RTEL1_HUMAN
ID RTEL1_HUMAN Reviewed; 1219 AA.
AC Q9NZ71; A2A397; A2A398; B4DRM5; B4DYM3; B4E3N6; E1P5J4; E1P5J5; Q5JTV3;
AC Q5JTV4; Q9BW37; Q9H402; Q9H4X6; Q9NX25; Q9NZ73; Q9UPR4; Q9Y4R6;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Regulator of telomere elongation helicase 1 {ECO:0000255|HAMAP-Rule:MF_03065};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03065};
DE AltName: Full=Novel helicase-like;
GN Name=RTEL1 {ECO:0000255|HAMAP-Rule:MF_03065};
GN Synonyms=C20orf41, KIAA1088, NHL;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
RP AMPLIFICATION IN GASTRIC TUMORS.
RX PubMed=10655513; DOI=10.1073/pnas.97.3.1230;
RA Bai C., Connolly B., Metzker M.L., Hilliard C.A., Liu X., Sandig V.,
RA Soderman A., Galloway S.M., Liu Q., Austin C.P., Caskey C.T.;
RT "Overexpression of M68/DcR3 in human gastrointestinal tract tumors
RT independent of gene amplification and its location in a four-gene
RT cluster.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1230-1235(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-1042.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP SEQUENCE REVISION TO 291-292.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5; 7; 8 AND 9), AND
RP VARIANTS THR-929 AND HIS-1042.
RC TISSUE=Colon carcinoma, Teratocarcinoma, Testis, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORMS 2; 5 AND 6).
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 708-1219 (ISOFORM 4).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF LYS-48.
RX PubMed=18957201; DOI=10.1016/j.cell.2008.08.016;
RA Barber L.J., Youds J.L., Ward J.D., McIlwraith M.J., O'Neil N.J.,
RA Petalcorin M.I.R., Martin J.S., Collis S.J., Cantor S.B., Auclair M.,
RA Tissenbaum H., West S.C., Rose A.M., Boulton S.J.;
RT "RTEL1 maintains genomic stability by suppressing homologous
RT recombination.";
RL Cell 135:261-271(2008).
RN [10]
RP INTERACTION WITH MMS19.
RX PubMed=22678361; DOI=10.1126/science.1219664;
RA Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M., Boulton S.J.;
RT "MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism.";
RL Science 337:243-245(2012).
RN [11]
RP FUNCTION, VARIANTS DKCB5 LYS-251; ILE-492; ARG-710; VAL-739; GLU-897;
RP TRP-957 AND LEU-964, VARIANT DKCB5 HIS-509 (ISOFORM 5), AND VARIANT DKCB5
RP HIS-1264 (ISOFORMS 1 AND 6).
RX PubMed=23453664; DOI=10.1016/j.ajhg.2013.02.001;
RA Walne A.J., Vulliamy T., Kirwan M., Plagnol V., Dokal I.;
RT "Constitutional mutations in RTEL1 cause severe dyskeratosis congenita.";
RL Am. J. Hum. Genet. 92:448-453(2013).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MMS19.
RX PubMed=23585563; DOI=10.1074/jbc.m112.416602;
RA Seki M., Takeda Y., Iwai K., Tanaka K.;
RT "IOP1 protein is an external component of the human cytosolic iron-sulfur
RT cluster assembly (CIA) machinery and functions in the MMS19 protein-
RT dependent CIA pathway.";
RL J. Biol. Chem. 288:16680-16689(2013).
RN [13]
RP INTERACTION WITH TERF1, AND VARIANT DKCB5 ILE-492.
RX PubMed=23959892; DOI=10.1073/pnas.1300600110;
RA Deng Z., Glousker G., Molczan A., Fox A.J., Lamm N., Dheekollu J.,
RA Weizman O.E., Schertzer M., Wang Z., Vladimirova O., Schug J., Aker M.,
RA Londono-Vallejo A., Kaestner K.H., Lieberman P.M., Tzfati Y.;
RT "Inherited mutations in the helicase RTEL1 cause telomere dysfunction and
RT Hoyeraal-Hreidarsson syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E3408-E3416(2013).
