ID POTE1_HUMAN Reviewed; 634 AA. AC Q9NUX5; O95018; Q5MJ36; Q9H662; Q9NW19; Q9UG95; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 202. DE RecName: Full=Protection of telomeres protein 1; DE Short=hPot1; DE AltName: Full=POT1-like telomere end-binding protein; GN Name=POT1; 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), TISSUE SPECIFICITY, AND RP SINGLE-STRANDED TELOMERE DNA-BINDING. RC TISSUE=Ovary; RX PubMed=11349150; DOI=10.1126/science.1060036; RA Baumann P., Cech T.R.; RT "Pot1, the putative telomere end-binding protein in fission yeast and RT humans."; RL Science 292:1171-1175(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 1 RP AND 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SINGLE-STRANDED RP TELOMERE DNA-BINDING. RX PubMed=12391173; DOI=10.1128/mcb.22.22.8079-8087.2002; RA Baumann P., Podell E., Cech T.R.; RT "Human Pot1 (protection of telomeres) protein: cytolocalization, gene RT structure, and alternative splicing."; RL Mol. Cell. Biol. 22:8079-8087(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta, Small intestine, and Teratocarcinoma; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 499-634 (ISOFORM 1). RC TISSUE=Uterus; 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 [8] RP FUNCTION IN TELOMERE REGULATION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), RP AND SINGLE-STRANDED TELOMERE DNA-BINDING. RX PubMed=12781132; DOI=10.1016/s0960-9822(03)00339-7; RA Colgin L.M., Baran K., Baumann P., Cech T.R., Reddel R.R.; RT "Human POT1 facilitates telomere elongation by telomerase."; RL Curr. Biol. 13:942-946(2003). RN [9] RP FUNCTION IN TELOMERE REGULATION, IDENTIFICATION IN A COMPLEX WITH TERF1; RP TINF2 AND TNKS1, AND INTERACTION WITH TNKS1. RX PubMed=12768206; DOI=10.1038/nature01688; RA Loayza D., De Lange T.; RT "POT1 as a terminal transducer of TRF1 telomere length control."; RL Nature 423:1013-1018(2003). RN [10] RP SINGLE-STRANDED TELOMERE DNA-BINDING. RX PubMed=14715659; DOI=10.1074/jbc.m312309200; RA Loayza D., Parsons H., Donigian J., Hoke K., de Lange T.; RT "DNA binding features of human POT1: a nonamer 5'-TAGGGTTAG-3' minimal RT binding site, sequence specificity, and internal binding to multimeric RT sites."; RL J. Biol. Chem. 279:13241-13248(2004). RN [11] RP INTERACTION WITH ACD. RX PubMed=15231715; DOI=10.1101/gad.1215404; RA Ye J.Z.-S., Hockemeyer D., Krutchinsky A.N., Loayza D., Hooper S.M., RA Chait B.T., de Lange T.; RT "POT1-interacting protein PIP1: a telomere length regulator that recruits RT POT1 to the TIN2/TRF1 complex."; RL Genes Dev. 18:1649-1654(2004). RN [12] RP IDENTIFICATION IN THE SHELTERIN COMPLEX. RX PubMed=15316005; DOI=10.1074/jbc.m409047200; RA Ye J.Z.-S., Donigian J.R., van Overbeek M., Loayza D., Luo Y., RA Krutchinsky A.N., Chait B.T., de Lange T.; RT "TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on RT telomeres."; RL J. Biol. Chem. 279:47264-47271(2004). RN [13] RP IDENTIFICATION IN THE SHELTERIN COMPLEX. RX PubMed=15383534; DOI=10.1074/jbc.m409293200; RA Liu D., O'Connor M.S., Qin J., Songyang Z.; RT "Telosome, a mammalian telomere-associated complex formed by multiple RT telomeric proteins."; RL J. Biol. Chem. 279:51338-51342(2004). RN [14] RP FUNCTION OF THE SHELTERIN COMPLEX. RX PubMed=16166375; DOI=10.1101/gad.1346005; RA de Lange T.; RT "Shelterin: the protein complex that shapes and safeguards human RT telomeres."; RL Genes Dev. 19:2100-2110(2005). RN [15] RP FUNCTION, SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH ACD AND RP SINGLE-STRANDED TELOMERIC DNA. RX PubMed=17237768; DOI=10.1038/nature05454; RA Wang F., Podell E.R., Zaug A.J., Yang Y., Baciu P., Cech T.R., Lei M.; RT "The POT1-TPP1 telomere complex is a telomerase processivity factor."; RL Nature 445:506-510(2007). RN [16] RP IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX. RX PubMed=19179534; DOI=10.1126/science.1165357; RA Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M., RA Veenstra T.D., Terns M.P., Artandi S.E.; RT "A human telomerase holoenzyme protein required for Cajal body