RFXK_HUMAN
ID RFXK_HUMAN Reviewed; 260 AA.
AC O14593; O95839; Q24JQ1; Q6FGA8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=DNA-binding protein RFXANK;
DE AltName: Full=Ankyrin repeat family A protein 1;
DE AltName: Full=Regulatory factor X subunit B;
DE Short=RFX-B;
DE AltName: Full=Regulatory factor X-associated ankyrin-containing protein;
GN Name=RFXANK; Synonyms=ANKRA1, RFXB;
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), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, AND INVOLVEMENT IN BLS2.
RC TISSUE=B-cell;
RX PubMed=9806546; DOI=10.1038/3081;
RA Masternak K., Barras E., Zufferey M., Conrad B., Corthals G., Aebersold R.,
RA Sanchez J.-C., Hochstrasser D.F., Mach B., Reith W.;
RT "A gene encoding a novel RFX-associated transactivator is mutated in the
RT majority of MHC class II deficiency patients.";
RL Nat. Genet. 20:273-277(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 79-95;
RP 180-198; 100-210 AND 238-248, FUNCTION (ISOFORMS 1 AND 2), AND INVOLVEMENT
RP IN BLS2.
RC TISSUE=Lymphoblast;
RX PubMed=10072068; DOI=10.1016/s1074-7613(00)80016-3;
RA Nagarajan U.M., Louis-Plence P., DeSandro A., Nilsen R., Bushey A.,
RA Boss J.M.;
RT "RFX-B is the gene responsible for the most common cause of the bare
RT lymphocyte syndrome, an MHC class II immunodeficiency.";
RL Immunity 10:153-162(1999).
RN [3]
RP ERRATUM OF PUBMED:10072068.
RA Nagarajan U.M., Louis-Plence P., DeSandro A., Nilsen R., Bushey A.,
RA Boss J.M.;
RL Immunity 10:399-399(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [9]
RP SUBUNIT.
RX PubMed=20732328; DOI=10.1016/j.jmb.2010.08.025;
RA Laird K.M., Briggs L.L., Boss J.M., Summers M.F., Garvie C.W.;
RT "Solution structure of the heterotrimeric complex between the interaction
RT domains of RFX5 and RFXAP from the RFX gene regulatory complex.";
RL J. Mol. Biol. 403:40-51(2010).
RN [10]
RP INTERACTION WITH RFX7.
RX PubMed=25752541; DOI=10.1016/j.str.2015.02.001;
RA Nie J., Xu C., Jin J., Aka J.A., Tempel W., Nguyen V., You L., Weist R.,
RA Min J., Pawson T., Yang X.J.;
RT "Ankyrin repeats of ANKRA2 recognize a PxLPxL motif on the 3M syndrome
RT protein CCDC8.";
RL Structure 23:700-712(2015).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 90-260 IN COMPLEX WITH RFX5
RP PEPTIDE, CHARACTERIZATION OF VARIANT BLS2 PRO-195, AND MUTAGENESIS OF
RP ASP-121 AND TYR-224.
RX PubMed=22649097; DOI=10.1126/scisignal.2002979;
RA Xu C., Jin J., Bian C., Lam R., Tian R., Weist R., You L., Nie J.,
RA Bochkarev A., Tempel W., Tan C.S., Wasney G.A., Vedadi M., Gish G.D.,
RA Arrowsmith C.H., Pawson T., Yang X.J., Min J.;
RT "Sequence-specific recognition of a PxLPxI/L motif by an ankyrin repeat
RT tumbler lock.";
RL Sci. Signal. 5:RA39-RA39(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 90-260 IN COMPLEX WITH RFX7.
RA Tempel W., Xu C., Dong A., Li Y., Bountra C., Arrowsmith C.H.,
RA Edwards A.M., Min J.;
RT "Crystal structure of RFXANK ankyrin repeats in complex with RFX7.";
RL Submitted (JUN-2014) to the PDB data bank.
RN [13]
RP VARIANT BLS2 PRO-195, AND FUNCTION.