RN [14]
RP INVOLVEMENT IN PFBMFT3, AND VARIANTS PFBMFT3 LEU-484; LEU-647 AND PRO-1124.
RX PubMed=25848748; DOI=10.1038/ng.3278;
RA Stuart B.D., Choi J., Zaidi S., Xing C., Holohan B., Chen R., Choi M.,
RA Dharwadkar P., Torres F., Girod C.E., Weissler J., Fitzgerald J.,
RA Kershaw C., Klesney-Tait J., Mageto Y., Shay J.W., Ji W., Bilguvar K.,
RA Mane S., Lifton R.P., Garcia C.K.;
RT "Exome sequencing links mutations in PARN and RTEL1 with familial pulmonary
RT fibrosis and telomere shortening.";
RL Nat. Genet. 47:512-517(2015).
RN [15]
RP VARIANT DKCB5 ASP-591, VARIANT DKCA4 THR-621, AND VARIANTS SER-124;
RP GLN-684; PRO-829; ASP-849; THR-929; HIS-1034; HIS-1042 AND THR-1059.
RX PubMed=23329068; DOI=10.1007/s00439-013-1265-8;
RA Ballew B.J., Yeager M., Jacobs K., Giri N., Boland J., Burdett L.,
RA Alter B.P., Savage S.A.;
RT "Germline mutations of regulator of telomere elongation helicase 1, RTEL1,
RT in dyskeratosis congenita.";
RL Hum. Genet. 132:473-480(2013).
RN [16]
RP VARIANTS DKCB5 MET-699 AND MET-745, VARIANT DKCB5 ARG-489 (ISOFORM 5), AND
RP VARIANT DKCB5 ARG-1244 (ISOFORMS 1 AND 6).
RX PubMed=23591994; DOI=10.1093/hmg/ddt178;
RA Le Guen T., Jullien L., Touzot F., Schertzer M., Gaillard L.,
RA Perderiset M., Carpentier W., Nitschke P., Picard C., Couillault G.,
RA Soulier J., Fischer A., Callebaut I., Jabado N., Londono-Vallejo A.,
RA de Villartay J.P., Revy P.;
RT "Human RTEL1 deficiency causes Hoyeraal-Hreidarsson syndrome with short
RT telomeres and genome instability.";
RL Hum. Mol. Genet. 22:3239-3249(2013).
RN [17]
RP VARIANTS DKCB5 HIS-509 (ISOFORM 5) AND HIS-1264 (ISOFORMS 1 AND 6),
RP FUNCTION, AND CHARACTERIZATION OF VARIANTS DKCB5 HIS-509 (ISOFORM 5) AND
RP HIS-1264 (ISOFORMS 1 AND 6).
RX PubMed=24009516; DOI=10.1371/journal.pgen.1003695;
RA Ballew B.J., Joseph V., De S., Sarek G., Vannier J.B., Stracker T.,
RA Schrader K.A., Small T.N., O'Reilly R., Manschreck C.,
RA Harlan Fleischut M.M., Zhang L., Sullivan J., Stratton K., Yeager M.,
RA Jacobs K., Giri N., Alter B.P., Boland J., Burdett L., Offit K.,
RA Boulton S.J., Savage S.A., Petrini J.H.;
RT "A recessive founder mutation in regulator of telomere elongation helicase
RT 1, RTEL1, underlies severe immunodeficiency and features of Hoyeraal
RT Hreidarsson syndrome.";
RL PLoS Genet. 9:E1003695-E1003695(2013).
CC -!- FUNCTION: ATP-dependent DNA helicase implicated in telomere-length
CC regulation, DNA repair and the maintenance of genomic stability. Acts
CC as an anti-recombinase to counteract toxic recombination and limit
CC crossover during meiosis. Regulates meiotic recombination and crossover
CC homeostasis by physically dissociating strand invasion events and
CC thereby promotes noncrossover repair by meiotic synthesis dependent
CC strand annealing (SDSA) as well as disassembly of D loop recombination
CC intermediates. Also disassembles T loops and prevents telomere
CC fragility by counteracting telomeric G4-DNA structures, which together
CC ensure the dynamics and stability of the telomere. {ECO:0000255|HAMAP-
CC Rule:MF_03065, ECO:0000269|PubMed:18957201,
CC ECO:0000269|PubMed:23453664, ECO:0000269|PubMed:24009516}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03065};
CC -!- SUBUNIT: Interacts with TERF1. Interacts (via PIP-box) with PCNA; the
CC interaction is direct and essential for suppressing telomere fragility.
