HNRPF_HUMAN
ID HNRPF_HUMAN Reviewed; 415 AA.
AC P52597; B3KM84; Q5T0N2; Q96AU2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 228.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein F;
DE Short=hnRNP F;
DE AltName: Full=Nucleolin-like protein mcs94-1;
DE Contains:
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein F, N-terminally processed;
GN Name=HNRNPF; Synonyms=HNRPF;
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], AND PROTEIN SEQUENCE OF 52-61; 78-83 AND
RP 128-136.
RX PubMed=7512260; DOI=10.1093/nar/22.6.1059;
RA Matunis M.J., Xing J., Dreyfuss G.;
RT "The hnRNP F protein: unique primary structure, nucleic acid-binding
RT properties, and subcellular localization.";
RL Nucleic Acids Res. 22:1059-1067(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7499401; DOI=10.1074/jbc.270.48.28780;
RA Honore B., Rasmussen H.H., Vorum H., Dejgaard K., Liu X., Gromov P.,
RA Madsen P., Gesser B., Tommerup N., Celis J.E.;
RT "Heterogeneous nuclear ribonucleoproteins H, H', and F are members of a
RT ubiquitously expressed subfamily of related but distinct proteins encoded
RT by genes mapping to different chromosomes.";
RL J. Biol. Chem. 270:28780-28789(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1351868; DOI=10.1016/0888-7543(92)90251-m;
RA McDonald H., Smailus D., Jenkins H., Adams K., Simpson N.E.,
RA Goodfellow P.J.;
RT "Identification and characterization of a gene at D10S94 in the MEN2A
RT region.";
RL Genomics 13:344-348(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-87.
RC TISSUE=Bone marrow, Lung, Ovary, Placenta, and Uterus;
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 PROTEIN SEQUENCE OF 1-14; 53-68; 82-87; 99-114; 151-167; 180-185 AND
RP 300-347, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND MET-2,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma, and Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (OCT-2008) to UniProtKB.
RN [9]
RP INTERACTION WITH TXNL4.
RX PubMed=11054566; DOI=10.1016/s0378-1119(00)00372-3;
RA Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E., Golemis E.A.;
RT "Evidence that Dim1 associates with proteins involved in pre-mRNA splicing,
RT and delineation of residues essential for Dim1 interactions with hnRNP F
RT and Npw38/PQBP-1.";
RL Gene 257:33-43(2000).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [12]
RP SUMOYLATION AT LYS-72.
RX PubMed=15161980; DOI=10.1073/pnas.0402889101;
RA Li T., Evdokimov E., Shen R.F., Chao C.C., Tekle E., Wang T.,
RA Stadtman E.R., Yang D.C., Chock P.B.;
RT "Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger
RT proteins, and nuclear pore complex proteins: a proteomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8551-8556(2004).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [14]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein
RT complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-224, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-187, AND
RP 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-107; SER-193;
RP THR-215 AND SER-265, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-167; LYS-185; LYS-200 AND
RP LYS-224, AND 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 [30]
RP STRUCTURE BY NMR OF 1-102; 103-194 AND 277-381 IN COMPLEX WITH BCL-X RNA,
RP AND MUTAGENESIS OF PHE-120; PHE-156; HIS-178 AND TYR-180.
RX PubMed=16885237; DOI=10.1093/nar/gkl488;
RA Dominguez C., Allain F.H.;
RT "NMR structure of the three quasi RNA recognition motifs (qRRMs) of human
RT hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel mode of RNA
RT recognition.";
RL Nucleic Acids Res. 34:3634-3645(2006).
RN [31]
RP STRUCTURE BY NMR OF 1-194 AND 277-381 IN COMPLEXES WITH AGGGAU RNA
RP OLIGONUCLEOTIDE, FUNCTION, AND MUTAGENESIS OF TRP-20; GLU-84; ARG-116;
RP PHE-120; LYS-150; LYS-173; ARG-179; TYR-180; GLU-182 AND PHE-184.
RX PubMed=20526337; DOI=10.1038/nsmb.1814;
RA Dominguez C., Fisette J.F., Chabot B., Allain F.H.;
RT "Structural basis of G-tract recognition and encaging by hnRNP F quasi-
RT RRMs.";
RL Nat. Struct. Mol. Biol. 17:853-861(2010).