RX PubMed=10725724; DOI=10.4049/jimmunol.164.7.3666;
RA Nagarajan U.M., Peijnenburg A., Gobin S.J., Boss J.M., van den Elsen P.J.;
RT "Novel mutations within the RFX-B gene and partial rescue of MHC and
RT related genes through exogenous class II transactivator in RFX-B-deficient
RT cells.";
RL J. Immunol. 164:3666-3674(2000).
CC -!- FUNCTION: Activates transcription from class II MHC promoters.
CC Activation requires the activity of the MHC class II
CC transactivator/CIITA. May regulate other genes in the cell. RFX binds
CC the X1 box of MHC-II promoters (PubMed:9806546, PubMed:10072068,
CC PubMed:10725724). May also potentiate the activation of RAF1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Z205,
CC ECO:0000269|PubMed:10072068, ECO:0000269|PubMed:10725724,
CC ECO:0000269|PubMed:9806546}.
CC -!- FUNCTION: Isoform 2 is not involved in the positive regulation of MHC
CC class II genes. {ECO:0000269|PubMed:10072068}.
CC -!- SUBUNIT: Forms homodimers (By similarity). The RFX heterotetrameric
CC complex consists of 2 molecules of RFX5 and one each of RFXAP and RFX-
CC B/RFXANK; with each subunit representing a separate complementation
CC group. Interacts (via ankyrin repeats) with RFX5 (via PxLPxI/L motif);
CC the interaction is direct. RFX forms cooperative DNA binding complexes
CC with X2BP and CBF/NF-Y. RFX associates with CIITA to form an active
CC transcriptional complex (PubMed:20732328, PubMed:22649097). Interacts
CC with RAF1 (By similarity). Interacts (via ankyrin repeats) with RFX7
CC (via PxLPxI/L motif) (PubMed:25752541). {ECO:0000250|UniProtKB:Q9Z205,
CC ECO:0000269|PubMed:20732328, ECO:0000269|PubMed:22649097,
CC ECO:0000269|PubMed:25752541, ECO:0000312|PDB:6MEW}.
CC -!- INTERACTION:
CC O14593; P48382: RFX5; NbExp=8; IntAct=EBI-1057665, EBI-923266;
CC O14593; Q2KHR2: RFX7; NbExp=2; IntAct=EBI-1057665, EBI-1222187;
CC O14593; O00287: RFXAP; NbExp=3; IntAct=EBI-1057665, EBI-3929296;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z205}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Z205}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=O14593-1; Sequence=Displayed;
CC Name=2; Synonyms=RFX-B-delta5;
CC IsoId=O14593-2; Sequence=VSP_000283, VSP_000284, VSP_054618;
CC Name=3;
CC IsoId=O14593-3; Sequence=VSP_000284;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: Interacts with RAF1 via its C-terminal ankyrin repeat domain.
CC The same domain also mediates its homodimerization (By similarity). The
CC third ankyrin repeat is required for association with the two other RFX
CC subunits; RFX5 and RFXAP. The three central ANK repeats mediate binding
CC to the PxLPxI/L motif of RFX5 (PubMed:20732328, PubMed:22649097).
CC {ECO:0000250|UniProtKB:Q9Z205, ECO:0000269|PubMed:20732328,
CC ECO:0000269|PubMed:22649097}.
CC -!- PTM: Phosphorylated by RAF1. {ECO:0000250|UniProtKB:Q9Z205}.
CC -!- DISEASE: Bare lymphocyte syndrome 2 (BLS2) [MIM:209920]: A severe
CC combined immunodeficiency disease with early onset. It is characterized
CC by a profound defect in constitutive and interferon-gamma induced MHC
CC II expression, absence of cellular and humoral T-cell response to
CC antigen challenge, hypogammaglobulinemia and impaired antibody
CC production. The consequence include extreme susceptibility to viral,
CC bacterial and fungal infections. {ECO:0000269|PubMed:10072068,
CC ECO:0000269|PubMed:10725724, ECO:0000269|PubMed:22649097,
CC ECO:0000269|PubMed:9806546}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=RFXANKbase; Note=RFXANK mutation db;
CC URL="http://structure.bmc.lu.se/idbase/RFXANKbase/";
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DR EMBL; AF094760; AAC69883.1; -; mRNA.