localization RT and telomere synthesis."; RL Science 323:644-648(2009). RN [17] RP FUNCTION. RX PubMed=20231318; DOI=10.1101/gad.1881810; RA Zaug A.J., Podell E.R., Nandakumar J., Cech T.R.; RT "Functional interaction between telomere protein TPP1 and telomerase."; RL Genes Dev. 24:613-622(2010). RN [18] RP INVOLVEMENT IN TPDS3, VARIANTS TPDS3 CYS-89; GLU-94 AND LEU-273, AND RP CHARACTERIZATION OF VARIANTS TPDS3 CYS-89; GLU-94 AND LEU-273. RX PubMed=24686849; DOI=10.1038/ng.2947; RA Robles-Espinoza C.D., Harland M., Ramsay A.J., Aoude L.G., Quesada V., RA Ding Z., Pooley K.A., Pritchard A.L., Tiffen J.C., Petljak M., Palmer J.M., RA Symmons J., Johansson P., Stark M.S., Gartside M.G., Snowden H., RA Montgomery G.W., Martin N.G., Liu J.Z., Choi J., Makowski M., Brown K.M., RA Dunning A.M., Keane T.M., Lopez-Otin C., Gruis N.A., Hayward N.K., RA Bishop D.T., Newton-Bishop J.A., Adams D.J.; RT "POT1 loss-of-function variants predispose to familial melanoma."; RL Nat. Genet. 46:478-481(2014). RN [19] RP INVOLVEMENT IN CRMCC3, VARIANT CRMCC3 LEU-322, CHARACTERIZATION OF VARIANT RP CRMCC3 LEU-322, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ACD. RX PubMed=27013236; DOI=10.1101/gad.276873.115; RA Takai H., Jenkinson E., Kabir S., Babul-Hirji R., Najm-Tehrani N., RA Chitayat D.A., Crow Y.J., de Lange T.; RT "A POT1 mutation implicates defective telomere end fill-in and telomere RT truncations in Coats plus."; RL Genes Dev. 30:812-826(2016). RN [20] RP INVOLVEMENT IN TPDS3, AND VARIANT TPDS3 CYS-95. RX PubMed=25482530; DOI=10.1093/jnci/dju384; RG Gliogene Consortium; RA Bainbridge M.N., Armstrong G.N., Gramatges M.M., Bertuch A.A., RA Jhangiani S.N., Doddapaneni H., Lewis L., Tombrello J., Tsavachidis S., RA Liu Y., Jalali A., Plon S.E., Lau C.C., Parsons D.W., Claus E.B., RA Barnholtz-Sloan J., Il'yasova D., Schildkraut J., Ali-Osman F., RA Sadetzki S., Johansen C., Houlston R.S., Jenkins R.B., Lachance D., RA Olson S.H., Bernstein J.L., Merrell R.T., Wrensch M.R., Walsh K.M., RA Davis F.G., Lai R., Shete S., Aldape K., Amos C.I., Thompson P.A., RA Muzny D.M., Gibbs R.A., Melin B.S., Bondy M.L.; RT "Germline mutations in shelterin complex genes are associated with familial RT glioma."; RL J. Natl. Cancer Inst. 107:384-384(2015). RN [21] RP INVOLVEMENT IN PFBMFT8, VARIANT PFBMFT8 SER-259, CHARACTERIZATION OF RP VARIANT PFBMFT8 SER-259, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION RP WITH ACD. RX PubMed=35420632; DOI=10.1084/jem.20211681; RA Kelich J., Aramburu T., van der Vis J.J., Showe L., Kossenkov A., RA van der Smagt J., Massink M., Schoemaker A., Hennekam E., Veltkamp M., RA van Moorsel C.H.M., Skordalakes E.; RT "Telomere dysfunction implicates POT1 in patients with idiopathic pulmonary RT fibrosis."; RL J. Exp. Med. 219:0-0(2022). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 6-299 IN COMPLEX WITH RP SINGLE-STRANDED TELOMERIC DNA. RX PubMed=15558049; DOI=10.1038/nsmb867; RA Lei M., Podell E.R., Cech T.R.; RT "Structure of human POT1 bound to telomeric single-stranded DNA provides a RT model for chromosome end-protection."; RL Nat. Struct. Mol. Biol. 11:1223-1229(2004). RN [23] RP VARIANTS TPDS3 HIS-137; ASN-224; ASN-270; PRO-532 AND HIS-623, AND RP CHARACTERIZATION OF VARIANTS TPDS3 HIS-137; ASN-270 AND HIS-623. RX PubMed=24686846; DOI=10.1038/ng.2941; RA Shi J., Yang X.R., Ballew B., Rotunno M., Calista D., Fargnoli M.C., RA Ghiorzo P., Bressac-de Paillerets B., Nagore E., Avril M.F., Caporaso N.E., RA McMaster M.L., Cullen M., Wang Z., Zhang X., Bruno W., Pastorino L., RA Queirolo P., Banuls-Roca J., Garcia-Casado Z., Vaysse A., Mohamdi H., RA Riazalhosseini Y., Foglio M., Jouenne F., Hua X., Hyland P.L., Yin J., RA Vallabhaneni H., Chai W., Minghetti P., Pellegrini C., Ravichandran S., RA Eggermont A., Lathrop M., Peris K., Scarra G.B., Landi G., Savage S.A., RA Sampson J.N., He J., Yeager M., Goldin L.R., Demenais F., Chanock S.J., RA Tucker M.A., Goldstein A.M., Liu Y., Landi M.T.; RT "Rare missense variants in POT1 predispose to familial cutaneous malignant RT melanoma."; RL Nat. Genet. 