CC Interacts with MMS19; the interaction mediates the association of RTEL1
CC with the cytosolic iron-sulfur protein assembly (CIA) complex.
CC {ECO:0000255|HAMAP-Rule:MF_03065, ECO:0000269|PubMed:22678361,
CC ECO:0000269|PubMed:23585563, ECO:0000269|PubMed:23959892}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065,
CC ECO:0000269|PubMed:23585563}. Note=Colocalizes with PCNA within the
CC replication foci in S-phase cells. {ECO:0000255|HAMAP-Rule:MF_03065}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Additional isoforms seem to exist.;
CC Name=2;
CC IsoId=Q9NZ71-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9NZ71-2; Sequence=VSP_036940;
CC Name=4;
CC IsoId=Q9NZ71-4; Sequence=VSP_007076, VSP_007077;
CC Name=5;
CC IsoId=Q9NZ71-5; Sequence=VSP_017093, VSP_017094;
CC Name=6;
CC IsoId=Q9NZ71-6; Sequence=VSP_017094;
CC Name=7;
CC IsoId=Q9NZ71-7; Sequence=VSP_036938;
CC Name=8;
CC IsoId=Q9NZ71-8; Sequence=VSP_036939;
CC Name=9;
CC IsoId=Q9NZ71-9; Sequence=VSP_036937;
CC -!- DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates the
CC interaction with PCNA and localization to replication foci.
CC {ECO:0000255|HAMAP-Rule:MF_03065}.
CC -!- DISEASE: Dyskeratosis congenita, autosomal recessive, 5 (DKCB5)
CC [MIM:615190]: A form of dyskeratosis congenita, a rare multisystem
CC disorder caused by defective telomere maintenance. It is characterized
CC by progressive bone marrow failure, and the clinical triad of
CC reticulated skin hyperpigmentation, nail dystrophy, and mucosal
CC leukoplakia. Common but variable features include premature graying,
CC aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and
CC liver fibrosis among others. Early mortality is often associated with
CC bone marrow failure, infections, fatal pulmonary complications, or
CC malignancy. DKCB5 is characterized by onset of bone marrow failure and
CC immunodeficiency in early childhood. Most patients also have growth and
CC developmental delay and cerebellar hypoplasia, consistent with a
CC clinical diagnosis of Hoyeraal-Hreidarsson syndrome.
CC {ECO:0000269|PubMed:23329068, ECO:0000269|PubMed:23453664,
CC ECO:0000269|PubMed:23591994, ECO:0000269|PubMed:23959892,
CC ECO:0000269|PubMed:24009516}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. RTEL1 mutations have also
CC been found in patients with a dyskeratosis congenita-like phenotype
CC consisting of one feature of dyskeratosis congenita and short
CC telomeres, in the absence of the typical DKC diagnostic triad
CC (PubMed:23329068). {ECO:0000269|PubMed:23329068}.
CC -!- DISEASE: Dyskeratosis congenita, autosomal dominant, 4 (DKCA4)
CC [MIM:615190]: A rare multisystem disorder caused by defective telomere
CC maintenance. It is characterized by progressive bone marrow failure,
CC and the clinical triad of reticulated skin hyperpigmentation, nail
CC dystrophy, and mucosal leukoplakia. Common but variable features
CC include premature graying, aplastic anemia, low platelets,
CC osteoporosis, pulmonary fibrosis, and liver fibrosis among others.
CC Early mortality is often associated with bone marrow failure,
CC infections, fatal pulmonary complications, or malignancy.