CC -!- FUNCTION: Component of the heterogeneous nuclear ribonucleoprotein
CC (hnRNP) complexes which provide the substrate for the processing events
CC that pre-mRNAs undergo before becoming functional, translatable mRNAs
CC in the cytoplasm. Plays a role in the regulation of alternative
CC splicing events. Binds G-rich sequences in pre-mRNAs and keeps target
CC RNA in an unfolded state. {ECO:0000269|PubMed:20526337}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with AGO1,
CC AGO2, TBP and TXNL4/DIM1. {ECO:0000269|PubMed:11054566,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:16885237,
CC ECO:0000269|PubMed:17932509}.
CC -!- INTERACTION:
CC P52597; Q53H80: AKIRIN2; NbExp=3; IntAct=EBI-352986, EBI-742928;
CC P52597; P41238: APOBEC1; NbExp=3; IntAct=EBI-352986, EBI-12819523;
CC P52597; Q86V38: ATN1; NbExp=3; IntAct=EBI-352986, EBI-11954292;
CC P52597; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-352986, EBI-12811889;
CC P52597; Q9BXC9: BBS2; NbExp=3; IntAct=EBI-352986, EBI-748297;
CC P52597; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-352986, EBI-12809220;
CC P52597; Q6P1W5: C1orf94; NbExp=6; IntAct=EBI-352986, EBI-946029;
CC P52597; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-352986, EBI-11523759;
CC P52597; Q86Y13: DZIP3; NbExp=6; IntAct=EBI-352986, EBI-948630;
CC P52597; Q9NRA8: EIF4ENIF1; NbExp=3; IntAct=EBI-352986, EBI-301024;
CC P52597; Q9NVL1-2: FAM86C1P; NbExp=3; IntAct=EBI-352986, EBI-12845222;
CC P52597; A0A024R5S0: hCG_2003792; NbExp=3; IntAct=EBI-352986, EBI-10188461;
CC P52597; P31943: HNRNPH1; NbExp=3; IntAct=EBI-352986, EBI-351590;
CC P52597; P52272: HNRNPM; NbExp=6; IntAct=EBI-352986, EBI-486809;
CC P52597; Q9BUJ2: HNRNPUL1; NbExp=5; IntAct=EBI-352986, EBI-1018153;
CC P52597; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-352986, EBI-3957665;
CC P52597; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-352986, EBI-747204;
CC P52597; Q0VD86: INCA1; NbExp=3; IntAct=EBI-352986, EBI-6509505;
CC P52597; Q6IPM2: IQCE; NbExp=3; IntAct=EBI-352986, EBI-3893098;
CC P52597; Q92993: KAT5; NbExp=3; IntAct=EBI-352986, EBI-399080;
CC P52597; Q13351: KLF1; NbExp=3; IntAct=EBI-352986, EBI-8284732;
CC P52597; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-352986, EBI-2796400;
CC P52597; Q5T749: KPRP; NbExp=3; IntAct=EBI-352986, EBI-10981970;
CC P52597; O95678: KRT75; NbExp=3; IntAct=EBI-352986, EBI-2949715;
CC P52597; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-352986, EBI-18394498;
CC P52597; Q14847-2: LASP1; NbExp=3; IntAct=EBI-352986, EBI-9088686;
CC P52597; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-352986, EBI-11742507;
CC P52597; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-352986, EBI-739832;
CC P52597; Q9NRX2: MRPL17; NbExp=3; IntAct=EBI-352986, EBI-7825154;
CC P52597; O43347: MSI1; NbExp=3; IntAct=EBI-352986, EBI-726515;
CC P52597; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-352986, EBI-10271199;
CC P52597; Q9BRJ7: NUDT16L1; NbExp=3; IntAct=EBI-352986, EBI-2949792;
CC P52597; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-352986, EBI-11022007;
CC P52597; Q9NR12: PDLIM7; NbExp=5; IntAct=EBI-352986, EBI-350517;
CC P52597; P62937-2: PPIA; NbExp=3; IntAct=EBI-352986, EBI-25884072;
CC P52597; P17252: PRKCA; NbExp=3; IntAct=EBI-352986, EBI-1383528;
CC P52597; O75360: PROP1; NbExp=3; IntAct=EBI-352986, EBI-9027467;
CC P52597; B1ATL7: PRR32; NbExp=3; IntAct=EBI-352986, EBI-18587059;
CC P52597; Q9NV39: PRR34; NbExp=3; IntAct=EBI-352986, EBI-11959565;