DR EMBL; AF105427; AAD17972.1; -; mRNA.
DR EMBL; AF105428; AAD17973.1; -; mRNA.
DR EMBL; AF077196; AAD26991.1; -; mRNA.
DR EMBL; CR542199; CAG46996.1; -; mRNA.
DR EMBL; AC002126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC003110; AAB86654.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84795.1; -; Genomic_DNA.
DR EMBL; BC114558; AAI14559.1; -; mRNA.
DR EMBL; BC114563; AAI14564.1; -; mRNA.
DR CCDS; CCDS12395.1; -. [O14593-1]
DR CCDS; CCDS62611.1; -. [O14593-3]
DR RefSeq; NP_001265656.1; NM_001278727.1. [O14593-3]
DR RefSeq; NP_001265657.1; NM_001278728.1.
DR RefSeq; NP_003712.1; NM_003721.3. [O14593-1]
DR RefSeq; NP_604389.1; NM_134440.2.
DR RefSeq; XP_005260191.1; XM_005260134.4. [O14593-1]
DR RefSeq; XP_005260192.1; XM_005260135.3. [O14593-1]
DR RefSeq; XP_016882904.1; XM_017027415.1.
DR RefSeq; XP_016882905.1; XM_017027416.1.
DR PDB; 3UXG; X-ray; 1.85 A; A=90-260.
DR PDB; 3V30; X-ray; 1.57 A; A=90-260.
DR PDB; 6MEW; X-ray; 1.78 A; A/C=90-260.
DR PDBsum; 3UXG; -.
DR PDBsum; 3V30; -.
DR PDBsum; 6MEW; -.
DR AlphaFoldDB; O14593; -.
DR SMR; O14593; -.
DR BioGRID; 114180; 164.
DR ComplexPortal; CPX-6461; RFX gene regulatory complex.
DR CORUM; O14593; -.
DR ELM; O14593; -.
DR IntAct; O14593; 25.
DR STRING; 9606.ENSP00000305071; -.
DR iPTMnet; O14593; -.
DR PhosphoSitePlus; O14593; -.
DR BioMuta; RFXANK; -.
DR EPD; O14593; -.
DR jPOST; O14593; -.
DR MassIVE; O14593; -.
DR MaxQB; O14593; -.
DR PaxDb; O14593; -.
DR PeptideAtlas; O14593; -.
DR PRIDE; O14593; -.
DR ProteomicsDB; 48101; -. [O14593-1]
DR ProteomicsDB; 48102; -. [O14593-2]
DR ProteomicsDB; 61266; -.
DR Antibodypedia; 15290; 356 antibodies from 21 providers.
DR DNASU; 8625; -.
DR Ensembl; ENST00000303088.9; ENSP00000305071.2; ENSG00000064490.14. [O14593-1]
DR Ensembl; ENST00000407360.7; ENSP00000384572.3; ENSG00000064490.14. [O14593-1]
DR Ensembl; ENST00000456252.7; ENSP00000409138.2; ENSG00000064490.14. [O14593-3]
DR GeneID; 8625; -.
DR KEGG; hsa:8625; -.
DR MANE-Select; ENST00000303088.9; ENSP00000305071.2; NM_003721.4; NP_003712.1.
DR UCSC; uc002nls.4; human. [O14593-1]
DR CTD; 8625; -.
DR DisGeNET; 8625; -.
DR GeneCards; RFXANK; -.
DR HGNC; HGNC:9987; RFXANK.
DR HPA; ENSG00000064490; Low tissue specificity.
DR MalaCards; RFXANK; -.
DR MIM; 209920; phenotype.
DR MIM; 603200; gene.
DR neXtProt; NX_O14593; -.
DR OpenTargets; ENSG00000064490; -.
