RADX_HUMAN
ID RADX_HUMAN Reviewed; 855 AA.
AC Q6NSI4; H7BY89; Q4G0L7; Q5JQS1; Q5JRF9; Q6PHY5; Q6PII9; Q6PJU8; Q9H7W5;
AC Q9NWA6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=RPA-related protein RADX {ECO:0000305};
DE AltName: Full=RPA-related and RAD51-antagonist, X-chromosome {ECO:0000303|PubMed:28735897};
GN Name=RADX {ECO:0000303|PubMed:28735897, ECO:0000312|HGNC:HGNC:25486};
GN Synonyms=CXorf57 {ECO:0000312|HGNC:HGNC:25486};
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-593.
RC TISSUE=Brain, Choriocarcinoma, and Leiomyosarcoma;
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]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-240; ARG-248;
RP 252-LYS--LYS-256; TRP-279; LYS-304; ARG-310 AND GLU-327.
RX PubMed=28735897; DOI=10.1016/j.molcel.2017.06.023;
RA Dungrawala H., Bhat K.P., Le Meur R., Chazin W.J., Ding X., Sharan S.K.,
RA Wessel S.R., Sathe A.A., Zhao R., Cortez D.;
RT "RADX promotes genome stability and modulates chemosensitivity by
RT regulating RAD51 at replication forks.";
RL Mol. Cell 67:374-386(2017).
CC -!- FUNCTION: Single-stranded DNA-binding protein recruited to replication
CC forks to maintain genome stability (PubMed:28735897). Prevents fork
CC collapse by antagonizing the accumulation of RAD51 at forks to ensure
CC the proper balance of fork remodeling and protection without
CC interfering with the capacity of cells to complete homologous
CC recombination of double-strand breaks (PubMed:28735897).
CC {ECO:0000269|PubMed:28735897}.
CC -!- INTERACTION:
CC Q6NSI4; P40692: MLH1; NbExp=9; IntAct=EBI-8634209, EBI-744248;
CC Q6NSI4; Q8IVD9: NUDCD3; NbExp=2; IntAct=EBI-8634209, EBI-744342;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:28735897}.
CC Note=Recruited to replication forks. {ECO:0000269|PubMed:28735897}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6NSI4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NSI4-2; Sequence=VSP_021182, VSP_021183;
CC Name=3;
CC IsoId=Q6NSI4-3; Sequence=VSP_044983, VSP_044984;
CC Name=4;
CC IsoId=Q6NSI4-4; Sequence=VSP_044984;
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DR EMBL; AK001040; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK024253; BAB14859.1; -; mRNA.
DR EMBL; AL590808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471120; EAX02740.1; -; Genomic_DNA.
DR EMBL; BC011483; AAH11483.1; -; mRNA.
DR EMBL; BC033709; AAH33709.1; -; mRNA.
DR EMBL; BC054032; AAH54032.1; ALT_SEQ; mRNA.
DR EMBL; BC070110; AAH70110.1; -; mRNA.
DR CCDS; CCDS14519.1; -. [Q6NSI4-1]
DR CCDS; CCDS55470.1; -. [Q6NSI4-4]
DR RefSeq; NP_001171711.1; NM_001184782.1. [Q6NSI4-4]
DR RefSeq; NP_060485.4; NM_018015.5. [Q6NSI4-1]
DR AlphaFoldDB; Q6NSI4; -.
DR SMR; Q6NSI4; -.
DR BioGRID; 120400; 36.
DR IntAct; Q6NSI4; 13.
DR MINT; Q6NSI4; -.
DR STRING; 9606.ENSP00000361628; -.
DR iPTMnet; Q6NSI4; -.
DR MetOSite; Q6NSI4; -.
DR PhosphoSitePlus; Q6NSI4; -.
DR BioMuta; CXorf57; -.
DR DMDM; 117949773; -.
DR EPD; Q6NSI4; -.
DR MassIVE; Q6NSI4; -.