CC P52597; O43251: RBFOX2; NbExp=4; IntAct=EBI-352986, EBI-746056;
CC P52597; O43251-10: RBFOX2; NbExp=3; IntAct=EBI-352986, EBI-11963050;
CC P52597; Q04864-2: REL; NbExp=3; IntAct=EBI-352986, EBI-10829018;
CC P52597; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-352986, EBI-6257312;
CC P52597; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-352986, EBI-9090795;
CC P52597; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-352986, EBI-10269374;
CC P52597; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-352986, EBI-12275818;
CC P52597; O60504: SORBS3; NbExp=3; IntAct=EBI-352986, EBI-741237;
CC P52597; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-352986, EBI-8635958;
CC P52597; Q96A09: TENT5B; NbExp=3; IntAct=EBI-352986, EBI-752030;
CC P52597; Q92734: TFG; NbExp=3; IntAct=EBI-352986, EBI-357061;
CC P52597; Q96PF1: TGM7; NbExp=3; IntAct=EBI-352986, EBI-12029034;
CC P52597; Q08117: TLE5; NbExp=3; IntAct=EBI-352986, EBI-717810;
CC P52597; Q08117-2: TLE5; NbExp=3; IntAct=EBI-352986, EBI-11741437;
CC P52597; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-352986, EBI-492476;
CC P52597; Q14142: TRIM14; NbExp=3; IntAct=EBI-352986, EBI-2820256;
CC P52597; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-352986, EBI-12817837;
CC P52597; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-352986, EBI-11975223;
CC P52597; Q99990: VGLL1; NbExp=3; IntAct=EBI-352986, EBI-11983165;
CC P52597; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-352986, EBI-2559305;
CC P52597; P61981: YWHAG; NbExp=3; IntAct=EBI-352986, EBI-359832;
CC P52597; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-352986, EBI-10188476;
CC P52597; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-352986, EBI-745520;
CC P52597; Q96H86: ZNF764; NbExp=3; IntAct=EBI-352986, EBI-745775;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- DOMAIN: The N-terminal RRM domains are responsible for recognizing the
CC G-tract of BCL-X RNA.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15161980}.
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DR EMBL; L28010; AAC37584.1; -; mRNA.
DR EMBL; AL512654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK001364; BAG50896.1; -; mRNA.
DR EMBL; CH471160; EAW86595.1; -; Genomic_DNA.
DR EMBL; BC001432; AAH01432.1; -; mRNA.
DR EMBL; BC004254; AAH04254.1; -; mRNA.
DR EMBL; BC015580; AAH15580.1; -; mRNA.
DR EMBL; BC016736; AAH16736.1; -; mRNA.
DR EMBL; BC106008; AAI06009.1; -; mRNA.
DR CCDS; CCDS7204.1; -.
DR PIR; S43484; S43484.
DR RefSeq; NP_001091674.1; NM_001098204.1.
DR RefSeq; NP_001091675.1; NM_001098205.1.
DR RefSeq; NP_001091676.1; NM_001098206.1.
DR RefSeq; NP_001091677.1; NM_001098207.1.
DR RefSeq; NP_001091678.1; NM_001098208.1.
DR RefSeq; NP_004957.1; NM_004966.3.
DR PDB; 2HGL; NMR; -; A=1-102.
DR PDB; 2HGM; NMR; -; A=103-194.
DR PDB; 2HGN; NMR; -; A=277-381.
DR PDB; 2KFY; NMR; -; A=1-102.
DR PDB; 2KG0; NMR; -; A=103-194.
DR PDB; 2KG1; NMR; -; A=277-381.
DR PDB; 3TFY; X-ray; 2.75 A; D/E/F=2-10.
DR PDBsum; 2HGL; -.
DR PDBsum; 2HGM; -.
DR PDBsum; 2HGN; -.
DR PDBsum; 2KFY; -.
DR PDBsum; 2KG0; -.
DR PDBsum; 2KG1; -.
DR PDBsum; 3TFY; -.
DR AlphaFoldDB; P52597; -.
DR SMR; P52597; -.
DR BioGRID; 109426; 441.
DR CORUM; P52597; -.
DR DIP; DIP-33145N; -.
DR IntAct; P52597; 183.
DR MINT; P52597; -.
DR STRING; 9606.ENSP00000400433; -.
DR ChEMBL; CHEMBL4523238; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; P52597; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P52597; -.
DR MetOSite; P52597; -.
