHYD 164
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 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 873
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 180..206
FT /evidence="ECO:0000255"
FT DISULFID 285..366
FT /evidence="ECO:0000255"
FT DISULFID 534..560
FT /evidence="ECO:0000255"
FT DISULFID 637..718
FT /evidence="ECO:0000255"
FT DISULFID 877..903
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..267
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047332"
FT VAR_SEQ 1
FT /note="M -> MTQTLPYHLSLLNVLFPGPCSRHFKFRRGKCAQPAWRKVSAPSQDLL
FT ITKVMWAM (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047331"
FT VAR_SEQ 1082
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_011627"
FT VARIANT 595
FT /note="A -> T (in dbSNP:rs17216603)"
FT /id="VAR_024379"
FT CONFLICT 55..56
FT /note="DI -> QR (in Ref. 7; BAA31673)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="V -> T (in Ref. 1; CAC35365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1158 AA; 130449 MW; CD032199E2E2868D CRC64;
MESGHLLWAL LFMQSLWPQL TDGATRVYYL GIRDVQWNYA PKGRNVITNQ PLDSDIVASS
FLKSDKNRIG GTYKKTIYKE YKDDSYTDEV AQPAWLGFLG PVLQAEVGDV ILIHLKNFAT
RPYTIHPHGV FYEKDSEGSL YPDGSSGPLK ADDSVPPGGS HIYNWTIPEG HAPTDADPAC
LTWIYHSHVD APRDIATGLI GPLITCKRGA LDGNSPPQRQ DVDHDFFLLF SVVDENLSWH
LNENIATYCS DPASVDKEDE TFQESNRMHA INGFVFGNLP ELNMCAQKRV AWHLFGMGNE
IDVHTAFFHG QMLTTRGHHT DVANIFPATF VTAEMVPWEP GTWLISCQVN SHFRDGMQAL
YKVKSCSMAP PVDLLTGKVR QYFIEAHEIQ WDYGPMGHDG STGKNLREPG SISDKFFQKS
SSRIGGTYWK VRYEAFQDET FQEKMHLEED RHLGILGPVI RAEVGDTIQV VFYNRASQPF
SMQPHGVFYE KDYEGTVYND GSSYPGLVAK PFEKVTYRWT VPPHAGPTAQ DPACLTWMYF
SAADPIRDTN SGLVGPLLVC RAGALGADGK QKGVDKEFFL LFTVLDENKS WYSNANQAAA
MLDFRLLSED IEGFQDSNRM HAINGFLFSN LPRLDMCKGD TVAWHLLGLG TETDVHGVMF
QGNTVQLQGM RKGAAMLFPH TFVMAIMQPD NLGTFEIYCQ AGSHREAGMR AIYNVSQCPG
HQATPRQRYQ AARIYYIMAE EVEWDYCPDR SWEREWHNQS EKDSYGYIFL SNKDGLLGSR
YKKAVFREYT DGTFRIPRPR TGPEEHLGIL GPLIKGEVGD ILTVVFKNNA SRPYSVHAHG
VLESTTVWPL AAEPGEVVTY QWNIPERSGP GPNDSACVSW IYYSAVDPIK DMYSGLVGPL
AICQKGILEP HGGRSDMDRE FALLFLIFDE NKSWYLEENV ATHGSQDPGS INLQDETFLE
SNKMHAINGK LYANLRGLTM YQGERVAWYM LAMGQDVDLH TIHFHAESFL YRNGENYRAD
VVDLFPGTFE VVEMVASNPG TWLMHCHVTD HVHAGMETLF TVFSRTEHLS PLTVITKETE
KAVPPRDIEE GNVKMLGMQI PIKNVEMLAS VLVAISVTLL LVVLALGGVV WYQHRQRKLR
RNRRSILDDS FKLLSFKQ