CC {ECO:0000269|PubMed:23329068}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Pulmonary fibrosis, and/or bone marrow failure, telomere-
CC related, 3 (PFBMFT3) [MIM:616373]: An autosomal dominant disease
CC associated with shortened telomeres. Pulmonary fibrosis is the most
CC common manifestation. Other manifestations include aplastic anemia due
CC to bone marrow failure, hepatic fibrosis, and increased cancer risk,
CC particularly myelodysplastic syndrome and acute myeloid leukemia.
CC Phenotype, age at onset, and severity are determined by telomere
CC length. {ECO:0000269|PubMed:25848748}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Amplified in gastric tumors.
CC -!- MISCELLANEOUS: [Isoform 1]: Variant in position: 1264:R->H (in DKCB5),
CC abolishes activity. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03065}.
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DR EMBL; AF217795; AAF33687.1; -; mRNA.
DR EMBL; AF217796; AAF35243.1; -; Genomic_DNA.
DR EMBL; AB029011; BAA83040.3; -; mRNA.
DR EMBL; AK000485; BAA91197.1; -; mRNA.
DR EMBL; AK302508; BAG63785.1; -; mRNA.
DR EMBL; AK299332; BAG61337.1; -; mRNA.
DR EMBL; AK304798; BAG65548.1; -; mRNA.
DR EMBL; AL353715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75238.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75239.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75240.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75241.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75245.1; -; Genomic_DNA.
DR EMBL; AL080127; CAB45725.1; -; mRNA.
DR CCDS; CCDS13530.3; -. [Q9NZ71-7]
DR CCDS; CCDS13531.1; -. [Q9NZ71-1]
DR CCDS; CCDS63331.1; -. [Q9NZ71-6]
DR CCDS; CCDS74751.1; -. [Q9NZ71-9]
DR PIR; T12516; T12516.
DR PIR; T45294; T45294.
DR RefSeq; NP_001269938.1; NM_001283009.1. [Q9NZ71-6]
DR RefSeq; NP_001269939.1; NM_001283010.1. [Q9NZ71-9]
DR RefSeq; NP_057518.1; NM_016434.3. [Q9NZ71-1]
DR RefSeq; NP_116575.3; NM_032957.4. [Q9NZ71-7]
DR AlphaFoldDB; Q9NZ71; -.
DR SMR; Q9NZ71; -.
DR BioGRID; 119711; 101.
DR IntAct; Q9NZ71; 30.
DR STRING; 9606.ENSP00000353332; -.
DR iPTMnet; Q9NZ71; -.
DR PhosphoSitePlus; Q9NZ71; -.
DR BioMuta; RTEL1; -.
DR DMDM; 229462743; -.
DR EPD; Q9NZ71; -.
DR jPOST; Q9NZ71; -.
DR MassIVE; Q9NZ71; -.
DR MaxQB; Q9NZ71; -.
DR PaxDb; Q9NZ71; -.
DR PeptideAtlas; Q9NZ71; -.
DR PRIDE; Q9NZ71; -.
DR ProteomicsDB; 83330; -. [Q9NZ71-1]
DR ProteomicsDB; 83331; -. [Q9NZ71-2]
DR ProteomicsDB; 83332; -. [Q9NZ71-4]
DR ProteomicsDB; 83333; -. [Q9NZ71-5]
DR ProteomicsDB; 83334; -. [Q9NZ71-6]
DR ProteomicsDB; 83335; -. [Q9NZ71-7]
DR ProteomicsDB; 83336; -. [Q9NZ71-8]
DR ProteomicsDB; 83337; -. [Q9NZ71-9]
DR Antibodypedia; 58405; 154 antibodies from 25 providers.
DR DNASU; 51750; -.
DR Ensembl; ENST00000318100.9; ENSP00000322287.5; ENSG00000258366.11. [Q9NZ71-9]
DR Ensembl; ENST00000360203.11; ENSP00000353332.5; ENSG00000258366.11. [Q9NZ71-6]
DR Ensembl; ENST00000370018.7; ENSP00000359035.3; ENSG00000258366.11. [Q9NZ71-1]
DR Ensembl; ENST00000482936.6; ENSP00000457868.2; ENSG00000258366.11. [Q9NZ71-8]
DR Ensembl; ENST00000508582.7; ENSP00000424307.2; ENSG00000258366.11. [Q9NZ71-7]
DR GeneID; 51750; -.
