TERF1_HUMAN
ID TERF1_HUMAN Reviewed; 439 AA.
AC P54274; A7XP29; Q15553; Q8NHT6; Q93029;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Telomeric repeat-binding factor 1;
DE AltName: Full=NIMA-interacting protein 2;
DE AltName: Full=TTAGGG repeat-binding factor 1;
DE AltName: Full=Telomeric protein Pin2/TRF1;
GN Name=TERF1; Synonyms=PIN2, TRBF1, TRF, TRF1;
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), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Cervix carcinoma;
RX PubMed=7502076; DOI=10.1126/science.270.5242.1663;
RA Chong L., van Steensel B., Broccoli D., Erdjument-Bromage H., Hanish J.,
RA Tempst P., de Lange T.;
RT "A human telomeric protein.";
RL Science 270:1663-1667(1995).
RN [2]
RP SEQUENCE REVISION TO 14.
RA de Lange T.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 1-138 (ISOFORMS 1 AND 2).
RX PubMed=9326950; DOI=10.1038/ng1097-231;
RA Broccoli D., Smogorzewska A., Chong L., de Lange T.;
RT "Human telomeres contain two distinct Myb-related proteins, TRF1 and
RT TRF2.";
RL Nat. Genet. 17:231-235(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Cervix carcinoma;
RX PubMed=9391075; DOI=10.1073/pnas.94.25.13618;
RA Shen M., Haggblom C., Vogt M., Hunter T., Lu K.P.;
RT "Characterization and cell cycle regulation of the related human telomeric
RT proteins Pin2 and TRF1 suggest a role in mitosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13618-13623(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 329-439 (ISOFORMS 1/2).
RC TISSUE=Cervix carcinoma;
RX PubMed=8614633; DOI=10.1093/nar/24.7.1294;
RA Bilaud T., Koering C.E., Binet-Brasselet E., Ancelin K., Pollice A.,
RA Gasser S.M., Gilson E.;
RT "The telobox, a Myb-related telomeric DNA binding motif found in proteins
RT from yeast, plants and human.";
RL Nucleic Acids Res. 24:1294-1303(1996).
RN [9]
RP MUTAGENESIS OF SER-219, PHOSPHORYLATION AT SER-219, AND INTERACTION WITH
RP ATM.
RX PubMed=11375976; DOI=10.1074/jbc.m011534200;
RA Kishi S., Zhou X.Z., Ziv Y., Khoo C., Hill D.E., Shiloh Y., Lu K.P.;
RT "Telomeric protein Pin2/TRF1 as an important ATM target in response to
RT double strand DNA breaks.";
RL J. Biol. Chem. 276:29282-29291(2001).
RN [10]
RP INTERACTION WITH MAPRE1 AND WITH THE MITOTIC SPINDLE.
RX PubMed=11943150; DOI=10.1016/s0014-5793(02)02363-3;
RA Nakamura M., Zhen Zhou X., Kishi S., Ping Lu K.;
RT "Involvement of the telomeric protein Pin2/TRF1 in the regulation of the
RT mitotic spindle.";
RL FEBS Lett. 514:193-198(2002).
RN [11]
RP ADP-RIBOSYLATION.
RX PubMed=11739745; DOI=10.1128/mcb.22.1.332-342.2002;
RA Cook B.D., Dynek J.N., Chang W., Shostak G., Smith S.;
RT "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at
RT human telomeres.";
RL Mol. Cell. Biol. 22:332-342(2002).
RN [12]
RP IDENTIFICATION IN A COMPLEX WITH POT1; TINF2 AND 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 [13]
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 [14]
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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [17]
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP INTERACTION WITH RLIM, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=19164295; DOI=10.1074/jbc.m806702200;
RA Her Y.R., Chung I.K.;
RT "Ubiquitin ligase RLIM modulates telomere length homeostasis through a
RT proteolysis of TRF1.";
RL J. Biol. Chem. 284:8557-8566(2009).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=19487455; DOI=10.1083/jcb.200812121;
RA Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.;
RT "GNL3L stabilizes the TRF1 complex and promotes mitotic transition.";
RL J. Cell Biol. 185:827-839(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-11, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [23]
RP INTERACTION WITH RTEL1.
