ID   NU133_HUMAN             Reviewed;        1156 AA.
AC   Q8WUM0; B2RAZ8; Q5T8N0; Q9H9W2; Q9NV71; Q9NVC4;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Nuclear pore complex protein Nup133;
DE   AltName: Full=133 kDa nucleoporin;
DE   AltName: Full=Nucleoporin Nup133;
GN   Name=NUP133;
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 {ECO:0000312|EMBL:AAH20107.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4] {ECO:0000305}
RP   IDENTIFICATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=11564755; DOI=10.1083/jcb.200101081;
RA   Belgareh N., Rabut G., Bai S.W., van Overbeek M., Beaudouin J., Daigle N.,
RA   Zatsepina O.V., Pasteau F., Labas V., Fromont-Racine M., Ellenberg J.,
RA   Doye V.;
RT   "An evolutionarily conserved NPC subcomplex, which redistributes in part to
RT   kinetochores in mammalian cells.";
RL   J. Cell Biol. 154:1147-1160(2001).
RN   [5] {ECO:0000305}
RP   IDENTIFICATION, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=11684705; DOI=10.1083/jcb.200108007;
RA   Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J.;
RT   "Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA
RT   export.";
RL   J. Cell Biol. 155:339-354(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-50, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-28; SER-41; SER-45
RP   AND SER-50, AND 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   [11]
RP   IDENTIFICATION BY MASS 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-50 AND SER-480, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-7; SER-27; THR-28; SER-45 AND SER-50, AND IDENTIFICATION
RP   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   [14]
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   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-15; SER-27; THR-28;
RP   SER-45; SER-50; SER-72; SER-131; SER-755 AND SER-1133, AND IDENTIFICATION
RP   BY 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   [18]
RP   IDENTIFICATION BY 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   [19]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-17, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [20]
RP   INTERACTION WITH NUP107.
RX   PubMed=26411495; DOI=10.1016/j.ajhg.2015.08.013;
RA   Miyake N., Tsukaguchi H., Koshimizu E., Shono A., Matsunaga S., Shiina M.,
RA   Mimura Y., Imamura S., Hirose T., Okudela K., Nozu K., Akioka Y.,
RA   Hattori M., Yoshikawa N., Kitamura A., Cheong H.I., Kagami S.,
RA   Yamashita M., Fujita A., Miyatake S., Tsurusaki Y., Nakashima M.,
RA   Saitsu H., Ohashi K., Imamoto N., Ryo A., Ogata K., Iijima K.,
RA   Matsumoto N.;
RT   "Biallelic mutations in nuclear pore complex subunit NUP107 cause early-
RT   childhood-onset steroid-resistant nephrotic syndrome.";
RL   Am. J. Hum. Genet. 97:555-566(2015).
RN   [21]
RP   TISSUE SPECIFICITY, AND INVOLVEMENT IN GAMOS8.
RX   PubMed=30427554; DOI=10.1002/ana.25370;
RA   Fujita A., Tsukaguchi H., Koshimizu E., Nakazato H., Itoh K., Kuraoka S.,
RA   Komohara Y., Shiina M., Nakamura S., Kitajima M., Tsurusaki Y.,
RA   Miyatake S., Ogata K., Iijima K., Matsumoto N., Miyake N.;
RT   "Homozygous splicing mutation in NUP133 causes Galloway-Mowat syndrome.";
RL   Ann. Neurol. 84:814-828(2018).
RN   [22]
RP   ERRATUM OF PUBMED:30427554.
RX   PubMed=30817857; DOI=10.1002/ana.25427;
RA   Fujita A., Tsukaguchi H., Koshimizu E., Nakazato H., Itoh K., Kuraoka S.,
RA   Komohara Y., Shiina M., Nakamura S., Kitajima M., Tsurusaki Y.,
RA   Miyatake S., Ogata K., Iijima K., Matsumoto N., Miyake N.;
RL   Ann. Neurol. 85:462-463(2019).
RN   [23]
RP   FUNCTION, INTERACTION WITH NUP107, INVOLVEMENT IN NPHS18, VARIANTS NPHS18
RP   GLY-231; ARG-974 AND SER-1055, AND CHARACTERIZATION OF VARIANTS NPHS18
RP   GLY-231; ARG-974 AND SER-1055.
RX   PubMed=30179222; DOI=10.1172/jci98688;
RA   Braun D.A., Lovric S., Schapiro D., Schneider R., Marquez J., Asif M.,
RA   Hussain M.S., Daga A., Widmeier E., Rao J., Ashraf S., Tan W., Lusk C.P.,
RA   Kolb A., Jobst-Schwan T., Schmidt J.M., Hoogstraten C.A., Eddy K.,
RA   Kitzler T.M., Shril S., Moawia A., Schrage K., Khayyat A.I.A., Lawson J.A.,
RA   Gee H.Y., Warejko J.K., Hermle T., Majmundar A.J., Hugo H., Budde B.,
RA   Motameny S., Altmueller J., Noegel A.A., Fathy H.M., Gale D.P.,
RA   Waseem S.S., Khan A., Kerecuk L., Hashmi S., Mohebbi N., Ettenger R.,
RA   Serdaroglu E., Alhasan K.A., Hashem M., Goncalves S., Ariceta G.,
RA   Ubetagoyena M., Antonin W., Baig S.M., Alkuraya F.S., Shen Q., Xu H.,
RA   Antignac C., Lifton R.P., Mane S., Nuernberg P., Khokha M.K.,
RA   Hildebrandt F.;
RT   "Mutations in multiple components of the nuclear pore complex cause
RT   nephrotic syndrome.";
RL   J. Clin. Invest. 128:4313-4328(2018).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 67-514.