DR KEGG; hsa:51750; -.
DR MANE-Select; ENST00000360203.11; ENSP00000353332.5; NM_001283009.2; NP_001269938.1. [Q9NZ71-6]
DR UCSC; uc002yfu.3; human. [Q9NZ71-1]
DR CTD; 51750; -.
DR DisGeNET; 51750; -.
DR GeneCards; RTEL1; -.
DR GeneReviews; RTEL1; -.
DR HGNC; HGNC:15888; RTEL1.
DR HPA; ENSG00000258366; Low tissue specificity.
DR MalaCards; RTEL1; -.
DR MIM; 608833; gene.
DR MIM; 615190; phenotype.
DR MIM; 616373; phenotype.
DR neXtProt; NX_Q9NZ71; -.
DR OpenTargets; ENSG00000258366; -.
DR Orphanet; 1775; Dyskeratosis congenita.
DR Orphanet; 3322; Hoyeraal-Hreidarsson syndrome.
DR Orphanet; 2032; Idiopathic pulmonary fibrosis.
DR PharmGKB; PA134915625; -.
DR VEuPathDB; HostDB:ENSG00000258366; -.
DR eggNOG; KOG1132; Eukaryota.
DR GeneTree; ENSGT00950000182970; -.
DR HOGENOM; CLU_006515_4_0_1; -.
DR InParanoid; Q9NZ71; -.
DR OMA; CSAMHEY; -.
DR OrthoDB; 1282784at2759; -.
DR PhylomeDB; Q9NZ71; -.
DR PathwayCommons; Q9NZ71; -.
DR Reactome; R-HSA-171319; Telomere Extension By Telomerase.
DR Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
DR Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
DR SignaLink; Q9NZ71; -.
DR BioGRID-ORCS; 51750; 428 hits in 1082 CRISPR screens.
DR GenomeRNAi; 51750; -.
DR Pharos; Q9NZ71; Tbio.
DR PRO; PR:Q9NZ71; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NZ71; protein.
DR Bgee; ENSG00000258366; Expressed in sural nerve and 93 other tissues.
DR ExpressionAtlas; Q9NZ71; baseline and differential.
DR Genevisible; Q9NZ71; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IMP:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IMP:UniProtKB.
DR GO; GO:0070182; F:DNA polymerase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:BHF-UCL.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; ISS:BHF-UCL.
DR GO; GO:0045910; P:negative regulation of DNA recombination; ISS:BHF-UCL.
DR GO; GO:1904430; P:negative regulation of t-circle formation; IMP:BHF-UCL.
DR GO; GO:1904506; P:negative regulation of telomere maintenance in response to DNA damage; ISS:BHF-UCL.
DR GO; GO:1904355; P:positive regulation of telomere capping; IMP:BHF-UCL.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISS:BHF-UCL.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; IMP:BHF-UCL.
DR GO; GO:1904535; P:positive regulation of telomeric loop disassembly; ISS:BHF-UCL.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; ISS:BHF-UCL.
DR GO; GO:0000732; P:strand displacement; ISS:BHF-UCL.
DR GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
DR GO; GO:0043247; P:telomere maintenance in response to DNA damage; ISS:BHF-UCL.
DR GO; GO:0090657; P:telomeric loop disassembly; IMP:BHF-UCL.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_03065; RTEL1; 1.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR010614; DEAD_2.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR InterPro; IPR030845; RTEL1.