DR MaxQB; Q6NSI4; -.
DR PaxDb; Q6NSI4; -.
DR PeptideAtlas; Q6NSI4; -.
DR PRIDE; Q6NSI4; -.
DR ProteomicsDB; 43542; -.
DR ProteomicsDB; 66630; -. [Q6NSI4-1]
DR ProteomicsDB; 66631; -. [Q6NSI4-2]
DR Antibodypedia; 348; 23 antibodies from 10 providers.
DR DNASU; 55086; -.
DR Ensembl; ENST00000372544.6; ENSP00000361623.2; ENSG00000147231.14. [Q6NSI4-4]
DR Ensembl; ENST00000372548.9; ENSP00000361628.4; ENSG00000147231.14. [Q6NSI4-1]
DR Ensembl; ENST00000461251.5; ENSP00000432238.1; ENSG00000147231.14. [Q6NSI4-2]
DR GeneID; 55086; -.
DR KEGG; hsa:55086; -.
DR MANE-Select; ENST00000372548.9; ENSP00000361628.4; NM_018015.6; NP_060485.4.
DR UCSC; uc004emi.5; human. [Q6NSI4-1]
DR CTD; 55086; -.
DR GeneCards; RADX; -.
DR HGNC; HGNC:25486; RADX.
DR HPA; ENSG00000147231; Tissue enhanced (brain, pituitary gland).
DR neXtProt; NX_Q6NSI4; -.
DR OpenTargets; ENSG00000147231; -.
DR PharmGKB; PA145149058; -.
DR VEuPathDB; HostDB:ENSG00000147231; -.
DR eggNOG; ENOG502QSE7; Eukaryota.
DR GeneTree; ENSGT00390000005094; -.
DR HOGENOM; CLU_016770_0_0_1; -.
DR InParanoid; Q6NSI4; -.
DR OMA; KYLHHST; -.
DR OrthoDB; 218331at2759; -.
DR PhylomeDB; Q6NSI4; -.
DR TreeFam; TF331019; -.
DR PathwayCommons; Q6NSI4; -.
DR SignaLink; Q6NSI4; -.
DR BioGRID-ORCS; 55086; 16 hits in 686 CRISPR screens.
DR ChiTaRS; CXorf57; human.
DR GenomeRNAi; 55086; -.
DR Pharos; Q6NSI4; Tdark.
DR PRO; PR:Q6NSI4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q6NSI4; protein.
DR Bgee; ENSG00000147231; Expressed in pituitary gland and 121 other tissues.
DR ExpressionAtlas; Q6NSI4; baseline and differential.
DR Genevisible; Q6NSI4; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005657; C:replication fork; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR040893; RADX.
DR PANTHER; PTHR14944; PTHR14944; 1.
DR Pfam; PF17659; DUF5521; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; DNA-binding; Reference proteome.
FT CHAIN 1..855
FT /note="RPA-related protein RADX"
FT /id="PRO_0000254127"
FT DNA_BIND 228..331
FT /note="OB"
FT /evidence="ECO:0000305|PubMed:28735897"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..225
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044983"
FT VAR_SEQ 482..578
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044984"
FT VAR_SEQ 525..567
FT /note="VESLLTAISEVRKEIEDLQYREQKRIAIQGIITAIKYIPHSSA -> GTNVI
FT ASPSKYVYILYVWLMLFQLVIFILFFYGSDLKFSNIHR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021182"
FT VAR_SEQ 568..855
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021183"
FT VARIANT 593
FT /note="I -> M (in dbSNP:rs5962707)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028816"
FT MUTAGEN 240
FT /note="R->E: Decreased binding to single-stranded DNA; when
FT associated with E-248; 252-E--E-256; A-279; E-304; E-310
FT and A-327."
FT /evidence="ECO:0000269|PubMed:28735897"
FT MUTAGEN 248
FT /note="R->E: Decreased binding to single-stranded DNA; when
FT associated with E-240; 252-E--E-256; A-279; E-304; E-310
FT and A-327."
