INSRR_HUMAN
ID INSRR_HUMAN Reviewed; 1297 AA.
AC P14616; O60724; Q5VZS3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Insulin receptor-related protein;
DE Short=IRR;
DE EC=2.7.10.1;
DE AltName: Full=IR-related receptor;
DE Contains:
DE RecName: Full=Insulin receptor-related protein alpha chain;
DE Contains:
DE RecName: Full=Insulin receptor-related protein beta chain;
DE Flags: Precursor;
GN Name=INSRR; Synonyms=IRR;
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].
RC TISSUE=Kidney;
RX PubMed=10226785; DOI=10.1055/s-2007-978702;
RA Haenze J., Berthold A., Klammt J., Gallaher B., Siebler T., Kratzsch J.,
RA Elmlinger M., Kiess W.;
RT "Cloning and sequencing of the complete cDNA encoding the human insulin
RT receptor related receptor.";
RL Horm. Metab. Res. 31:77-79(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-1297.
RX PubMed=2768234; DOI=10.1016/s0021-9258(18)63737-8;
RA Shier P., Watt V.M.;
RT "Primary structure of a putative receptor for a ligand of the insulin
RT family.";
RL J. Biol. Chem. 264:14605-14608(1989).
RN [5]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-127; VAL-161; HIS-244; ARG-246;
RP GLN-278; CYS-554; LEU-928 AND GLU-1065.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [6]
RP FUNCTION, MUTAGENESIS OF 1145-TYR-TYR-1146, AND AUTOPHOSPHORYLATION.
RX PubMed=21641549; DOI=10.1016/j.cmet.2011.03.022;
RA Deyev I.E., Sohet F., Vassilenko K.P., Serova O.V., Popova N.V.,
RA Zozulya S.A., Burova E.B., Houillier P., Rzhevsky D.I., Berchatova A.A.,
RA Murashev A.N., Chugunov A.O., Efremov R.G., Nikol'sky N.N., Bertelli E.,
RA Eladari D., Petrenko A.G.;
RT "Insulin receptor-related receptor as an extracellular alkali sensor.";
RL Cell Metab. 13:679-689(2011).
CC -!- FUNCTION: Receptor with tyrosine-protein kinase activity. Functions as
CC a pH sensing receptor which is activated by increased extracellular pH.
CC Activates an intracellular signaling pathway that involves IRS1 and
CC AKT1/PKB. {ECO:0000269|PubMed:21641549}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Probable tetramer of 2 alpha and 2 beta chains linked by
CC disulfide bonds. The alpha chains contribute to the formation of the
CC ligand-binding domain, while the beta chains carry the kinase domain.
CC -!- INTERACTION:
CC P14616; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-6424336, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DOMAIN: The extracellular domain is required for sensing alterations in
CC external pH.
CC -!- PTM: Autophosphorylated on tyrosine residues between pH 7.9 and pH
CC 10.5.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AF064078; AAC17167.1; -; mRNA.
DR EMBL; AL158169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52903.1; -; Genomic_DNA.
DR EMBL; J05046; AAC31759.1; -; mRNA.
DR CCDS; CCDS1160.1; -.
DR PIR; B36502; B36502.
DR RefSeq; NP_055030.1; NM_014215.2.
DR AlphaFoldDB; P14616; -.
DR SASBDB; P14616; -.
DR SMR; P14616; -.
DR BioGRID; 109856; 60.
DR IntAct; P14616; 4.
DR MINT; P14616; -.
DR STRING; 9606.ENSP00000357178; -.
DR BindingDB; P14616; -.
DR ChEMBL; CHEMBL5483; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; P14616; -.
DR GuidetoPHARMACOLOGY; 1802; -.
DR GlyGen; P14616; 10 sites.
DR iPTMnet; P14616; -.
DR PhosphoSitePlus; P14616; -.
DR BioMuta; INSRR; -.
DR DMDM; 12644000; -.
DR EPD; P14616; -.
DR jPOST; P14616; -.
DR MassIVE; P14616; -.