DR PhosphoSitePlus; P52597; -.
DR SwissPalm; P52597; -.
DR BioMuta; HNRNPF; -.
DR DMDM; 1710628; -.
DR OGP; P52597; -.
DR EPD; P52597; -.
DR jPOST; P52597; -.
DR MassIVE; P52597; -.
DR MaxQB; P52597; -.
DR PaxDb; P52597; -.
DR PeptideAtlas; P52597; -.
DR PRIDE; P52597; -.
DR ProteomicsDB; 56497; -.
DR Antibodypedia; 13432; 357 antibodies from 33 providers.
DR DNASU; 3185; -.
DR Ensembl; ENST00000337970.7; ENSP00000338477.3; ENSG00000169813.17.
DR Ensembl; ENST00000356053.7; ENSP00000348345.3; ENSG00000169813.17.
DR Ensembl; ENST00000357065.8; ENSP00000349573.4; ENSG00000169813.17.
DR Ensembl; ENST00000443950.6; ENSP00000400433.2; ENSG00000169813.17.
DR Ensembl; ENST00000544000.5; ENSP00000438061.1; ENSG00000169813.17.
DR Ensembl; ENST00000682386.1; ENSP00000507787.1; ENSG00000169813.17.
DR GeneID; 3185; -.
DR KEGG; hsa:3185; -.
DR MANE-Select; ENST00000682386.1; ENSP00000507787.1; NM_001098204.2; NP_001091674.1.
DR UCSC; uc001jar.2; human.
DR CTD; 3185; -.
DR DisGeNET; 3185; -.
DR GeneCards; HNRNPF; -.
DR HGNC; HGNC:5039; HNRNPF.
DR HPA; ENSG00000169813; Low tissue specificity.
DR MIM; 601037; gene.
DR neXtProt; NX_P52597; -.
DR OpenTargets; ENSG00000169813; -.
DR PharmGKB; PA162391271; -.
DR VEuPathDB; HostDB:ENSG00000169813; -.
DR eggNOG; KOG4211; Eukaryota.
DR GeneTree; ENSGT00940000157838; -.
DR HOGENOM; CLU_032003_1_0_1; -.
DR InParanoid; P52597; -.
DR OMA; GDACVIF; -.
DR OrthoDB; 603679at2759; -.
DR PhylomeDB; P52597; -.
DR TreeFam; TF316157; -.
DR PathwayCommons; P52597; -.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR SignaLink; P52597; -.
DR BioGRID-ORCS; 3185; 127 hits in 1092 CRISPR screens.
DR ChiTaRS; HNRNPF; human.
DR EvolutionaryTrace; P52597; -.
DR GeneWiki; HNRPF; -.
DR GenomeRNAi; 3185; -.
DR Pharos; P52597; Tbio.
DR PRO; PR:P52597; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P52597; protein.
DR Bgee; ENSG00000169813; Expressed in ventricular zone and 196 other tissues.
DR ExpressionAtlas; P52597; baseline and differential.
DR Genevisible; P52597; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR DisProt; DP01736; -.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR012996; Znf_CHHC.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF08080; zf-RNPHF; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Ubl conjugation.
FT CHAIN 1..415
FT /note="Heterogeneous nuclear ribonucleoprotein F"
FT /id="PRO_0000367114"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..415
FT /note="Heterogeneous nuclear ribonucleoprotein F, N-
FT terminally processed"
FT /id="PRO_0000081852"
FT DOMAIN 13..85
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 111..188
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 289..366
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 81..86
FT /note="Interaction with RNA"
FT REGION 179..184
FT /note="Interaction with RNA"
FT REGION 355..360
FT /note="Interaction with RNA"
FT SITE 16
FT /note="Interaction with RNA"
FT SITE 20
FT /note="Interaction with RNA"
FT SITE 52
FT /note="Interaction with RNA"
FT SITE 75
FT /note="Interaction with RNA"
FT SITE 116
FT /note="Interaction with RNA"
FT SITE 120
FT /note="Interaction with RNA"
FT SITE 150
FT /note="Interaction with RNA"
FT SITE 173
FT /note="Interaction with RNA"
FT SITE 294
FT /note="Interaction with RNA"
FT SITE 298
FT /note="Interaction with RNA"
FT SITE 326
FT /note="Interaction with RNA"
FT SITE 349
FT /note="Interaction with RNA"
FT MOD_RES 1
FT /note="N-acetylmethionine; in Heterogeneous nuclear
FT ribonucleoprotein F; alternate"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylmethionine; in Heterogeneous nuclear
FT ribonucleoprotein F, N-terminally processed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q794E4"
FT MOD_RES 200
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2X1"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 224
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15161980"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 87
FT /note="K -> R (in dbSNP:rs17851426)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027999"
FT MUTAGEN 20
FT /note="W->A: Loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:20526337"
FT MUTAGEN 84
FT /note="E->A: Loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:20526337"
FT MUTAGEN 116
FT /note="R->A: Decreases affinity for RNA oligonucleotide
FT 100-fold."
