RTKN_HUMAN
ID RTKN_HUMAN Reviewed; 563 AA.
AC Q9BST9; H7BXD4; Q8WVN1; Q96PT6; Q9HB05;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Rhotekin;
GN Name=RTKN {ECO:0000312|HGNC:HGNC:10466}; Synonyms=RTKN1;
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] {ECO:0000305, ECO:0000312|EMBL:AAL16767.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Kidney {ECO:0000269|PubMed:10873388};
RX PubMed=10873388; DOI=10.1006/geno.2000.6212;
RA Fu Q., Yu L., Liu Q., Zhang J., Zhang H., Zhao S.;
RT "Molecular cloning, expression characterization, and mapping of a novel
RT putative inhibitor of rho GTPase activity, RTKN, to D2S145-D2S286.";
RL Genomics 66:328-332(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAG01181.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH RHOA AND
RP TAX1BP3, AND MUTAGENESIS OF 561-SER--VAL-563.
RC TISSUE=Leukocyte {ECO:0000269|PubMed:10940294};
RX PubMed=10940294; DOI=10.1074/jbc.m000465200;
RA Reynaud C., Fabre S., Jalinot P.;
RT "The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is
RT involved in Rho signaling to the serum response element.";
RL J. Biol. Chem. 275:33962-33968(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH04558.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH17727.1}, and
RC Placenta {ECO:0000312|EMBL:AAH04558.2};
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 [5] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15480428; DOI=10.1038/sj.onc.1208106;
RA Liu C.-A., Wang M.-J., Chi C.-W., Wu C.-W., Chen J.-Y.;
RT "Rho/Rhotekin-mediated NF-kappaB activation confers resistance to
RT apoptosis.";
RL Oncogene 23:8731-8742(2004).
RN [6] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH SEPT9.
RX PubMed=16007136; DOI=10.1038/sj.onc.1208862;
RA Ito H., Iwamoto I., Morishita R., Nozawa Y., Narumiya S., Asano T.,
RA Nagata K.;
RT "Possible role of Rho/Rhotekin signaling in mammalian septin
RT organization.";
RL Oncogene 24:7064-7072(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-543, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520 AND SER-529, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-106, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-14, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Mediates Rho signaling to activate NF-kappa-B and may confer
CC increased resistance to apoptosis to cells in gastric tumorigenesis.
CC May play a novel role in the organization of septin structures.
CC {ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:15480428,
CC ECO:0000269|PubMed:16007136}.
CC -!- SUBUNIT: Interacts via its C-terminal region with the TAX1BP3 PDZ
CC domain. This interaction facilitates Rho-mediated activation of the c-
CC Fos serum response element (SRE). Interacts with SEPT9. Specifically
CC binds to GTP-bound RHOA, RHOB and RHOC and inhibits their GTPase
CC activity. {ECO:0000250|UniProtKB:Q8C6B2, ECO:0000269|PubMed:10940294,
CC ECO:0000269|PubMed:16007136}.
CC -!- INTERACTION:
CC Q9BST9; P61586: RHOA; NbExp=6; IntAct=EBI-446694, EBI-446668;
CC Q9BST9; O60504: SORBS3; NbExp=3; IntAct=EBI-446694, EBI-741237;
CC Q9BST9; O60504-2: SORBS3; NbExp=3; IntAct=EBI-446694, EBI-1222956;
CC Q9BST9; Q9QUI0: Rhoa; Xeno; NbExp=2; IntAct=EBI-446694, EBI-643583;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:10873388};
CC IsoId=Q9BST9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q9BST9-2; Sequence=VSP_052004;
CC Name=3 {ECO:0000269|PubMed:10940294};
CC IsoId=Q9BST9-3; Sequence=VSP_052005;
CC -!- TISSUE SPECIFICITY: Highly expressed in prostate, moderately in kidney,
CC heart, brain, spleen, testis, placenta, small intestine, pancreas,
CC skeletal muscle and peripheral blood leukocytes, and weakly in ovary,
CC colon and thymus. Weakly expressed in all normal cell lines tested.