46:482-486(2014). RN [24] RP VARIANT TPDS3 THR-78, CHARACTERIZATION OF TPDS3 THR-78, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=30586141; DOI=10.1001/jamadermatol.2018.3662; RA Wong K., Robles-Espinoza C.D., Rodriguez D., Rudat S.S., Puig S., RA Potrony M., Wong C.C., Hewinson J., Aguilera P., Puig-Butille J.A., RA Bressac-de Paillerets B., Zattara H., van der Weyden L., Fletcher C.D.M., RA Brenn T., Arends M.J., Quesada V., Newton-Bishop J.A., Lopez-Otin C., RA Bishop D.T., Harms P.W., Johnson T.M., Durham A.B., Lombard D.B., RA Adams D.J.; RT "Association of the POT1 Germline Missense Variant p.I78T With Familial RT Melanoma."; RL JAMA Dermatol. 155:604-609(2019). RN [25] RP VARIANTS TPDS3 THR-78 AND GLN-273, CHARACTERIZATION OF VARIANTS TPDS3 RP THR-78 AND GLN-273, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=37140166; DOI=10.1056/nejmoa2300503; RA DeBoy E.A., Tassia M.G., Schratz K.E., Yan S.M., Cosner Z.L., McNally E.J., RA Gable D.L., Xiang Z., Lombard D.B., Antonarakis E.S., Gocke C.D., RA McCoy R.C., Armanios M.; RT "Familial Clonal Hematopoiesis in a Long Telomere Syndrome."; RL N. Engl. J. Med. 388:2422-2433(2023). CC -!- FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex CC that is essential for the replication of chromosome termini. Is a CC component of the double-stranded telomeric DNA-binding TRF1 complex CC which is involved in the regulation of telomere length by cis- CC inhibition of telomerase. Also acts as a single-stranded telomeric DNA- CC binding protein and thus may act as a downstream effector of the TRF1 CC complex and may transduce information about telomere maintenance and/or CC length to the telomere terminus. Component of the shelterin complex CC (telosome) that is involved in the regulation of telomere length and CC protection. Shelterin associates with arrays of double-stranded TTAGGG CC repeats added by telomerase and protects chromosome ends; without its CC protective activity, telomeres are no longer hidden from the DNA damage CC surveillance and chromosome ends are inappropriately processed by DNA CC repair pathways. Binds to two or more telomeric single-stranded 5'- CC TTAGGG-3' repeats (G-strand) and with high specificity to a minimal CC telomeric single-stranded 5'-TAGGGTTAG-3' sequence. Binds telomeric CC single-stranded sequences internally or at proximity of a 3'-end. Its CC activity is TERT dependent but it does not increase TERT activity by CC itself. In contrast, the ACD-POT1 heterodimer enhances telomere CC elongation by increasing telomerase processivity. CC {ECO:0000269|PubMed:12768206, ECO:0000269|PubMed:12781132, CC ECO:0000269|PubMed:16166375, ECO:0000269|PubMed:17237768, CC ECO:0000269|PubMed:20231318, ECO:0000269|PubMed:27013236, CC ECO:0000269|PubMed:35420632}. CC -!- SUBUNIT: Homodimer or homooligomer (PubMed:17237768). Component of the CC shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP, CC ACD and POT1 (PubMed:15316005, PubMed:15383534). Binds single-stranded CC telomeric DNA as a monomer (PubMed:15558049). Associated component of CC the telomerase holoenzyme complex (PubMed:19179534). Found in a complex CC with TERF1, TINF2 and TNKS1 (PubMed:12768206). Interacts with TNKS1. CC Forms heterodimers with ACD (PubMed:15231715, PubMed:27013236, CC PubMed:35420632). Identified in a complex with ACD and single-stranded CC telomeric DNA (PubMed:17237768). {ECO:0000269|PubMed:12768206, CC ECO:0000269|PubMed:15231715, ECO:0000269|PubMed:15316005, CC ECO:0000269|PubMed:15383534, ECO:0000269|PubMed:15558049, CC ECO:0000269|PubMed:17237768, ECO:0000269|PubMed:19179534, CC ECO:0000269|PubMed:27013236, ECO:0000269|PubMed:35420632}. CC -!