DR PANTHER; PTHR11472; PTHR11472; 2.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Alternative splicing; ATP-binding; Disease variant; DNA damage;
KW DNA repair; DNA-binding; Dyskeratosis congenita; Helicase; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1219
FT /note="Regulator of telomere elongation helicase 1"
FT /id="PRO_0000101985"
FT DOMAIN 7..296
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 287..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 151..167
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOTIF 250..253
FT /note="DEAH box"
FT MOTIF 871..877
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOTIF 1178..1185
FT /note="PIP-box"
FT COMPBIAS 848..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 163
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 207
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT VAR_SEQ 1..755
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017093"
FT VAR_SEQ 1..223
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036937"
FT VAR_SEQ 131
FT /note="Y -> YRSRCRATLWVLETAPPRPTVLSPT (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036938"
FT VAR_SEQ 998..1219
FT /note="GRTAPDPKLTVSTAAAQQLDPQEHLNQGRPHLSPRPPPTGDPGSQPQWGSGV
FT PRAGKQGQHAVSAYLADARRALGSAGCSQLLAALTAYKQDDDLDKVLAVLAALTTAKPE
FT DFPLLHRFSMFVRPHHKQRFSQTCTDLTGRPYPGMEPPGPQEERLAVPPVLTHRAPQPG
FT PSRSEKTGKTQSKISSFLRQRPAGTVGAGGEDAGPSQSSGPPHGPAASEWGL -> ERR
FT RIPS (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036939"
FT VAR_SEQ 999..1023
FT /note="RTAPDPKLTVSTAAAQQLDPQEHLN -> NFPDALDQLCGSTSLHQEERRRI
FT PS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_007076"
FT VAR_SEQ 1024..1219
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_007077"
FT VAR_SEQ 1219
FT /note="L -> EPHGRDIAGQQATGAPGGPLSAGCVCQGCGAEDVVPFQCPACDFQRC
FT QACWQRHLQASRMCPACHTASRKQSVMQVFWPEPHKDHEGAGGARPVAAVPGVGAACPA
FT AGAGCTRSGRNTHLPLAGRRDRGAAGVCPVPPRHLCAAAVPPRQPHDVWPVSTAPLHAV
FT LELPGALPLLQRPLRGA (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:10655513"
FT /id="VSP_036940"
FT VAR_SEQ 1219
FT /note="L -> EPHGRDIAGQQATGAPGGPLSAGCVCQGCGAEDVVPFQCPACDFQRC
FT QACWQRHLQASRMCPACHTASRKQSVMQVFWPEPQ (in isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017094"
FT VARIANT 124
FT /note="N -> S (in dbSNP:rs3848668)"
FT /evidence="ECO:0000269|PubMed:23329068"
FT /id="VAR_054970"
FT VARIANT 251
FT /note="E -> K (in DKCB5; severe form consistent with
FT Hoyeraal-Hreidarsson syndrome; dbSNP:rs398123019)"
FT /evidence="ECO:0000269|PubMed:23453664"
FT /id="VAR_069714"
FT VARIANT 484
FT /note="P -> L (in PFBMFT3; dbSNP:rs786205700)"
FT /evidence="ECO:0000269|PubMed:25848748"
FT /id="VAR_073795"
FT VARIANT 492
FT /note="M -> I (in DKCB5; severe form consistent with
FT Hoyeraal-Hreidarsson syndrome; dbSNP:rs370343781)"
FT /evidence="ECO:0000269|PubMed:23453664,