CC Overexpressed in various cancer cell lines.
CC {ECO:0000269|PubMed:10873388, ECO:0000269|PubMed:15480428}.
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence.
CC {ECO:0000269|PubMed:10940294}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL16767.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF049227; AAL16767.1; ALT_FRAME; mRNA.
DR EMBL; AF290512; AAG01181.1; -; mRNA.
DR EMBL; AC005041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004558; AAH04558.2; -; mRNA.
DR EMBL; BC017727; AAH17727.1; -; mRNA.
DR CCDS; CCDS1941.1; -. [Q9BST9-2]
DR CCDS; CCDS33226.1; -. [Q9BST9-1]
DR CCDS; CCDS42699.1; -. [Q9BST9-3]
DR RefSeq; NP_001015055.1; NM_001015055.1. [Q9BST9-1]
DR RefSeq; NP_001015056.1; NM_001015056.1. [Q9BST9-3]
DR RefSeq; NP_149035.1; NM_033046.2. [Q9BST9-2]
DR RefSeq; XP_016860124.1; XM_017004635.1. [Q9BST9-2]
DR AlphaFoldDB; Q9BST9; -.
DR SMR; Q9BST9; -.
DR BioGRID; 112156; 101.
DR DIP; DIP-31098N; -.
DR IntAct; Q9BST9; 15.
DR MINT; Q9BST9; -.
DR STRING; 9606.ENSP00000272430; -.
DR iPTMnet; Q9BST9; -.
DR PhosphoSitePlus; Q9BST9; -.
DR BioMuta; RTKN; -.
DR DMDM; 74733052; -.
DR EPD; Q9BST9; -.
DR jPOST; Q9BST9; -.
DR MassIVE; Q9BST9; -.
DR MaxQB; Q9BST9; -.
DR PaxDb; Q9BST9; -.
DR PeptideAtlas; Q9BST9; -.
DR PRIDE; Q9BST9; -.
DR ProteomicsDB; 43242; -.
DR ProteomicsDB; 78923; -. [Q9BST9-1]
DR ProteomicsDB; 78924; -. [Q9BST9-2]
DR ProteomicsDB; 78925; -. [Q9BST9-3]
DR Antibodypedia; 31499; 255 antibodies from 31 providers.
DR DNASU; 6242; -.
DR Ensembl; ENST00000233330.6; ENSP00000233330.6; ENSG00000114993.17. [Q9BST9-3]
DR Ensembl; ENST00000272430.10; ENSP00000272430.5; ENSG00000114993.17. [Q9BST9-1]
DR Ensembl; ENST00000305557.9; ENSP00000305298.5; ENSG00000114993.17. [Q9BST9-2]
DR GeneID; 6242; -.
DR KEGG; hsa:6242; -.
DR MANE-Select; ENST00000272430.10; ENSP00000272430.5; NM_001015055.2; NP_001015055.1.
DR UCSC; uc002slc.4; human. [Q9BST9-1]
DR CTD; 6242; -.
DR DisGeNET; 6242; -.
DR GeneCards; RTKN; -.
DR HGNC; HGNC:10466; RTKN.
DR HPA; ENSG00000114993; Tissue enhanced (brain, liver).
DR MIM; 602288; gene.
DR neXtProt; NX_Q9BST9; -.
DR OpenTargets; ENSG00000114993; -.
DR PharmGKB; PA34879; -.
DR VEuPathDB; HostDB:ENSG00000114993; -.
DR eggNOG; ENOG502QRWR; Eukaryota.
DR GeneTree; ENSGT00940000158491; -.
DR HOGENOM; CLU_025066_2_0_1; -.
DR InParanoid; Q9BST9; -.
DR OMA; KGLPRTW; -.
DR OrthoDB; 497196at2759; -.
DR PhylomeDB; Q9BST9; -.
DR TreeFam; TF331476; -.
DR PathwayCommons; Q9BST9; -.