- INTERACTION: CC Q9NUX5; Q96AP0: ACD; NbExp=9; IntAct=EBI-752420, EBI-717666; CC Q9NUX5; P30838: ALDH3A1; NbExp=2; IntAct=EBI-752420, EBI-3905126; CC Q9NUX5; P07355: ANXA2; NbExp=2; IntAct=EBI-752420, EBI-352622; CC Q9NUX5; Q9BV29: CCDC32; NbExp=2; IntAct=EBI-752420, EBI-2874058; CC Q9NUX5; Q549N0: CFL2; NbExp=3; IntAct=EBI-752420, EBI-10201319; CC Q9NUX5; Q9Y281: CFL2; NbExp=3; IntAct=EBI-752420, EBI-351218; CC Q9NUX5; O95833: CLIC3; NbExp=2; IntAct=EBI-752420, EBI-10192241; CC Q9NUX5; Q6PJW8: CNST; NbExp=2; IntAct=EBI-752420, EBI-750390; CC Q9NUX5; O60496: DOK2; NbExp=2; IntAct=EBI-752420, EBI-1046024; CC Q9NUX5; O94808: GFPT2; NbExp=2; IntAct=EBI-752420, EBI-6916534; CC Q9NUX5; Q99795: GPA33; NbExp=2; IntAct=EBI-752420, EBI-4289554; CC Q9NUX5; P46952: HAAO; NbExp=2; IntAct=EBI-752420, EBI-743215; CC Q9NUX5; P50747: HLCS; NbExp=2; IntAct=EBI-752420, EBI-3915568; CC Q9NUX5; P09601: HMOX1; NbExp=2; IntAct=EBI-752420, EBI-2806151; CC Q9NUX5; P0DMV8: HSPA1A; NbExp=2; IntAct=EBI-752420, EBI-11052499; CC Q9NUX5; Q9NPH2: ISYNA1; NbExp=2; IntAct=EBI-752420, EBI-720563; CC Q9NUX5; Q96A73: KIAA1191; NbExp=2; IntAct=EBI-752420, EBI-725897; CC Q9NUX5; Q8WXG6: MADD; NbExp=2; IntAct=EBI-752420, EBI-310528; CC Q9NUX5; P43358: MAGEA4; NbExp=2; IntAct=EBI-752420, EBI-743122; CC Q9NUX5; Q12851: MAP4K2; NbExp=2; IntAct=EBI-752420, EBI-49783; CC Q9NUX5; Q03426: MVK; NbExp=2; IntAct=EBI-752420, EBI-740630; CC Q9NUX5; Q9BY11: PACSIN1; NbExp=2; IntAct=EBI-752420, EBI-721769; CC Q9NUX5; Q96GU1: PAGE5; NbExp=2; IntAct=EBI-752420, EBI-11305258; CC Q9NUX5; Q01064: PDE1B; NbExp=2; IntAct=EBI-752420, EBI-7413304; CC Q9NUX5; Q5SRE7: PHYHD1; NbExp=2; IntAct=EBI-752420, EBI-2623130; CC Q9NUX5; Q8IUZ5: PHYKPL; NbExp=2; IntAct=EBI-752420, EBI-751947; CC Q9NUX5; Q9P0Z9: PIPOX; NbExp=2; IntAct=EBI-752420, EBI-725582; CC Q9NUX5; Q86WR7: PROSER2; NbExp=2; IntAct=EBI-752420, EBI-2880603; CC Q9NUX5; Q9BRP8: PYM1; NbExp=2; IntAct=EBI-752420, EBI-2352802; CC Q9NUX5; Q9BWH6: RPAP1; NbExp=2; IntAct=EBI-752420, EBI-1048085; CC Q9NUX5; O43704: SULT1B1; NbExp=2; IntAct=EBI-752420, EBI-10179062; CC Q9NUX5; Q9BR01: SULT4A1; NbExp=2; IntAct=EBI-752420, EBI-6690555; CC Q9NUX5; Q96A49: SYAP1; NbExp=2; IntAct=EBI-752420, EBI-10770179; CC Q9NUX5; Q15554: TERF2; NbExp=7; IntAct=EBI-752420, EBI-706637; CC Q9NUX5; Q9BSI4: TINF2; NbExp=3; IntAct=EBI-752420, EBI-717399; CC Q9NUX5; P63313: TMSB10; NbExp=2; IntAct=EBI-752420, EBI-2688673; CC Q9NUX5; Q9Y4P8: WIPI2; NbExp=2; IntAct=EBI-752420, EBI-719396; CC Q9NUX5-1; Q96AP0: ACD; NbExp=4; IntAct=EBI-15593881, EBI-717666; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12391173, CC ECO:0000269|PubMed:27013236, ECO:0000269|PubMed:30586141, CC ECO:0000269|PubMed:35420632, ECO:0000269|PubMed:37140166}. Chromosome, CC telomere {ECO:0000269|PubMed:12391173, ECO:0000269|PubMed:27013236, CC ECO:0000269|PubMed:30586141, ECO:0000269|PubMed:35420632, CC ECO:0000269|PubMed:37140166}. Note=Colocalizes with telomeric DNA. CC {ECO:0000269|PubMed:12391173}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=A number of isoforms are produced.; CC Name=1; Synonyms=Variant 1; CC IsoId=Q9NUX5-1; Sequence=Displayed; CC Name=2; Synonyms=Variant 3; CC IsoId=Q9NUX5-2; Sequence=VSP_010846, VSP_010847; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11349150, CC ECO:0000269|PubMed:12391173}. CC -!- DISEASE: Tumor predisposition syndrome 3 (TPDS3) [MIM:615848]: An CC autosomal dominant disorder characterized by an increased risk for the CC development of various types of benign and malignant neoplasms CC throughout life, with age-dependent penetrance. Affected individuals CC can develop neoplasms involving epithelial, mesenchymal, and neuronal CC tissues, as well as lymphoid and myeloid cancers. The disorder is CC associated with elongated telomeres. {ECO:0000269|PubMed:24686846, CC ECO:0000269|PubMed:24686849, ECO:0000269|PubMed:25482530, CC ECO:0000269|PubMed:30586141, ECO:0000269|PubMed:37140166}. Note=Disease CC susceptibility is associated with variants affecting the gene CC represented in this entry. CC -!