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 [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-213; LYS-325 AND LYS-366, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [25]
RP STRUCTURE BY NMR OF 378-430.
RX PubMed=9739097; DOI=10.1016/s0969-2126(98)00106-3;
RA Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y.;
RT "Solution structure of the DNA-binding domain of human telomeric protein,
RT hTRF1.";
RL Structure 6:1057-1065(1998).
RN [26]
RP STRUCTURE BY NMR OF 371-439.
RX PubMed=11738049; DOI=10.1016/s0969-2126(01)00688-8;
RA Nishikawa T., Okamura H., Nagadoi A., Koenig P., Rhodes D., Nishimura Y.;
RT "Solution structure of a telomeric DNA complex of human TRF1.";
RL Structure 9:1237-1251(2001).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 48-268, AND MUTAGENESIS OF ALA-74;
RP ALA-75; TRP-77 AND PHE-81.
RX PubMed=11545737; DOI=10.1016/s1097-2765(01)00321-5;
RA Fairall L., Chapman L., Moss H., de Lange T., Rhodes D.;
RT "Structure of the TRFH dimerization domain of the human telomeric proteins
RT TRF1 and TRF2.";
RL Mol. Cell 8:351-361(2001).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 379-431 IN COMPLEX WITH TELOMERIC
RP DNA, AND SUBUNIT.
RX PubMed=15608617; DOI=10.1038/sj.embor.7400314;
RA Court R., Chapman L., Fairall L., Rhodes D.;
RT "How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a
RT view from high-resolution crystal structures.";
RL EMBO Rep. 6:39-45(2005).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-268 IN COMPLEX WITH TINF2,
RP INTERACTION WITH TINF2 AND PINX1, DOMAIN TRFH DIMERIZATION, AND SUBUNIT.
RX PubMed=18202258; DOI=10.1126/science.1151804;
RA Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P., de Lange T.,
RA Lei M.;
RT "A shared docking motif in TRF1 and TRF2 used for differential recruitment
RT of telomeric proteins.";
RL Science 319:1092-1096(2008).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 58-268 IN COMPLEX WITH FBXO4,
RP MUTAGENESIS OF LEU-115 AND LEU-120, INTERACTION WITH TINF2, SUBUNIT, AND
RP UBIQUITINATION.
RX PubMed=20159592; DOI=10.1016/j.devcel.2010.01.007;
RA Zeng Z., Wang W., Yang Y., Chen Y., Yang X., Diehl J.A., Liu X., Lei M.;
RT "Structural basis of selective ubiquitination of TRF1 by SCFFbx4.";
RL Dev. Cell 18:214-225(2010).
CC -!- FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and
CC negatively regulates telomere length. Involved in the regulation of the
CC mitotic spindle. Component of the shelterin complex (telosome) that is
CC involved in the regulation of telomere length and protection. Shelterin
CC associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by
CC telomerase and protects chromosome ends; without its protective
CC activity, telomeres are no longer hidden from the DNA damage
CC surveillance and chromosome ends are inappropriately processed by DNA
CC repair pathways. {ECO:0000269|PubMed:16166375}.
CC -!- SUBUNIT: Homodimer; can contain both isoforms. Found in a complex with
CC POT1; TINF2 and TNKS1. Interacts with ATM, TINF2, TNKS1, TNKS2, PINX1,
CC NEK2 and MAPRE1. Component of the shelterin complex (telosome) composed
CC of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with RLIM (via
CC N-terminus). Interacts with FBXO4. Interaction with TINF2 protects
CC against interaction with FBXO4 and subsequent polyubiquitination and
CC proteasomal degradation. Interacts with GNL3L; this interaction
CC promotes homodimerization. Interacts with TIN2. Interacts with RTEL1.
