HEPH_MOUSE
ID HEPH_MOUSE Reviewed; 1157 AA.
AC Q9Z0Z4; A2AI63; Q6ZQ65; Q80Y80; Q8C4S2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Hephaestin;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=Heph; Synonyms=Kiaa0698;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=9988272; DOI=10.1038/5979;
RA Vulpe C.D., Kuo Y.M., Murphy T.L., Cowley L., Askwith C., Libina N.,
RA Gitschier J., Anderson G.J.;
RT "Hephaestin, a ceruloplasmin homologue implicated in intestinal iron
RT transport, is defective in the sla mouse.";
RL Nat. Genet. 21:195-199(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-889.
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1144; SER-1149 AND SER-1154,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z0Z4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0Z4-2; Sequence=VSP_011628;
CC -!- DISEASE: Note=Defects in Heph are a cause of the sex-linked anemia
CC (sla) that is characterized by moderate to severe microcytic
CC hypochronic anemia.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98004.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF082567; AAD16035.1; -; mRNA.
DR EMBL; AK129194; BAC98004.1; ALT_INIT; mRNA.
DR EMBL; AL732365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466564; EDL14216.1; -; Genomic_DNA.
DR EMBL; BC048237; AAH48237.1; -; mRNA.
DR EMBL; BC054442; AAH54442.1; -; mRNA.
DR EMBL; AK081330; BAC38197.1; -; mRNA.
DR CCDS; CCDS30289.1; -. [Q9Z0Z4-1]
DR RefSeq; NP_001153099.1; NM_001159627.1. [Q9Z0Z4-1]
DR RefSeq; NP_001153100.1; NM_001159628.1. [Q9Z0Z4-2]
DR RefSeq; NP_034547.2; NM_010417.2. [Q9Z0Z4-1]
DR RefSeq; NP_851790.1; NM_181273.4.
DR AlphaFoldDB; Q9Z0Z4; -.
DR SMR; Q9Z0Z4; -.
DR BioGRID; 200273; 1.
DR STRING; 10090.ENSMUSP00000033553; -.
DR GlyGen; Q9Z0Z4; 8 sites.
DR iPTMnet; Q9Z0Z4; -.
DR PhosphoSitePlus; Q9Z0Z4; -.
DR jPOST; Q9Z0Z4; -.
DR MaxQB; Q9Z0Z4; -.
DR PaxDb; Q9Z0Z4; -.
DR PeptideAtlas; Q9Z0Z4; -.
DR PRIDE; Q9Z0Z4; -.
DR ProteomicsDB; 269698; -. [Q9Z0Z4-1]
DR ProteomicsDB; 269699; -. [Q9Z0Z4-2]
DR Antibodypedia; 13137; 154 antibodies from 24 providers.
DR DNASU; 15203; -.
DR Ensembl; ENSMUST00000033553; ENSMUSP00000033553; ENSMUSG00000031209. [Q9Z0Z4-1]
DR Ensembl; ENSMUST00000113838; ENSMUSP00000109469; ENSMUSG00000031209. [Q9Z0Z4-1]
DR GeneID; 15203; -.
DR KEGG; mmu:15203; -.
DR UCSC; uc009tuk.2; mouse. [Q9Z0Z4-1]
DR UCSC; uc009tul.2; mouse. [Q9Z0Z4-2]
DR CTD; 9843; -.
DR MGI; MGI:1332240; Heph.
DR VEuPathDB; HostDB:ENSMUSG00000031209; -.
DR eggNOG; KOG1263; Eukaryota.
DR GeneTree; ENSGT00940000158517; -.
DR HOGENOM; CLU_005569_0_0_1; -.
DR InParanoid; Q9Z0Z4; -.
DR OMA; YCQEGSH; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; Q9Z0Z4; -.
DR TreeFam; TF329807; -.
DR Reactome; R-MMU-425410; Metal ion SLC transporters.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR BioGRID-ORCS; 15203; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Heph; mouse.
DR PRO; PR:Q9Z0Z4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9Z0Z4; protein.
DR Bgee; ENSMUSG00000031209; Expressed in ileum and 217 other tissues.
DR ExpressionAtlas; Q9Z0Z4; baseline and differential.
DR Genevisible; Q9Z0Z4; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; ISO:MGI.
DR GO; GO:0008198; F:ferrous iron binding; ISO:MGI.
DR GO; GO:0004322; F:ferroxidase activity; ISO:MGI.