DR Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR SignaLink; Q9BST9; -.
DR SIGNOR; Q9BST9; -.
DR BioGRID-ORCS; 6242; 28 hits in 1079 CRISPR screens.
DR ChiTaRS; RTKN; human.
DR GeneWiki; RTKN; -.
DR GenomeRNAi; 6242; -.
DR Pharos; Q9BST9; Tbio.
DR PRO; PR:Q9BST9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BST9; protein.
DR Bgee; ENSG00000114993; Expressed in C1 segment of cervical spinal cord and 157 other tissues.
DR ExpressionAtlas; Q9BST9; baseline and differential.
DR Genevisible; Q9BST9; HS.
DR GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005095; F:GTPase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
DR GO; GO:0031106; P:septin ring organization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR012966; AHD.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR030471; RTKN.
DR PANTHER; PTHR21538:SF19; PTHR21538:SF19; 1.
DR Pfam; PF08174; Anillin; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00742; Hr1; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51860; REM_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Coiled coil; GTP-binding; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..563
FT /note="Rhotekin"
FT /id="PRO_0000233940"
FT DOMAIN 17..98
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 309..416
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 96..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 230
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8C6B2"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10940294"
FT /id="VSP_052005"
FT VAR_SEQ 1..36
FT /note="MFSRNHRSRVTVARGSALEMEFKRGRFRLSLFSDLP -> MQDRLHILEDLN
FT MLYIRQMALSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052004"
FT MUTAGEN 561..563
FT /note="SPV->APA: Impairs interaction with TAX1BP3."
FT /evidence="ECO:0000269|PubMed:10940294"
FT CONFLICT 18..19
FT /note="LE -> WR (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="A -> P (in Ref. 1; AAL16767)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="A -> P (in Ref. 1; AAL16767)"
FT /evidence="ECO:0000305"
FT CONFLICT 65..66
FT /note="RE -> AR (in Ref. 1; AAL16767)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="S -> N (in Ref. 1; AAL16767)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="A -> P (in Ref. 1; AAL16767)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="Q -> H (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="E -> D (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="S -> N (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 202..205
FT /note="EEGA -> KKRG (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="R -> K (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="R -> L (in Ref. 1; AAL16767)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="G -> S (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="L -> F (in Ref. 1; AAL16767)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..366
FT /note="RV -> PI (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="D -> E (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..406
FT /note="REALQS -> LETLQN (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 437..439
FT /note="RKP -> PKT (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="A -> V (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="P -> T (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="L -> F (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="P -> L (in Ref. 2; AAG01181)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 563 AA; 62667 MW; B3C64CB737E88501 CRC64;
MFSRNHRSRV TVARGSALEM EFKRGRFRLS LFSDLPEDTE LQRKLDHEIR MREGACKLLA
ACSQREQALE ATKSLLVCNS RILSYMGELQ RRKEAQVLGK TSRRPSDSGP PAERSPCRGR
VCISDLRIPL MWKDTEYFKN KGDLHRWAVF LLLQLGEHIQ DTEMILVDRT LTDISFQSNV
LFAEAGPDFE LRLELYGACV EEEGALTGGP KRLATKLSSS LGRSSGRRVR ASLDSAGGSG
SSPILLPTPV VGGPRYHLLA HTTLTLAAVQ DGFRTHDLTL ASHEENPAWL PLYGSVCCRL
AAQPLCMTQP TASGTLRVQQ AGEMQNWAQV HGVLKGTNLF CYRQPEDADT GEEPLLTIAV
NKETRVRAGE LDQALGRPFT LSISNQYGDD EVTHTLQTES REALQSWMEA LWQLFFDMSQ
WKQCCDEIMK IETPAPRKPP QALAKQGSLY HEMAIEPLDD IAAVTDILTQ REGARLETPP
PWLAMFTDQP ALPNPCSPAS VAPAPDWTHP LPWGRPRTFS LDAVPPDHSP RARSVAPLPP
QRSPRTRGLC SKGQPRTWLQ SPV