- DISEASE: Cerebroretinal microangiopathy with calcifications and cysts 3 CC (CRMCC3) [MIM:620368]: An autosomal recessive disorder characterized by CC intrauterine growth retardation, retinal exudates, global developmental CC delay, neurologic regression, intracranial calcifications, and CC leukoencephalopathy. {ECO:0000269|PubMed:27013236}. Note=The disease CC may be caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Pulmonary fibrosis, and/or bone marrow failure syndrome, CC telomere-related, 8 (PFBMFT8) [MIM:620367]: An autosomal dominant CC disease associated with shortened telomeres. Pulmonary fibrosis is the CC most common manifestation. Other features include aplastic anemia due CC to bone marrow failure, hepatic fibrosis, and increased cancer risk. CC Phenotype, age at onset, and severity are determined by telomere CC length. PFBMFT8 is characterized by the onset of progressive pulmonary CC fibrosis in adulthood, signs of bone marrow failure, such as CC thrombocytopenia, liver dysfunction, and features of dyskeratosis CC congenita, including premature graying of the hair, in some affected CC individuals. {ECO:0000269|PubMed:35420632}. Note=The disease may be CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the telombin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15404.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AY823520; AAW22613.1; -; mRNA. DR EMBL; AK001230; BAA91568.1; -; mRNA. DR EMBL; AK001935; BAA91988.1; -; mRNA. DR EMBL; AK022580; BAB14110.1; -; mRNA. DR EMBL; AK026234; BAB15404.1; ALT_INIT; mRNA. DR EMBL; AC004925; AAD08852.1; -; Genomic_DNA. DR EMBL; AC096665; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC110791; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471070; EAW83616.1; -; Genomic_DNA. DR EMBL; BC002923; AAH02923.1; -; mRNA. DR EMBL; AL050120; CAB43281.1; -; mRNA. DR CCDS; CCDS5793.1; -. [Q9NUX5-1] DR PIR; T08766; T08766. DR RefSeq; NP_001036059.1; NM_001042594.1. DR RefSeq; NP_056265.2; NM_015450.2. [Q9NUX5-1] DR RefSeq; XP_006715980.1; XM_006715917.3. DR PDB; 1XJV; X-ray; 1.73 A; A=6-299. DR PDB; 3KJO; X-ray; 1.80 A; A=1-299. DR PDB; 3KJP; X-ray; 1.80 A; A=1-299. DR PDB; 5H65; X-ray; 2.10 A; A=341-634. DR PDB; 5UN7; X-ray; 2.10 A; A=330-634. DR PDB; 7QXB; EM; 3.91 A; P=1-634. DR PDB; 7QXS; EM; 3.91 A; P=1-634. DR PDB; 7S1O; X-ray; 2.55 A; A/B=325-634. DR PDB; 7S1T; X-ray; 2.90 A; A/D/G/J=325-634. DR PDB; 7S1U; X-ray; 2.55 A; A/B=331-634. DR PDB; 8SH0; X-ray; 2.16 A; A=1-299. DR PDB; 8SH1; X-ray; 2.60 A; A=1-299. DR PDB; 8SOJ; EM; 3.80 A; D=2-634. DR PDB; 8SOK; EM; 4.10 A; D=2-634. DR PDBsum; 1XJV; -. DR PDBsum; 3KJO; -. DR PDBsum; 3KJP; -. DR PDBsum; 5H65; -. DR PDBsum; 5UN7; -. DR PDBsum; 7QXB; -. DR PDBsum; 7QXS; -. DR PDBsum; 7S1O; -. DR PDBsum; 7S1T; -. DR PDBsum; 7S1U; -. DR PDBsum; 8SH0; -. DR PDBsum; 8SH1; -. DR PDBsum; 8SOJ; -. DR PDBsum; 8SOK; -. DR AlphaFoldDB; Q9NUX5; -. DR EMDB; EMD-14197; -. DR EMDB; EMD-14199; -. DR EMDB; EMD-40659; -. DR EMDB; EMD-40660; -. DR SMR; Q9NUX5; -. DR BioGRID; 117417; 240. DR ComplexPortal; CPX-152; Shelterin complex. DR CORUM; Q9NUX5; -. DR DIP; DIP-29610N; -. DR IntAct; Q9NUX5; 183. DR STRING; 9606.ENSP00000350249; -. DR BindingDB; Q9NUX5; -. DR ChEMBL; CHEMBL5908; -. DR MoonDB; Q9NUX5; Predicted. DR GlyGen; Q9NUX5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NUX5; -. DR PhosphoSitePlus; Q9NUX5; -. DR BioMuta; POT1; -. DR DMDM; 50401179; -. DR EPD; Q9NUX5; -. DR jPOST; Q9NUX5; -. DR MassIVE; Q9NUX5; -. DR MaxQB; Q9NUX5; -. DR PaxDb; 9606-ENSP00000350249; -. DR PeptideAtlas; Q9NUX5; -. DR ProteomicsDB; 82726; -. [Q9NUX5-1] DR ProteomicsDB; 82727; -. [Q9NUX5-2] DR Pumba; Q9NUX5; -. DR Antibodypedia; 31798; 340 antibodies from 32 providers. DR DNASU; 25913; -. DR Ensembl; ENST00000357628.8; ENSP00000350249.3; ENSG00000128513.16. [Q9NUX5-1] DR Ensembl; ENST00000653241.1; ENSP00000499476.1; ENSG00000128513.16. [Q9NUX5-1] DR Ensembl; ENST00000655761.1; ENSP00000499635.1; ENSG00000128513.16. [Q9NUX5-1] DR Ensembl; ENST00000664366.1; ENSP00000499290.1; ENSG00000128513.16. [Q9NUX5-1] DR Ensembl; ENST00000668382.1; ENSP00000499546.1; ENSG00000128513.16. [Q9NUX5-1] DR GeneID; 25913; -. DR KEGG; hsa:25913; -. DR MANE-Select; ENST00000357628.8; ENSP00000350249.3; NM_015450.3; NP_056265.2. DR UCSC; uc003vlm.4; human. [Q9NUX5-1] DR AGR; HGNC:17284; -. DR CTD; 25913; -. DR DisGeNET; 25913; -. DR GeneCards; POT1; -. DR