DR MaxQB; P14616; -.
DR PaxDb; P14616; -.
DR PeptideAtlas; P14616; -.
DR PRIDE; P14616; -.
DR Antibodypedia; 20446; 393 antibodies from 34 providers.
DR DNASU; 3645; -.
DR Ensembl; ENST00000368195.4; ENSP00000357178.3; ENSG00000027644.5.
DR GeneID; 3645; -.
DR KEGG; hsa:3645; -.
DR MANE-Select; ENST00000368195.4; ENSP00000357178.3; NM_014215.3; NP_055030.1.
DR UCSC; uc010pht.3; human.
DR CTD; 3645; -.
DR DisGeNET; 3645; -.
DR GeneCards; INSRR; -.
DR HGNC; HGNC:6093; INSRR.
DR HPA; ENSG00000027644; Group enriched (brain, kidney).
DR MIM; 147671; gene.
DR neXtProt; NX_P14616; -.
DR OpenTargets; ENSG00000027644; -.
DR PharmGKB; PA29899; -.
DR VEuPathDB; HostDB:ENSG00000027644; -.
DR eggNOG; KOG1095; Eukaryota.
DR eggNOG; KOG4258; Eukaryota.
DR GeneTree; ENSGT00940000160437; -.
DR HOGENOM; CLU_000288_166_0_1; -.
DR InParanoid; P14616; -.
DR OMA; GTRGRWQ; -.
DR OrthoDB; 750182at2759; -.
DR PhylomeDB; P14616; -.
DR TreeFam; TF351636; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; P14616; -.
DR SignaLink; P14616; -.
DR BioGRID-ORCS; 3645; 12 hits in 1097 CRISPR screens.
DR GeneWiki; INSRR; -.
DR GenomeRNAi; 3645; -.
DR Pharos; P14616; Tchem.
DR PRO; PR:P14616; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P14616; protein.
DR Bgee; ENSG00000027644; Expressed in adult mammalian kidney and 60 other tissues.
DR Genevisible; P14616; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005899; C:insulin receptor complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005009; F:insulin receptor activity; IBA:GO_Central.
DR GO; GO:0043560; F:insulin receptor substrate binding; IBA:GO_Central.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
DR GO; GO:0071469; P:cellular response to alkaline pH; IDA:UniProtKB.
DR GO; GO:0030238; P:male sex determination; IEA:Ensembl.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00063; FN3; 3.
DR CDD; cd00064; FU; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.80.20.20; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR028792; INSRR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF338; PTHR24416:SF338; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PIRSF; PIRSF000620; Insulin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00261; FU; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; SSF49265; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1297
FT /note="Insulin receptor-related protein"
FT /id="PRO_0000016701"
FT CHAIN 27..742
FT /note="Insulin receptor-related protein alpha chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000016702"
FT CHAIN 747..1297
FT /note="Insulin receptor-related protein beta chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000016703"
FT TOPO_DOM 747..921
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 922..943
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 944..1297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 483..603
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 607..707
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 818..913
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 979..1254
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 666..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1115
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 985..993
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1013
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1145
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000305"
FT MOD_RES 1146
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000305"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 214..222
FT /evidence="ECO:0000250"
FT DISULFID 216..228
FT /evidence="ECO:0000250"
FT DISULFID 229..237
FT /evidence="ECO:0000250"
FT DISULFID 233..246
FT /evidence="ECO:0000250"
FT DISULFID 249..258
FT /evidence="ECO:0000250"
FT DISULFID 262..274
FT /evidence="ECO:0000250"
FT DISULFID 280..300
FT /evidence="ECO:0000250"
FT DISULFID 304..317
FT /evidence="ECO:0000250"
FT DISULFID 320..324
FT /evidence="ECO:0000250"
FT DISULFID 657..864
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255"
FT VARIANT 127
FT /note="A -> E (in dbSNP:rs55757706)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041434"
FT VARIANT 161
FT /note="A -> V (in dbSNP:rs55971900)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041435"
FT VARIANT 244
FT /note="R -> H (in dbSNP:rs55951840)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041436"
FT VARIANT 246
FT /note="C -> R (in dbSNP:rs56377825)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041437"
FT VARIANT 278
FT /note="E -> Q (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041438"
FT VARIANT 554
FT /note="R -> C (in dbSNP:rs56068937)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041439"
FT VARIANT 928
FT /note="P -> L (in dbSNP:rs56252149)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041440"
FT VARIANT 1065
FT /note="G -> E (in a glioblastoma multiforme sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041441"
FT MUTAGEN 1145..1146
FT /note="YY->FF: Abolishes autophosphorylation."