CC Interactions with GNL3L and TIN2 are mutually exclusive. Interacts with
CC CCDC79/TERB1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P54274; Q9BWD1: ACAT2; NbExp=2; IntAct=EBI-710997, EBI-1047273;
CC P54274; Q03154: ACY1; NbExp=2; IntAct=EBI-710997, EBI-742064;
CC P54274; Q01433: AMPD2; NbExp=2; IntAct=EBI-710997, EBI-8796759;
CC P54274; P49418: AMPH; NbExp=2; IntAct=EBI-710997, EBI-7121510;
CC P54274; Q13315: ATM; NbExp=3; IntAct=EBI-710997, EBI-495465;
CC P54274; P54132: BLM; NbExp=3; IntAct=EBI-710997, EBI-621372;
CC P54274; Q6P2H3: CEP85; NbExp=2; IntAct=EBI-710997, EBI-2808308;
CC P54274; Q9BR76: CORO1B; NbExp=2; IntAct=EBI-710997, EBI-351152;
CC P54274; P53674: CRYBB1; NbExp=2; IntAct=EBI-710997, EBI-7519424;
CC P54274; Q14894: CRYM; NbExp=2; IntAct=EBI-710997, EBI-7107048;
CC P54274; Q96C57: CUSTOS; NbExp=2; IntAct=EBI-710997, EBI-11305571;
CC P54274; Q9UMR2: DDX19B; NbExp=2; IntAct=EBI-710997, EBI-719232;
CC P54274; Q9BUQ8: DDX23; NbExp=2; IntAct=EBI-710997, EBI-540096;
CC P54274; O00148: DDX39A; NbExp=2; IntAct=EBI-710997, EBI-348253;
CC P54274; P25685: DNAJB1; NbExp=2; IntAct=EBI-710997, EBI-357034;
CC P54274; O43598: DNPH1; NbExp=2; IntAct=EBI-710997, EBI-748674;
CC P54274; Q9H4G0: EPB41L1; NbExp=2; IntAct=EBI-710997, EBI-465536;
CC P54274; Q9UKT5-1: FBXO4; NbExp=2; IntAct=EBI-710997, EBI-960421;
CC P54274; P07332: FES; NbExp=2; IntAct=EBI-710997, EBI-1055635;
CC P54274; P48637: GSS; NbExp=2; IntAct=EBI-710997, EBI-2969145;
CC P54274; P14317: HCLS1; NbExp=2; IntAct=EBI-710997, EBI-750369;
CC P54274; Q96MH2: HEXIM2; NbExp=2; IntAct=EBI-710997, EBI-5460660;
CC P54274; Q93099: HGD; NbExp=2; IntAct=EBI-710997, EBI-3907760;
CC P54274; P17066: HSPA6; NbExp=2; IntAct=EBI-710997, EBI-355106;
CC P54274; Q14145: KEAP1; NbExp=2; IntAct=EBI-710997, EBI-751001;
CC P54274; Q8TBB5: KLHDC4; NbExp=2; IntAct=EBI-710997, EBI-8472352;
CC P54274; P07195: LDHB; NbExp=2; IntAct=EBI-710997, EBI-358748;
CC P54274; Q6UWE0: LRSAM1; NbExp=2; IntAct=EBI-710997, EBI-720984;
CC P54274; Q15691: MAPRE1; NbExp=2; IntAct=EBI-710997, EBI-1004115;
CC P54274; P40925: MDH1; NbExp=2; IntAct=EBI-710997, EBI-709625;
CC P54274; Q9BU76: MMTAG2; NbExp=2; IntAct=EBI-710997, EBI-742459;
CC P54274; P26038: MSN; NbExp=2; IntAct=EBI-710997, EBI-528768;
CC P54274; P55209: NAP1L1; NbExp=2; IntAct=EBI-710997, EBI-356392;
CC P54274; P07196: NEFL; NbExp=2; IntAct=EBI-710997, EBI-475646;
CC P54274; Q9UGY1: NOL12; NbExp=2; IntAct=EBI-710997, EBI-716098;
CC P54274; Q9Y5A7: NUB1; NbExp=8; IntAct=EBI-710997, EBI-3936907;
CC P54274; Q9UNF0: PACSIN2; NbExp=2; IntAct=EBI-710997, EBI-742503;
CC P54274; O96013: PAK4; NbExp=2; IntAct=EBI-710997, EBI-713738;
CC P54274; P12955: PEPD; NbExp=2; IntAct=EBI-710997, EBI-948765;