FT /evidence="ECO:0000269|PubMed:20526337"
FT MUTAGEN 120
FT /note="F->A: Little disruption of binding RNA. Decreases
FT affinity for RNA oligonucleotide 100-fold. Abrogates RNA-
FT binding; when associated with A-180."
FT /evidence="ECO:0000269|PubMed:16885237,
FT ECO:0000269|PubMed:20526337"
FT MUTAGEN 150
FT /note="K->A: No effect on affinity for RNA
FT oligonucleotide."
FT /evidence="ECO:0000269|PubMed:20526337"
FT MUTAGEN 156
FT /note="F->A: Drastically effects folding of RRM2."
FT /evidence="ECO:0000269|PubMed:16885237"
FT MUTAGEN 173
FT /note="K->A: Minimal effect on affinity for RNA
FT oligonucleotide."
FT /evidence="ECO:0000269|PubMed:20526337"
FT MUTAGEN 178
FT /note="H->A: Little disruption of binding RNA."
FT /evidence="ECO:0000269|PubMed:16885237"
FT MUTAGEN 179
FT /note="R->A: Decreases affinity for RNA oligonucleotide
FT 100-fold."
FT /evidence="ECO:0000269|PubMed:20526337"
FT MUTAGEN 180
FT /note="Y->A: Decreases affinity for RNA oligonucleotide 10-
FT fold. Abrogates RNA-binding; when associated with A-120."
FT /evidence="ECO:0000269|PubMed:16885237,
FT ECO:0000269|PubMed:20526337"
FT MUTAGEN 182
FT /note="E->A: Decreases affinity for RNA oligonucleotide
FT 100-fold."
FT /evidence="ECO:0000269|PubMed:20526337"
FT MUTAGEN 184
FT /note="F->A: Minimal effect on affinity for RNA
FT oligonucleotide."
FT /evidence="ECO:0000269|PubMed:20526337"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:2HGL"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:2HGL"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:2HGL"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2HGL"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2HGL"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2HGL"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2HGL"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:2HGL"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2HGL"
FT STRAND 75..87
FT /evidence="ECO:0007829|PDB:2HGL"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:2HGL"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2HGM"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2HGM"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:2HGM"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2HGM"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:2HGM"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:2HGM"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:2HGM"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:2HGM"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:2HGM"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:2KG0"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2HGM"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:2HGM"
FT STRAND 284..294
FT /evidence="ECO:0007829|PDB:2KG1"
FT HELIX 302..309
FT /evidence="ECO:0007829|PDB:2HGN"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:2HGN"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:2HGN"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:2HGN"
FT HELIX 337..344
FT /evidence="ECO:0007829|PDB:2HGN"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:2HGN"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:2KG1"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:2KG1"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:2KG1"
SQ SEQUENCE 415 AA; 45672 MW; D14E170631FB1F31 CRC64;
MMLGPEGGEG FVVKLRGLPW SCSVEDVQNF LSDCTIHDGA AGVHFIYTRE GRQSGEAFVE
LGSEDDVKMA LKKDRESMGH RYIEVFKSHR TEMDWVLKHS GPNSADSAND GFVRLRGLPF
GCTKEEIVQF FSGLEIVPNG ITLPVDPEGK ITGEAFVQFA SQELAEKALG KHKERIGHRY
IEVFKSSQEE VRSYSDPPLK FMSVQRPGPY DRPGTARRYI GIVKQAGLER MRPGAYSTGY
GGYEEYSGLS DGYGFTTDLF GRDLSYCLSG MYDHRYGDSE FTVQSTTGHC VHMRGLPYKA
TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHEE AVAAMSKDRA NMQHRYIELF
LNSTTGASNG AYSSQVMQGM GVSAAQATYS GLESQSVSGC YGAGYSGQNS MGGYD