DR Orphanet; 572; Immunodeficiency by defective expression of MHC class II.
DR PharmGKB; PA34357; -.
DR VEuPathDB; HostDB:ENSG00000064490; -.
DR eggNOG; KOG0502; Eukaryota.
DR GeneTree; ENSGT00940000160753; -.
DR HOGENOM; CLU_000134_23_0_1; -.
DR InParanoid; O14593; -.
DR OMA; ADSGHMD; -.
DR PhylomeDB; O14593; -.
DR TreeFam; TF333112; -.
DR PathwayCommons; O14593; -.
DR SignaLink; O14593; -.
DR SIGNOR; O14593; -.
DR BioGRID-ORCS; 8625; 25 hits in 1083 CRISPR screens.
DR ChiTaRS; RFXANK; human.
DR GeneWiki; RFXANK; -.
DR GenomeRNAi; 8625; -.
DR Pharos; O14593; Tbio.
DR PRO; PR:O14593; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O14593; protein.
DR Bgee; ENSG00000064490; Expressed in lower esophagus mucosa and 187 other tissues.
DR ExpressionAtlas; O14593; baseline and differential.
DR Genevisible; O14593; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ARUK-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR IDEAL; IID00427; -.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017362; DNA-bd_RFXANK.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF13857; Ank_5; 1.
DR PIRSF; PIRSF038034; DNA-binding_RFXANK; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; ANK repeat; Cytoplasm;
KW Direct protein sequencing; Disease variant; DNA-binding; Nucleus;
KW Reference proteome; Repeat; SCID; Transcription; Transcription regulation.
FT CHAIN 1..260
FT /note="DNA-binding protein RFXANK"
FT /id="PRO_0000067049"
FT REPEAT 89..118
FT /note="ANK 1"
FT REPEAT 123..152
FT /note="ANK 2"
FT REPEAT 156..185
FT /note="ANK 3"
FT REPEAT 189..218
FT /note="ANK 4"
FT REPEAT 222..251
FT /note="ANK 5"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10072068"
FT /id="VSP_000283"
FT VAR_SEQ 91..113
FT /note="SLSIHQLAAQGELDQLKEHLRKG -> C (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10072068,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000284"
FT VAR_SEQ 159..172
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10072068"
FT /id="VSP_054618"
FT VARIANT 48
FT /note="E -> D (in dbSNP:rs34282046)"
FT /id="VAR_048311"
FT VARIANT 195
FT /note="L -> P (in BLS2; loss of expression;
FT dbSNP:rs751386365)"
FT /evidence="ECO:0000269|PubMed:10725724,
FT ECO:0000269|PubMed:22649097"
FT /id="VAR_009941"
FT VARIANT 251
FT /note="Q -> E (in dbSNP:rs1802498)"
FT /id="VAR_014472"
FT MUTAGEN 121
FT /note="D->V: Loss of expression."
FT /evidence="ECO:0000269|PubMed:22649097"
FT MUTAGEN 224
FT /note="Y->A: Loss of interaction with RFX5."
FT /evidence="ECO:0000269|PubMed:22649097"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:3V30"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:3V30"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:3V30"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:3V30"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:3V30"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:3V30"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:3V30"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3V30"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:3V30"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:3V30"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:3V30"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:3V30"
SQ SEQUENCE 260 AA; 28102 MW; 6280B490F54816D2 CRC64;
MELTQPAEDL IQTQQTPASE LGDPEDPGEE AADGSDTVVL SLFPCTPEPV NPEPDASVSS
PQAGSSLKHS TTLTNRQRGN EVSALPATLD SLSIHQLAAQ GELDQLKEHL RKGDNLVNKP
DERGFTPLIW ASAFGEIETV RFLLEWGADP HILAKERESA LSLASTGGYT DIVGLLLERD
VDINIYDWNG GTPLLYAVRG NHVKCVEALL ARGADLTTEA DSGYTPMDLA VALGYRKVQQ
VIENHILKLF QSNLVPADPE