CC P54274; Q96BK5: PINX1; NbExp=3; IntAct=EBI-710997, EBI-721782;
CC P54274; O15355: PPM1G; NbExp=2; IntAct=EBI-710997, EBI-725702;
CC P54274; Q06830: PRDX1; NbExp=2; IntAct=EBI-710997, EBI-353193;
CC P54274; P30041: PRDX6; NbExp=2; IntAct=EBI-710997, EBI-2255129;
CC P54274; P54829: PTPN5; NbExp=2; IntAct=EBI-710997, EBI-1220572;
CC P54274; P0DJD3: RBMY1A1; NbExp=2; IntAct=EBI-710997, EBI-8638511;
CC P54274; O94761: RECQL4; NbExp=2; IntAct=EBI-710997, EBI-722861;
CC P54274; Q8N5U6: RNF10; NbExp=2; IntAct=EBI-710997, EBI-714023;
CC P54274; Q9H6T3: RPAP3; NbExp=2; IntAct=EBI-710997, EBI-356928;
CC P54274; P84098: RPL19; NbExp=2; IntAct=EBI-710997, EBI-916524;
CC P54274; O95197: RTN3; NbExp=2; IntAct=EBI-710997, EBI-740467;
CC P54274; Q9Y3L3: SH3BP1; NbExp=2; IntAct=EBI-710997, EBI-346869;
CC P54274; Q9NUL5: SHFL; NbExp=2; IntAct=EBI-710997, EBI-10313866;
CC P54274; O76070: SNCG; NbExp=2; IntAct=EBI-710997, EBI-1053810;
CC P54274; P35610: SOAT1; NbExp=2; IntAct=EBI-710997, EBI-6621955;
CC P54274; P19623: SRM; NbExp=2; IntAct=EBI-710997, EBI-1056183;
CC P54274; Q8WVM7: STAG1; NbExp=4; IntAct=EBI-710997, EBI-1175097;
CC P54274; O00267: SUPT5H; NbExp=2; IntAct=EBI-710997, EBI-710464;
CC P54274; P43405: SYK; NbExp=2; IntAct=EBI-710997, EBI-78302;
CC P54274; Q8NA31: TERB1; NbExp=4; IntAct=EBI-710997, EBI-21942840;
CC P54274; Q9NWX6: THG1L; NbExp=2; IntAct=EBI-710997, EBI-746510;
CC P54274; Q9BSI4: TINF2; NbExp=11; IntAct=EBI-710997, EBI-717399;
CC P54274; Q9BSI4-3: TINF2; NbExp=2; IntAct=EBI-710997, EBI-717418;
CC P54274; P29401: TKT; NbExp=2; IntAct=EBI-710997, EBI-1050560;
CC P54274; O95271: TNKS; NbExp=6; IntAct=EBI-710997, EBI-1105254;
CC P54274; Q9H2K2: TNKS2; NbExp=4; IntAct=EBI-710997, EBI-4398527;
CC P54274; O14787: TNPO2; NbExp=2; IntAct=EBI-710997, EBI-431907;
CC P54274; P60174: TPI1; NbExp=2; IntAct=EBI-710997, EBI-717475;
CC P54274; Q9NXH9: TRMT1; NbExp=2; IntAct=EBI-710997, EBI-748900;
CC P54274; Q13509: TUBB3; NbExp=2; IntAct=EBI-710997, EBI-350989;
CC P54274; P23381: WARS1; NbExp=2; IntAct=EBI-710997, EBI-721244;
CC P54274; O76024: WFS1; NbExp=2; IntAct=EBI-710997, EBI-720609;
CC P54274; PRO_0000037315 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-710997, EBI-25487941;
CC P54274-2; Q9NR81: ARHGEF3; NbExp=3; IntAct=EBI-711018, EBI-10312733;
CC P54274-2; Q13315: ATM; NbExp=5; IntAct=EBI-711018, EBI-495465;
CC P54274-2; P55212: CASP6; NbExp=3; IntAct=EBI-711018, EBI-718729;
CC P54274-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-711018, EBI-10976677;
CC P54274-2; Q86X45: DNAAF11; NbExp=3; IntAct=EBI-711018, EBI-9379658;
CC P54274-2; Q9UKT5-1: FBXO4; NbExp=3; IntAct=EBI-711018, EBI-960421;