FT ECO:0000269|PubMed:23959892"
FT /id="VAR_069715"
FT VARIANT 591
FT /note="E -> D (in DKCB5; severe form consistent with
FT Hoyeraal-Hreidarsson syndrome; dbSNP:rs398123051)"
FT /evidence="ECO:0000269|PubMed:23329068"
FT /id="VAR_069716"
FT VARIANT 621
FT /note="A -> T (in DKCA4; dbSNP:rs398123052)"
FT /evidence="ECO:0000269|PubMed:23329068"
FT /id="VAR_069717"
FT VARIANT 647
FT /note="P -> L (in PFBMFT3; dbSNP:rs1177091623)"
FT /evidence="ECO:0000269|PubMed:25848748"
FT /id="VAR_073796"
FT VARIANT 684
FT /note="R -> Q (in dbSNP:rs35640778)"
FT /evidence="ECO:0000269|PubMed:23329068"
FT /id="VAR_069718"
FT VARIANT 699
FT /note="I -> M (in DKCB5; severe form consistent with
FT Hoyeraal-Hreidarsson syndrome; dbSNP:rs398123048)"
FT /evidence="ECO:0000269|PubMed:23591994"
FT /id="VAR_069719"
FT VARIANT 710
FT /note="L -> R (in DKCB5; severe form consistent with
FT Hoyeraal-Hreidarsson syndrome)"
FT /evidence="ECO:0000269|PubMed:23453664"
FT /id="VAR_069720"
FT VARIANT 739
FT /note="G -> V (in DKCB5; severe form consistent with
FT Hoyeraal-Hreidarsson syndrome; dbSNP:rs398123016)"
FT /evidence="ECO:0000269|PubMed:23453664"
FT /id="VAR_069721"
FT VARIANT 745
FT /note="V -> M (in DKCB5; severe form consistent with
FT Hoyeraal-Hreidarsson syndrome; dbSNP:rs398123049)"
FT /evidence="ECO:0000269|PubMed:23591994"
FT /id="VAR_069722"
FT VARIANT 829
FT /note="Q -> P"
FT /evidence="ECO:0000269|PubMed:23329068"
FT /id="VAR_069723"
FT VARIANT 849
FT /note="G -> D (in dbSNP:rs190887884)"
FT /evidence="ECO:0000269|PubMed:23329068"
FT /id="VAR_069724"
FT VARIANT 897
FT /note="K -> E (in DKCB5; severe form consistent with
FT Hoyeraal-Hreidarsson syndrome)"
FT /evidence="ECO:0000269|PubMed:23453664"
FT /id="VAR_069725"
FT VARIANT 929
FT /note="A -> T (in dbSNP:rs61736615)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:23329068"
FT /id="VAR_069726"
FT VARIANT 957
FT /note="R -> W (in DKCB5; severe form consistent with
FT Hoyeraal-Hreidarsson syndrome; dbSNP:rs398123018)"
FT /evidence="ECO:0000269|PubMed:23453664"
FT /id="VAR_069727"
FT VARIANT 964
FT /note="F -> L (in DKCB5; severe form consistent with
FT Hoyeraal-Hreidarsson syndrome; dbSNP:rs1470145133)"
FT /evidence="ECO:0000269|PubMed:23453664"
FT /id="VAR_069728"
FT VARIANT 1034
FT /note="P -> H (in dbSNP:rs115610405)"
FT /evidence="ECO:0000269|PubMed:23329068"
FT /id="VAR_069729"
FT VARIANT 1042
FT /note="Q -> H (in dbSNP:rs3208008)"
FT /evidence="ECO:0000269|PubMed:10470851,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:23329068"
FT /id="VAR_054971"
FT VARIANT 1059
FT /note="A -> T (in dbSNP:rs115303435)"
FT /evidence="ECO:0000269|PubMed:23329068"
FT /id="VAR_069730"
FT VARIANT 1124
FT /note="H -> P (in PFBMFT3; dbSNP:rs786205702)"
FT /evidence="ECO:0000269|PubMed:25848748"
FT /id="VAR_073797"