GeneReviews; POT1; -. DR HGNC; HGNC:17284; POT1. DR HPA; ENSG00000128513; Low tissue specificity. DR MalaCards; POT1; -. DR MIM; 606478; gene. DR MIM; 615848; phenotype. DR MIM; 620367; phenotype. DR MIM; 620368; phenotype. DR neXtProt; NX_Q9NUX5; -. DR OpenTargets; ENSG00000128513; -. DR Orphanet; 251630; Anaplastic oligodendroglioma. DR Orphanet; 67038; B-cell chronic lymphocytic leukemia. DR Orphanet; 618; Familial melanoma. DR Orphanet; 251627; Oligodendroglioma. DR PharmGKB; PA134934904; -. DR VEuPathDB; HostDB:ENSG00000128513; -. DR eggNOG; KOG4757; Eukaryota. DR GeneTree; ENSGT00390000018285; -. DR HOGENOM; CLU_019567_0_0_1; -. DR InParanoid; Q9NUX5; -. DR OMA; VPNGDAF; -. DR OrthoDB; 52603at2759; -. DR PhylomeDB; Q9NUX5; -. DR TreeFam; TF328398; -. DR PathwayCommons; Q9NUX5; -. DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine. DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine. DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine. DR Reactome; R-HSA-110331; Cleavage of the damaged purine. DR Reactome; R-HSA-1221632; Meiotic synapsis. DR Reactome; R-HSA-171306; Packaging Of Telomere Ends. DR Reactome; R-HSA-171319; Telomere Extension By Telomerase. DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere. DR Reactome; R-HSA-174414; Processive synthesis on the C-strand of the telomere. DR Reactome; R-HSA-174417; Telomere C-strand (Lagging Strand) Synthesis. DR Reactome; R-HSA-174430; Telomere C-strand synthesis initiation. DR Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand. DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence. DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere. DR SignaLink; Q9NUX5; -. DR SIGNOR; Q9NUX5; -. DR BioGRID-ORCS; 25913; 392 hits in 1169 CRISPR screens. DR ChiTaRS; POT1; human. DR EvolutionaryTrace; Q9NUX5; -. DR GeneWiki; POT1; -. DR GenomeRNAi; 25913; -. DR Pharos; Q9NUX5; Tbio. DR PRO; PR:Q9NUX5; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9NUX5; Protein. DR Bgee; ENSG00000128513; Expressed in secondary oocyte and 193 other cell types or tissues. DR ExpressionAtlas; Q9NUX5; baseline and differential. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB. DR GO; GO:0000783; C:nuclear telomere cap complex; IDA:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0070187; C:shelterin complex; IDA:BHF-UCL. DR GO; GO:1905773; F:8-hydroxy-2'-deoxyguanosine DNA binding; IDA:BHF-UCL. DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:BHF-UCL. DR GO; GO:1990955; F:G-rich single-stranded DNA binding; IDA:BHF-UCL. DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL. DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:BHF-UCL. DR GO; GO:0010521; F:telomerase inhibitor activity; IDA:BHF-UCL. DR GO; GO:0061821; F:telomeric D-loop binding; IDA:BHF-UCL. DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL. DR GO; GO:0032508; P:DNA duplex unwinding; IDA:BHF-UCL. DR GO; GO:0070200; P:establishment of protein localization to telomere; IMP:BHF-UCL. DR GO; GO:0051974; P:negative regulation of telomerase activity; IDA:BHF-UCL. DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IGI:BHF-UCL. DR GO; GO:1905776; P:positive regulation of DNA helicase activity; IDA:BHF-UCL. DR GO; GO:0060383; P:positive regulation of DNA strand elongation; IDA:BHF-UCL. DR GO; GO:0051096; P:positive regulation of helicase activity; IDA:BHF-UCL. DR GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL. DR GO; GO:0032206; P:positive regulation of telomere maintenance; NAS:ComplexPortal. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IDA:BHF-UCL. DR GO; GO:1905774; P:regulation of DNA helicase activity; IDA:BHF-UCL. DR GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; IDA:CACAO. DR GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IGI:BHF-UCL. DR GO; GO:0032202; P:telomere assembly; IDA:BHF-UCL. DR GO; GO:0016233; P:telomere capping; IDA:ComplexPortal. DR GO; GO:0007004; P:telomere maintenance via telomerase; IDA:UniProtKB. DR GO; GO:0061820; P:telomeric D-loop disassembly; IGI:BHF-UCL. DR CDD; cd04497; hPOT1_OB1_like; 1. DR CDD; cd04498; hPOT1_OB2; 1. DR CDD; cd20374; Pot1C; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR028389; POT1. DR InterPro; IPR048953; POT1_C_insert. DR InterPro; IPR032042; POT1PC. DR InterPro; IPR011564; Telomer_end-bd_POT1/Cdc13. DR PANTHER; PTHR14513; PROTECTION OF TELOMERES 1; 1. DR PANTHER; PTHR14513:SF0; PROTECTION OF TELOMERES PROTEIN 1; 1. DR Pfam; PF02765; POT1; 1. DR Pfam; PF21375; POT1_C_insert; 1. DR Pfam; PF16686; POT1PC; 1. DR SMART; SM00976; Telo_bind; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2. DR Genevisible; Q9NUX5; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosome; Disease variant; KW DNA-binding; Nucleus; Reference proteome; Telomere. FT CHAIN 1..634 FT /note="Protection of telomeres protein 1" FT /id="PRO_0000121728" FT REGION 33..48 FT /note="DNA-binding" FT REGION 270..273 FT /note="DNA-binding" FT SITE 243 FT /note="DNA-binding" FT VAR_SEQ 532..538 FT /note="ALGIVPL -> DVNSVLV (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_010846" FT VAR_SEQ 539..634 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_010847" FT VARIANT 78 FT /note="I -> T (in TPDS3; uncertain significance; decreased FT DNA binding; affects function in telomere maintenance; FT telomere length is increased when the mutant is expressed FT in heterologous cells)" FT /evidence="ECO:0000269|PubMed:30586141, FT ECO:0000269|PubMed:37140166" FT /id="VAR_088595" FT VARIANT 89 FT /note="Y -> C (in TPDS3; complete abolition of POT1-DNA FT complex formation, thus disrupting the interaction with FT telomeres and leading to elongated telomeres; FT dbSNP:rs587777472)" FT /evidence="ECO:0000269|PubMed:24686849" FT /id="VAR_071390" FT VARIANT 94 FT /note="Q -> E (in TPDS3; complete abolition of POT1-DNA FT complex formation, thus disrupting the interaction with FT telomeres and leading to elongated telomeres; FT dbSNP:rs587777474)" FT /evidence="ECO:0000269|PubMed:24686849" FT /id="VAR_071391" FT VARIANT 95 FT /note="G -> C (in TPDS3; dbSNP:rs797045168)" FT /evidence="ECO:0000269|PubMed:25482530" FT /id="VAR_075717" FT VARIANT 137 FT /note="R -> H (in TPDS3; increased telomere intensity FT signals and telomere fragility; dbSNP:rs587777475)" FT /evidence="ECO:0000269|PubMed:24686846" FT /id="VAR_071392" FT VARIANT 224 FT /note="D -> N (in TPDS3; dbSNP:rs202187871)" FT /evidence="ECO:0000269|PubMed:24686846" FT /id="VAR_071393" FT VARIANT 259 FT /note="L -> S (in PFBMFT8; uncertain significance; affects FT function in telomere maintenance in patient cells and when FT expressed in heterologous cells; decreased DNA binding; FT decreased localization to nucleus; no effect on interaction FT with ADC; no effect on localization to telomeres)" FT /evidence="ECO:0000269|PubMed:35420632" FT /id="VAR_088596" FT VARIANT 270 FT /note="S -> N (in TPDS3; significantly increased telomere FT length and numbers of fragile telomeres; FT dbSNP:rs587777477)" FT /evidence="ECO:0000269|PubMed:24686846" FT /id="VAR_071394" FT VARIANT 273 FT /note="R -> L (in TPDS3; complete abolition of POT1-DNA FT complex formation, thus disrupting the interaction with FT telomeres and leading to elongated telomeres; FT dbSNP:rs587777476)" FT /evidence="ECO:0000269|PubMed:24686849" FT /id="VAR_071395" FT VARIANT 273 FT /note="R -> Q (in TPDS3; likely pathogenic; decreased DNA FT binding)" FT /evidence="ECO:0000269|PubMed:37140166" FT /id="VAR_088597" FT VARIANT 322 FT /note="S -> L (in CRMCC3; uncertain significance; affects FT function in telomere maintenance when expressed in FT heterologous cells; no effect on interaction with ADC; no FT effect on localization to telomeres)" FT /evidence="ECO:0000269|PubMed:27013236" FT /id="VAR_088598" FT VARIANT 529 FT /note="V -> M (in dbSNP:rs34973253)" FT /id="VAR_034393" FT VARIANT 532 FT /note="A -> P (in TPDS3; dbSNP:rs537377921)" FT /evidence="ECO:0000269|PubMed:24686846" FT /id="VAR_071396" FT VARIANT 623 FT /note="Q -> H (in TPDS3; increased telomere intensity FT signals and telomere fragility; dbSNP:rs587777478)" FT /evidence="ECO:0000269|PubMed:24686846" FT /id="VAR_071397" FT CONFLICT 410 FT /note="D -> V (in Ref. 3; BAA91568)" FT /evidence="ECO:0000305" FT CONFLICT 412 FT /note="K -> Q (in Ref. 3; BAB15404)" FT /evidence="ECO:0000305" FT CONFLICT 499 FT /note="H -> D (in Ref. 7; CAB43281)" FT /evidence="ECO:0000305" FT HELIX 14..16 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 19..37 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 39..50 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 56..65 FT /evidence="ECO:0007829|PDB:1XJV" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 78..89 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 92..106 FT /evidence="ECO:0007829|PDB:1XJV" FT HELIX 127..143 FT /evidence="ECO:0007829|PDB:1XJV" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 161..173 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 175..184 FT /evidence="ECO:0007829|PDB:1XJV" FT TURN 200..202 FT /evidence="ECO:0007829|PDB:3KJP" FT HELIX 207..213 FT /evidence="ECO:0007829|PDB:1XJV" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 217..223 FT /evidence="ECO:0007829|PDB:1XJV" FT HELIX 226..232 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 238..251 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 257..265 FT /evidence="ECO:0007829|PDB:1XJV" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 274..278 FT /evidence="ECO:0007829|PDB:1XJV" FT HELIX 283..297 FT /evidence="ECO:0007829|PDB:1XJV" FT STRAND 334..339 FT /evidence="ECO:0007829|PDB:5UN7" FT HELIX 348..352 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 359..370 FT /evidence="ECO:0007829|PDB:5H65" FT HELIX 374..377 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 378..381 FT /evidence="ECO:0007829|PDB:5H65" FT TURN 383..385 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:5H65" FT HELIX 394..404 FT /evidence="ECO:0007829|PDB:5H65" FT HELIX 411..413 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 417..425 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 433..439 FT /evidence="ECO:0007829|PDB:5H65" FT HELIX 448..450 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 452..457 FT /evidence="ECO:0007829|PDB:5H65" FT HELIX 460..469 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 470..478 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 480..486 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 492..495 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 498..500 FT /evidence="ECO:0007829|PDB:5H65" FT TURN 504..506 FT /evidence="ECO:0007829|PDB:5H65" FT HELIX 512..517 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 521..523 FT /evidence="ECO:0007829|PDB:5H65" FT HELIX 526..532 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 539..549 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 554..563 FT /evidence="ECO:0007829|PDB:5H65" FT TURN 564..566 FT /evidence="ECO:0007829|PDB:5H65" FT HELIX 570..573 FT /evidence="ECO:0007829|PDB:5H65" FT HELIX 577..590 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 593..595 FT /evidence="ECO:0007829|PDB:5H65" FT HELIX 597..599 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 603..611 FT /evidence="ECO:0007829|PDB:5H65" FT STRAND 614..616 FT /evidence="ECO:0007829|PDB:7S1T" FT STRAND 620..626 FT /evidence="ECO:0007829|PDB:5H65" FT TURN 630..632 FT /evidence="ECO:0007829|PDB:5H65" SQ SEQUENCE 634 AA; 71442 MW; 123A12CABE708C91 CRC64; MSLVPATNYI YTPLNQLKGG TIVNVYGVVK FFKPPYLSKG TDYCSVVTIV DQTNVKLTCL LFSGNYEALP IIYKNGDIVR FHRLKIQVYK KETQGITSSG FASLTFEGTL GAPIIPRTSS KYFNFTTEDH KMVEALRVWA STHMSPSWTL LKLCDVQPMQ YFDLTCQLLG KAEVDGASFL LKVWDGTRTP FPSWRVLIQD LVLEGDLSHI HRLQNLTIDI LVYDNHVHVA RSLKVGSFLR IYSLHTKLQS MNSENQTMLS LEFHLHGGTS YGRGIRVLPE SNSDVDQLKK DLESANLTAN QHSDVICQSE PDDSFPSSGS VSLYEVERCQ QLSATILTDH QYLERTPLCA ILKQKAPQQY RIRAKLRSYK PRRLFQSVKL HCPKCHLLQE VPHEGDLDII FQDGATKTPD VKLQNTSLYD SKIWTTKNQK GRKVAVHFVK NNGILPLSNE CLLLIEGGTL SEICKLSNKF NSVIPVRSGH EDLELLDLSA PFLIQGTIHH YGCKQCSSLR SIQNLNSLVD KTSWIPSSVA EALGIVPLQY VFVMTFTLDD GTGVLEAYLM DSDKFFQIPA SEVLMDDDLQ KSVDMIMDMF CPPGIKIDAY PWLECFIKSY NVTNGTDNQI CYQIFDTTVA EDVI //