CC P54274-2; P22607: FGFR3; NbExp=3; IntAct=EBI-711018, EBI-348399;
CC P54274-2; Q53GS7: GLE1; NbExp=3; IntAct=EBI-711018, EBI-1955541;
CC P54274-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-711018, EBI-8285963;
CC P54274-2; P06396: GSN; NbExp=3; IntAct=EBI-711018, EBI-351506;
CC P54274-2; O00291: HIP1; NbExp=3; IntAct=EBI-711018, EBI-473886;
CC P54274-2; P30519: HMOX2; NbExp=3; IntAct=EBI-711018, EBI-712096;
CC P54274-2; P01112: HRAS; NbExp=3; IntAct=EBI-711018, EBI-350145;
CC P54274-2; Q96MP8-2: KCTD7; NbExp=7; IntAct=EBI-711018, EBI-11954971;
CC P54274-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-711018, EBI-21591415;
CC P54274-2; P02545: LMNA; NbExp=3; IntAct=EBI-711018, EBI-351935;
CC P54274-2; Q8IVT2: MISP; NbExp=5; IntAct=EBI-711018, EBI-2555085;
CC P54274-2; P35240: NF2; NbExp=3; IntAct=EBI-711018, EBI-1014472;
CC P54274-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-711018, EBI-748974;
CC P54274-2; Q15004: PCLAF; NbExp=3; IntAct=EBI-711018, EBI-10971436;
CC P54274-2; P62826: RAN; NbExp=3; IntAct=EBI-711018, EBI-286642;
CC P54274-2; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-711018, EBI-2623095;
CC P54274-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-711018, EBI-5235340;
CC P54274-2; P31948: STIP1; NbExp=3; IntAct=EBI-711018, EBI-1054052;
CC P54274-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-711018, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
CC Chromosome, telomere. Note=Colocalizes with telomeric DNA in interphase
CC and prophase cells. Telomeric localization decreases in metaphase,
CC anaphase and telophase. Associates with the mitotic spindle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=TRF1;
CC IsoId=P54274-1; Sequence=Displayed;
CC Name=2; Synonyms=Pin2;
CC IsoId=P54274-2; Sequence=VSP_003303;
CC -!- TISSUE SPECIFICITY: Highly expressed and ubiquitous. Isoform Pin2
CC predominates.
CC -!- INDUCTION: Expression is tightly regulated during the cell cycle;
CC levels are low in G1 and S phase and increase during G2 phase and
CC mitosis.
CC -!- DOMAIN: The acidic N-terminal domain binds to the ankyrin repeats of
CC TNKS1 and TNKS2. The C-terminal domain binds microtubules.
CC {ECO:0000269|PubMed:18202258}.
CC -!- DOMAIN: The TRFH dimerization region mediates the interaction with
CC TINF2. {ECO:0000269|PubMed:18202258}.
CC -!- DOMAIN: The HTH domain is an independent structural unit and mediates
CC binding to telomeric DNA. {ECO:0000269|PubMed:18202258}.
CC -!- PTM: Phosphorylated preferentially on Ser-219 in an ATM-dependent
CC manner in response to ionizing DNA damage.
CC {ECO:0000269|PubMed:11375976}.
CC -!- PTM: ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind
CC to telomeric DNA.