FT /evidence="ECO:0000269|PubMed:21641549"
SQ SEQUENCE 1297 AA; 143720 MW; BB22C7FF61E3065D CRC64;
MAVPSLWPWG ACLPVIFLSL GFGLDTVEVC PSLDIRSEVA ELRQLENCSV VEGHLQILLM
FTATGEDFRG LSFPRLTQVT DYLLLFRVYG LESLRDLFPN LAVIRGTRLF LGYALVIFEM
PHLRDVALPA LGAVLRGAVR VEKNQELCHL STIDWGLLQP APGANHIVGN KLGEECADVC
PGVLGAAGEP CAKTTFSGHT DYRCWTSSHC QRVCPCPHGM ACTARGECCH TECLGGCSQP
EDPRACVACR HLYFQGACLW ACPPGTYQYE SWRCVTAERC ASLHSVPGRA STFGIHQGSC
LAQCPSGFTR NSSSIFCHKC EGLCPKECKV GTKTIDSIQA AQDLVGCTHV EGSLILNLRQ
GYNLEPQLQH SLGLVETITG FLKIKHSFAL VSLGFFKNLK LIRGDAMVDG NYTLYVLDNQ
NLQQLGSWVA AGLTIPVGKI YFAFNPRLCL EHIYRLEEVT GTRGRQNKAE INPRTNGDRA
ACQTRTLRFV SNVTEADRIL LRWERYEPLE ARDLLSFIVY YKESPFQNAT EHVGPDACGT
QSWNLLDVEL PLSRTQEPGV TLASLKPWTQ YAVFVRAITL TTEEDSPHQG AQSPIVYLRT
LPAAPTVPQD VISTSNSSSH LLVRWKPPTQ RNGNLTYYLV LWQRLAEDGD LYLNDYCHRG
LRLPTSNNDP RFDGEDGDPE AEMESDCCPC QHPPPGQVLP PLEAQEASFQ KKFENFLHNA
ITIPISPWKV TSINKSPQRD SGRHRRAAGP LRLGGNSSDF EIQEDKVPRE RAVLSGLRHF
TEYRIDIHAC NHAAHTVGCS AATFVFARTM PHREADGIPG KVAWEASSKN SVLLRWLEPP
DPNGLILKYE IKYRRLGEEA TVLCVSRLRY AKFGGVHLAL LPPGNYSARV RATSLAGNGS
WTDSVAFYIL GPEEEDAGGL HVLLTATPVG LTLLIVLAAL GFFYGKKRNR TLYASVNPEY
FSASDMYVPD EWEVPREQIS IIRELGQGSF GMVYEGLARG LEAGEESTPV ALKTVNELAS
PRECIEFLKE ASVMKAFKCH HVVRLLGVVS QGQPTLVIME LMTRGDLKSH LRSLRPEAEN
NPGLPQPALG EMIQMAGEIA DGMAYLAANK FVHRDLAARN CMVSQDFTVK IGDFGMTRDV
YETDYYRKGG KGLLPVRWMA PESLKDGIFT THSDVWSFGV VLWEIVTLAE QPYQGLSNEQ
VLKFVMDGGV LEELEGCPLQ LQELMSRCWQ PNPRLRPSFT HILDSIQEEL RPSFRLLSFY
YSPECRGARG SLPTTDAEPD SSPTPRDCSP QNGGPGH