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; ISO:MGI.
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 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; 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 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1157
FT /note="Hephaestin"
FT /id="PRO_0000002916"
FT TOPO_DOM 19..1109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1110..1130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1131..1157
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..559
FT /note="Plastocyanin-like 3"
FT DOMAIN 569..717
FT /note="Plastocyanin-like 4"
FT DOMAIN 730..902
FT /note="Plastocyanin-like 5"
FT DOMAIN 910..1086
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 655
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 698
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 703
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 708
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 999
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 1002
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 1004
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 1044
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="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1046
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 1050
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 1055
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 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 930
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 533..559
FT /evidence="ECO:0000255"
FT DISULFID 636..717
FT /evidence="ECO:0000255"
FT DISULFID 876..902
FT /evidence="ECO:0000255"
FT VAR_SEQ 1081
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011628"
FT CONFLICT 501..542
FT /note="Missing (in Ref. 6; BAC38197)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="N -> S (in Ref. 2; BAC98004 and 5; AAH48237/
FT AAH54442)"
FT /evidence="ECO:0000305"
FT CONFLICT 856..889
FT /note="VLTYQWNIPERSGPGPSDSACVSWIYYSAVDPIK -> LEHLMKRQRLYNPF
FT TLVFWFIPFNILHSWAGQVT (in Ref. 6; BAC38197)"
FT /evidence="ECO:0000305"
FT CONFLICT 1068
FT /note="F -> Y (in Ref. 1; AAD16035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1157 AA; 129666 MW; 41055EC4DA11DC12 CRC64;
MKAGHLLWAL LLMHSLWSIP TDGAIRNYYL GIQDMQWNYA PKGRNVITNQ TLNNDTVASS
FLKSGKNRIG SSYKKTVYKE YSDGTYTEEI AKPAWLGFLG PLLQAEVGDV ILIHLKNFAS
RPYTIHPHGV FYEKDSEGSL YPDGSSGYLK ADDSVPPGGS HVYNWSIPES HAPTEADPAC
LTWIYHSHVD APRDIATGLI GPLITCKRGT LDGNSPPQRK DVDHNFFLLF SVIDENLSWH
LDDNIATYCS DPASVDKEDG AFQDSNRMHA INGFVFGNLP ELSMCAQKHV AWHLFGMGNE
IDVHTAFFHG QMLSIRGHHT DVANIFPATF VTAEMVPQKS GTWLISCEVN SHLRSGMQAF
YKVDSCSMDP PVDQLTGKVR QYFIQAHEIQ WDYGPIGYDG RTGKSLREPG SGPDKYFQKS
SSRIGGTYWK VRYEAFQDET FQERVHQEEE THLGILGPVI RAEVGDTIQV VFYNRASQPF
SIQPHGVFYE KNSEGTVYND GTSHPKVAKS FEKVTYYWTV PPHAGPTAQD PACLTWMYFS
AADPTRDTNS GLVGPLLVCK AGALGADGKQ KGVDKEFFLL FTVFDENESW YNNANQAAGM
LDSRLLSEDV EGFQDSNRMH AINGFLFSNL PRLDMCKGDT VAWHLLGLGT ETDVHGVMFE
GNTVQLQGMR KGAVMLFPHT FVTAIMQPDN PGIFEIYCQA GSHREEGMQA IYNVSQCSSH
QDSPRQHYQA SRVYYIMAEE IEWDYCPDRS WELEWHNTSE KDSYGHVFLS NKDGLLGSKY
KKAVFREYTD GTFRIPRPRS GPEEHLGILG PLIRGEVGDI LTVVFKNKAS RPYSIHAHGV
LESNTGGPQA AEPGEVLTYQ WNIPERSGPG PSDSACVSWI YYSAVDPIKD MYSGLVGPLV
ICRNGILEPN GGRNDMDREF ALLFLIFDEN QSWYLKENIA TYGPQESSHV NLKDATFLES
NKMHAINGKL YANLRGLTVY QGERVAWYML AMGQDTDIHT VHFHAESFLY QNGQSYRADV
VDLFPGTFEV VEMVASNPGT WLMHCHVTDH VHAGMETIFT VLSHEEHFST MTTITKEIGK
AVILRDIGGD NVKMLGMNIP IKDVEILSSA LIAICVLLLL IALALGGVVW YQHRQRKLRR
NRRSILDDSF KLLSLKQ