CC -!- PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the
CC proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-
CC protein ligase complex, leading to its degradation by the proteasome.
CC {ECO:0000269|PubMed:19164295, ECO:0000269|PubMed:20159592}.
CC -!- WEB RESOURCE: Name=NIEHS SNPs;
CC URL="http://egp.gs.washington.edu/data/terf1/";
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DR EMBL; U40705; AAB54036.1; -; mRNA.
DR EMBL; AF003001; AAB81137.1; -; mRNA.
DR EMBL; AH003684; AAB17975.1; -; Genomic_DNA.
DR EMBL; U74382; AAB53363.1; -; mRNA.
DR EMBL; EU088287; ABV02580.1; -; Genomic_DNA.
DR EMBL; AC022893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029378; AAH29378.1; -; mRNA.
DR EMBL; X93511; CAA63768.1; -; mRNA.
DR CCDS; CCDS6210.1; -. [P54274-2]
DR CCDS; CCDS6211.1; -. [P54274-1]
DR PIR; A57573; A57573.
DR RefSeq; NP_003209.2; NM_003218.3. [P54274-2]
DR RefSeq; NP_059523.2; NM_017489.2. [P54274-1]
DR PDB; 1BA5; NMR; -; A=378-430.
DR PDB; 1H6O; X-ray; 2.90 A; A=62-265.
DR PDB; 1ITY; NMR; -; A=371-439.
DR PDB; 1IV6; NMR; -; A=371-439.
DR PDB; 1W0T; X-ray; 2.00 A; A/B=379-431.
DR PDB; 3BQO; X-ray; 2.00 A; A=58-268.
DR PDB; 3L82; X-ray; 2.40 A; A=58-268.
DR PDB; 5HKP; X-ray; 2.20 A; C/D=1-55.
DR PDB; 5WIR; X-ray; 2.10 A; A/B=62-265.
DR PDB; 5XUP; X-ray; 2.10 A; A/B=65-266.
DR PDBsum; 1BA5; -.
DR PDBsum; 1H6O; -.
DR PDBsum; 1ITY; -.
DR PDBsum; 1IV6; -.
DR PDBsum; 1W0T; -.
DR PDBsum; 3BQO; -.
DR PDBsum; 3L82; -.
DR PDBsum; 5HKP; -.
DR PDBsum; 5WIR; -.
DR PDBsum; 5XUP; -.
DR AlphaFoldDB; P54274; -.
DR BMRB; P54274; -.
DR SMR; P54274; -.
DR BioGRID; 112872; 336.
DR ComplexPortal; CPX-152; Shelterin complex.
DR CORUM; P54274; -.
DR DIP; DIP-29412N; -.
DR ELM; P54274; -.
DR IntAct; P54274; 241.
DR MINT; P54274; -.
DR STRING; 9606.ENSP00000276603; -.
DR iPTMnet; P54274; -.
DR PhosphoSitePlus; P54274; -.
DR BioMuta; TERF1; -.
DR DMDM; 206729904; -.
DR EPD; P54274; -.
DR jPOST; P54274; -.
DR MassIVE; P54274; -.
DR MaxQB; P54274; -.
DR PaxDb; P54274; -.
DR PeptideAtlas; P54274; -.
DR PRIDE; P54274; -.
DR ProteomicsDB; 56664; -. [P54274-1]
DR ProteomicsDB; 56665; -. [P54274-2]
DR Antibodypedia; 12281; 692 antibodies from 40 providers.
DR DNASU; 7013; -.
DR Ensembl; ENST00000276602.10; ENSP00000276602.6; ENSG00000147601.15. [P54274-2]
DR Ensembl; ENST00000276603.10; ENSP00000276603.5; ENSG00000147601.15. [P54274-1]
DR GeneID; 7013; -.
DR KEGG; hsa:7013; -.
DR MANE-Select; ENST00000276603.10; ENSP00000276603.5; NM_017489.3; NP_059523.2.
DR UCSC; uc003xzd.3; human. [P54274-1]
DR CTD; 7013; -.
DR DisGeNET; 7013; -.