FT /evidence="ECO:0000269|PubMed:28735897"
FT MUTAGEN 252..256
FT /note="KPDKK->EPDEE: Decreased binding to single-stranded
FT DNA; when associated with E-240; E-248; A-279; E-304; E-310
FT and A-327."
FT /evidence="ECO:0000269|PubMed:28735897"
FT MUTAGEN 279
FT /note="W->A: Decreased binding to single-stranded DNA; when
FT associated with E-240; E-248; 252-E--E-256; E-304; E-310
FT and A-327."
FT /evidence="ECO:0000269|PubMed:28735897"
FT MUTAGEN 304
FT /note="K->E: Decreased binding to single-stranded DNA; when
FT associated with E-240; E-248; 252-E--E-256; A-279; E-310
FT and A-327."
FT /evidence="ECO:0000269|PubMed:28735897"
FT MUTAGEN 310
FT /note="R->E: Decreased binding to single-stranded DNA; when
FT associated with E-240; E-248; 252-E--E-256; A-279; E-304
FT and A-327."
FT /evidence="ECO:0000269|PubMed:28735897"
FT MUTAGEN 327
FT /note="E->A: Decreased binding to single-stranded DNA; when
FT associated with E-240; E-248; 252-E--E-256; A-279; E-304
FT and E-310."
FT /evidence="ECO:0000269|PubMed:28735897"
FT CONFLICT 29
FT /note="V -> A (in Ref. 1; AK001040)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="V -> L (in Ref. 4; AAH70110)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="K -> E (in Ref. 4; AAH11483)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="E -> K (in Ref. 4; AAH54032)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="K -> N (in Ref. 1; BAB14859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 855 AA; 97554 MW; 31EE2E17E7D9BF47 CRC64;
MSGESGQPEA GPSHAGLDWP NPERNRAGVP GGVIRRAGSQ GPRSWIQKVL EQIMDSPRQC
VTPSEVVPVT VLAVQRYLLE DEPRDTVPKP PLYCYDVTIS DGVYQEKCYL DPSLNSLVYQ
NILKVGIQMR ISRVSCLYNE KRIGQGILCI DNVHCGETSD SISLETPFRN RAHQEKPERP
LRGGKSHYLA LWNNEDPYGD IWLTDKQPEE HNFSDTKIIS LSHLEMTWTN RRNFPALLVR
ILHKSKLRYY GKPDKKMIEP YQTFLEVADS SGTVSVIMWN ALCPEWYKSL RVGLVLLLQD
YSVKKSYPFR IQPVPVDPQI KLISTMEICL NLRDPPTNII IIPEKQVKPE WRLPKLNHRF
TTRSELDDMP ENCICDVIGL LVFVGRVQRS KKKENREDFW SYRWIHIADG TSEQPFIVEL
FSTSQPEIFE NIYPMAYFVC TQLKVVRNDN QVPKLLYLTT TNESGVFITG HRGQPYTYDA
KVKNFIQWIR TKSDSGEQKN MVIGGYYPYP PVPETFSKYS SSIKVESLLT AISEVRKEIE
DLQYREQKRI AIQGIITAIK YIPHSSATES ASASETLRNA NRPSTSQAAR VEIQERNGKR
HQDDEPVNSQ YFQTTSTNLS LSNKIRILQG PHANPVAVPQ PGASVQTKGI KPGMPSIFNR
RANINANLQG KARKTISDRW ESQLWREKKF GLIDHLHYSR VYPESIPRKF MFEHRKFLSD
QYNSQPAKYV PPEGRPPKLD DFKSARSLGH FEVTILGLNH EIAIDVAFLP MYCPEDIRTS
QIDTLLTSMN YSCAYPQDTT GNDRLPGPRA VAGDIIKAAT ELDRVHIVGI LDICNLGNNK
VEVYLHKIYS PENTS