FT MUTAGEN 48
FT /note="K->R: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:18957201"
FT CONFLICT 41
FT /note="E -> G (in Ref. 5; BAG63785)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="K -> R (in Ref. 5; BAG61337)"
FT /evidence="ECO:0000305"
FT CONFLICT 845
FT /note="A -> V (in Ref. 5; BAG63785)"
FT /evidence="ECO:0000305"
FT CONFLICT 986
FT /note="R -> Q (in Ref. 5; BAG61337)"
FT /evidence="ECO:0000305"
FT VARIANT Q9NZ71-2:1244
FT /note="C -> R (in DKCB5, severe form consistent with
FT Hoyeraal-Hreidarsson syndrome)"
FT /evidence="ECO:0000269|PubMed:23591994"
FT /id="VAR_082827"
FT CONFLICT Q9NZ71-2:1352
FT /note="C -> R (in Ref. 2; BAA83040)"
FT /evidence="ECO:0000305"
FT VARIANT Q9NZ71-5:489
FT /note="C -> R (in DKCB5, severe form consistent with
FT Hoyeraal-Hreidarsson syndrome)"
FT /evidence="ECO:0000269|PubMed:23591994"
FT /id="VAR_082828"
FT VARIANT Q9NZ71-5:509
FT /note="R -> H (in DKCB5, abolishes activity)"
FT /evidence="ECO:0000269|PubMed:23453664,
FT ECO:0000269|PubMed:24009516"
FT /id="VAR_082829"
FT VARIANT Q9NZ71-6:1244
FT /note="C -> R (in DKCB5, severe form consistent with
FT Hoyeraal-Hreidarsson syndrome; dbSNP:rs587777037)"
FT /evidence="ECO:0000269|PubMed:23591994"
FT /id="VAR_082830"
FT VARIANT Q9NZ71-6:1264
FT /note="R -> H (in DKCB5, abolishes activity;
FT dbSNP:rs201540674)"
FT /evidence="ECO:0000269|PubMed:23453664"
FT /id="VAR_082831"
SQ SEQUENCE 1219 AA; 133683 MW; 28DFCFCC48BC0055 CRC64;
MPKIVLNGVT VDFPFQPYKC QQEYMTKVLE CLQQKVNGIL ESPTGTGKTL CLLCTTLAWR
EHLRDGISAR KIAERAQGEL FPDRALSSWG NAAAAAGDPI ACYTDIPKII YASRTHSQLT
QVINELRNTS YRPKVCVLGS REQLCIHPEV KKQESNHLQI HLCRKKVASR SCHFYNNVEE
KSLEQELASP ILDIEDLVKS GSKHRVCPYY LSRNLKQQAD IIFMPYNYLL DAKSRRAHNI
DLKGTVVIFD EAHNVEKMCE ESASFDLTPH DLASGLDVID QVLEEQTKAA QQGEPHPEFS
ADSPSPGLNM ELEDIAKLKM ILLRLEGAID AVELPGDDSG VTKPGSYIFE LFAEAQITFQ
TKGCILDSLD QIIQHLAGRA GVFTNTAGLQ KLADIIQIVF SVDPSEGSPG SPAGLGALQS
YKVHIHPDAG HRRTAQRSDA WSTTAARKRG KVLSYWCFSP GHSMHELVRQ GVRSLILTSG
TLAPVSSFAL EMQIPFPVCL ENPHIIDKHQ IWVGVVPRGP DGAQLSSAFD RRFSEECLSS
LGKALGNIAR VVPYGLLIFF PSYPVMEKSL EFWRARDLAR KMEALKPLFV EPRSKGSFSE
TISAYYARVA APGSTGATFL AVCRGKASEG LDFSDTNGRG VIVTGLPYPP RMDPRVVLKM
QFLDEMKGQG GAGGQFLSGQ EWYRQQASRA VNQAIGRVIR HRQDYGAVFL CDHRFAFADA
RAQLPSWVRP HVRVYDNFGH VIRDVAQFFR VAERTMPAPA PRATAPSVRG EDAVSEAKSP
GPFFSTRKAK SLDLHVPSLK QRSSGSPAAG DPESSLCVEY EQEPVPARQR PRGLLAALEH
SEQRAGSPGE EQAHSCSTLS LLSEKRPAEE PRGGRKKIRL VSHPEEPVAG AQTDRAKLFM
VAVKQELSQA NFATFTQALQ DYKGSDDFAA LAACLGPLFA EDPKKHNLLQ GFYQFVRPHH
KQQFEEVCIQ LTGRGCGYRP EHSIPRRQRA QPVLDPTGRT APDPKLTVST AAAQQLDPQE
HLNQGRPHLS PRPPPTGDPG SQPQWGSGVP RAGKQGQHAV SAYLADARRA LGSAGCSQLL
AALTAYKQDD DLDKVLAVLA ALTTAKPEDF PLLHRFSMFV RPHHKQRFSQ TCTDLTGRPY
PGMEPPGPQE ERLAVPPVLT HRAPQPGPSR SEKTGKTQSK ISSFLRQRPA GTVGAGGEDA
GPSQSSGPPH GPAASEWGL