DR GeneCards; TERF1; -.
DR HGNC; HGNC:11728; TERF1.
DR HPA; ENSG00000147601; Low tissue specificity.
DR MIM; 600951; gene.
DR neXtProt; NX_P54274; -.
DR OpenTargets; ENSG00000147601; -.
DR PharmGKB; PA36445; -.
DR VEuPathDB; HostDB:ENSG00000147601; -.
DR eggNOG; ENOG502RYK3; Eukaryota.
DR GeneTree; ENSGT00940000155268; -.
DR HOGENOM; CLU_034265_0_0_1; -.
DR InParanoid; P54274; -.
DR OMA; AVAAEWM; -.
DR OrthoDB; 605826at2759; -.
DR PhylomeDB; P54274; -.
DR TreeFam; TF333209; -.
DR PathwayCommons; P54274; -.
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; P54274; -.
DR SIGNOR; P54274; -.
DR BioGRID-ORCS; 7013; 599 hits in 1099 CRISPR screens.
DR ChiTaRS; TERF1; human.
DR EvolutionaryTrace; P54274; -.
DR GeneWiki; TERF1; -.
DR GenomeRNAi; 7013; -.
DR Pharos; P54274; Tbio.
DR PRO; PR:P54274; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P54274; protein.
DR Bgee; ENSG00000147601; Expressed in buccal mucosa cell and 215 other tissues.
DR ExpressionAtlas; P54274; baseline and differential.
DR Genevisible; P54274; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0000783; C:nuclear telomere cap complex; IDA:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070187; C:shelterin complex; IDA:BHF-UCL.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0071532; F:ankyrin repeat binding; IPI:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0008301; F:DNA binding, bending; IDA:BHF-UCL.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:UniProtKB.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045141; P:meiotic telomere clustering; IEA:Ensembl.
DR GO; GO:0008156; P:negative regulation of DNA replication; IDA:BHF-UCL.
DR GO; GO:1904850; P:negative regulation of establishment of protein localization to telomere; IMP:BHF-UCL.
DR GO; GO:1904914; P:negative regulation of establishment of protein-containing complex localization to telomere; IC:BHF-UCL.
DR GO; GO:1904911; P:negative regulation of establishment of RNA localization to telomere; IMP:BHF-UCL.
DR GO; GO:1905778; P:negative regulation of exonuclease activity; IDA:BHF-UCL.
DR GO; GO:0051974; P:negative regulation of telomerase activity; IGI:BHF-UCL.
DR GO; GO:0032214; P:negative regulation of telomere maintenance via semi-conservative replication; NAS:BHF-UCL.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IGI:BHF-UCL.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; TAS:BHF-UCL.
DR GO; GO:1905839; P:negative regulation of telomeric D-loop disassembly; IDA:BHF-UCL.
DR GO; GO:1904792; P:positive regulation of shelterin complex assembly; IMP:BHF-UCL.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IC:ComplexPortal.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0090656; P:t-circle formation; TAS:BHF-UCL.
DR GO; GO:0016233; P:telomere capping; IDA:ComplexPortal.
DR GO; GO:0000723; P:telomere maintenance; IMP:BHF-UCL.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IDA:BHF-UCL.
DR GO; GO:0061820; P:telomeric D-loop disassembly; IGI:BHF-UCL.
DR DisProt; DP02415; -.
DR Gene3D; 1.25.40.210; -; 1.
DR IDEAL; IID00155; -.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR013867; Telomere_rpt-bd_fac_dimer_dom.
DR InterPro; IPR036507; Telomere_rpt-bd_fac_dimer_sf.
DR InterPro; IPR017357; TERF1/2.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF08558; TRF; 1.
