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 27-MAR-2024, entry version 179. 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 Placenta RC {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=9; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 111. DR DIP; DIP-31098N; -. DR IntAct; Q9BST9; 19. 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; 9606-ENSP00000272430; -. DR PeptideAtlas; Q9BST9; -. DR ProteomicsDB; 43242; -. DR ProteomicsDB; 78923; -. [Q9BST9-1] DR ProteomicsDB; 78924; -. [Q9BST9-2] DR ProteomicsDB; 78925; -. [Q9BST9-3] DR Pumba; Q9BST9; -. DR Antibodypedia; 31499; 288 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 AGR; HGNC:10466; -. 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; CMTQPSA; -. DR OrthoDB; 5393023at2759; -. 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; 29 hits in 1157 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 159 other cell types or tissues. DR ExpressionAtlas; Q9BST9; baseline and differential. 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 CDD; cd13249; PH_rhotekin2; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR012966; AHD. DR InterPro; IPR011072; HR1_rho-bd. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR21538; ANILLIN/RHOTEKIN RTKN; 1. DR PANTHER; PTHR21538:SF19; RHOTEKIN; 1. DR Pfam; PF08174; Anillin; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00742; Hr1; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS51860; REM_1; 1. DR Genevisible; Q9BST9; HS. 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 //