DR PIRSF; PIRSF038016; Telomere_bd-1_Pin2; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF63600; SSF63600; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
KW Cell cycle; Cell division; Chromosome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Telomere; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231"
FT CHAIN 2..439
FT /note="Telomeric repeat-binding factor 1"
FT /id="PRO_0000197129"
FT DOMAIN 375..432
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 403..428
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..268
FT /note="TRFH dimerization"
FT REGION 265..378
FT /note="Interaction with RLIM"
FT /evidence="ECO:0000269|PubMed:19164295"
FT REGION 266..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 337..356
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 18..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000269|PubMed:11375976"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 296..315
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9326950, ECO:0000303|PubMed:9391075"
FT /id="VSP_003303"
FT MUTAGEN 74
FT /note="A->D: Abolishes dimerization and telomere binding;
FT when associated with P-75."
FT /evidence="ECO:0000269|PubMed:11545737"
FT MUTAGEN 75
FT /note="A->P: Abolishes dimerization and telomere binding;
FT when associated with D-74."
FT /evidence="ECO:0000269|PubMed:11545737"
FT MUTAGEN 77
FT /note="W->P: Abolishes telomere binding."
FT /evidence="ECO:0000269|PubMed:11545737"
FT MUTAGEN 81
FT /note="F->P: Abolishes telomere binding."
FT /evidence="ECO:0000269|PubMed:11545737"
FT MUTAGEN 90
FT /note="F->P: Diminishes telomere binding."
FT MUTAGEN 115
FT /note="L->R: Loss of interaction with FBXO4."
FT /evidence="ECO:0000269|PubMed:20159592"
FT MUTAGEN 120
FT /note="L->R: Loss of interaction with FBXO4."
FT /evidence="ECO:0000269|PubMed:20159592"
FT MUTAGEN 219
FT /note="S->A: Loss of phosphorylation; induction of mitotic
FT entry and apoptosis and increased radiation
FT hypersensitivity of ataxia-telangiectasia cells."
FT /evidence="ECO:0000269|PubMed:11375976"
FT MUTAGEN 219
FT /note="S->D,E: Fails to induce apoptosis and decreases
FT radiation hypersensitivity of ataxia-telangiectasia cells
FT (phospho-mimicking mutants)."
FT /evidence="ECO:0000269|PubMed:11375976"
FT CONFLICT 14
FT /note="G -> R (in Ref. 1; AAB54036, 3; AAB17975/AAB81137
FT and 4; AAB53363)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="K -> E (in Ref. 8; CAA63768)"
FT /evidence="ECO:0000305"
FT HELIX 63..92
FT /evidence="ECO:0007829|PDB:3BQO"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:3BQO"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3L82"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:3BQO"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:3BQO"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:3BQO"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:3BQO"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:3BQO"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:3BQO"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3L82"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:3BQO"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:3BQO"
FT HELIX 233..251
FT /evidence="ECO:0007829|PDB:3BQO"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1H6O"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:3BQO"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:1ITY"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:1W0T"
FT HELIX 403..409
FT /evidence="ECO:0007829|PDB:1W0T"
FT HELIX 417..428
FT /evidence="ECO:0007829|PDB:1W0T"
SQ SEQUENCE 439 AA; 50246 MW; AB548E7D3124A211 CRC64;
MAEDVSSAAP SPRGCADGRD ADPTEEQMAE TERNDEEQFE CQELLECQVQ VGAPEEEEEE
EEDAGLVAEA EAVAAGWMLD FLCLSLCRAF RDGRSEDFRR TRNSAEAIIH GLSSLTACQL
RTIYICQFLT RIAAGKTLDA QFENDERITP LESALMIWGS IEKEHDKLHE EIQNLIKIQA
IAVCMENGNF KEAEEVFERI FGDPNSHMPF KSKLLMIISQ KDTFHSFFQH FSYNHMMEKI
KSYVNYVLSE KSSTFLMKAA AKVVESKRTR TITSQDKPSG NDVEMETEAN LDTRKSVSDK
QSAVTESSEG TVSLLRSHKN LFLSKLQHGT QQQDLNKKER RVGTPQSTKK KKESRRATES
RIPVSKSQPV TPEKHRARKR QAWLWEEDKN LRSGVRKYGE GNWSKILLHY KFNNRTSVML
KDRWRTMKKL KLISSDSED