RX   PubMed=15557116; DOI=10.1083/jcb.200408109;
RA   Berke I.C., Boehmer T., Blobel G., Schwartz T.U.;
RT   "Structural and functional analysis of Nup133 domains reveals modular
RT   building blocks of the nuclear pore complex.";
RL   J. Cell Biol. 167:591-597(2004).
RN   [25]
RP   VARIANTS [LARGE SCALE ANALYSIS] VAL-326 AND ARG-448.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Involved in poly(A)+ RNA transport. Involved in nephrogenesis
CC       (PubMed:30179222). {ECO:0000269|PubMed:11684705,
CC       ECO:0000269|PubMed:30179222}.
CC   -!- SUBUNIT: Forms part of the Nup160 subcomplex in the nuclear pore which
CC       is composed of NUP160, NUP133, NUP107 and Nup96. This complex plays a
CC       role in RNA export and in tethering Nup98 and NUP153 to the nucleus.
CC       {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705,
CC       ECO:0000269|PubMed:26411495, ECO:0000269|PubMed:30179222}.
CC   -!- INTERACTION:
CC       Q8WUM0; P49454: CENPF; NbExp=2; IntAct=EBI-295695, EBI-968343;
CC       Q8WUM0; Q5S007: LRRK2; NbExp=4; IntAct=EBI-295695, EBI-5323863;
CC       Q8WUM0; P57740: NUP107; NbExp=14; IntAct=EBI-295695, EBI-295687;
CC       Q8WUM0; Q9BW27: NUP85; NbExp=2; IntAct=EBI-295695, EBI-716392;
CC       Q8WUM0; P46673: NUP85; Xeno; NbExp=5; IntAct=EBI-295695, EBI-12345;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC       {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}. Chromosome,
CC       centromere, kinetochore {ECO:0000269|PubMed:11564755}. Note=Located on
CC       both the cytoplasmic and nuclear sides of the nuclear pore
CC       (PubMed:11564755). During mitosis, localizes to the kinetochores
CC       (PubMed:11564755). {ECO:0000269|PubMed:11564755,
CC       ECO:0000269|PubMed:11684705}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues.
CC       Expressed in the brain and kidney. {ECO:0000269|PubMed:30427554}.
CC   -!- DISEASE: Nephrotic syndrome 18 (NPHS18) [MIM:618177]: A form of
CC       nephrotic syndrome, a renal disease clinically characterized by severe
CC       proteinuria, resulting in complications such as hypoalbuminemia,
CC       hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC       changes such as focal segmental glomerulosclerosis and diffuse
CC       mesangial proliferation. Some affected individuals have an inherited
CC       steroid-resistant form that progresses to end-stage renal failure.
CC       NPHS18 is an autosomal recessive, steroid-resistant progressive form
CC       with onset in the first decade of life. {ECO:0000269|PubMed:30179222}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- DISEASE: Galloway-Mowat syndrome 8 (GAMOS8) [MIM:618349]: A form of
CC       Galloway-Mowat syndrome, a severe renal-neurological disease
CC       characterized by early-onset nephrotic syndrome associated with
CC       microcephaly, central nervous system abnormalities, developmental
CC       delays, and a propensity for seizures. Brain anomalies include gyration
CC       defects ranging from lissencephaly to pachygyria and polymicrogyria,
CC       and cerebellar hypoplasia. Most patients show facial dysmorphism
CC       characterized by a small, narrow forehead, large/floppy ears, deep-set
CC       eyes, hypertelorism and micrognathia. Additional variable features are
CC       visual impairment and arachnodactyly. Most patients die in early
CC       childhood. GAMOS8 inheritance is autosomal recessive.
CC       {ECO:0000269|PubMed:30427554}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the nucleoporin Nup133 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA91885.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB14106.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK001676; BAA91829.1; -; mRNA.
DR   EMBL; AK001754; BAA91885.1; ALT_INIT; mRNA.
DR   EMBL; AK022572; BAB14106.1; ALT_INIT; mRNA.
DR   EMBL; AK314431; BAG37045.1; -; mRNA.
DR   EMBL; AL121990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL160004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020107; AAH20107.1; -; mRNA.
DR   CCDS; CCDS1579.1; -.
DR   RefSeq; NP_060700.2; NM_018230.2.
DR   PDB; 1XKS; X-ray; 2.35 A; A=67-514.
DR   PDB; 3CQC; X-ray; 2.53 A; B=935-1156.
DR   PDB; 3CQG; X-ray; 3.00 A; B=934-1156.
DR   PDB; 3I4R; X-ray; 3.53 A; B=517-1156.
DR   PDB; 5A9Q; EM; 23.00 A; 3/C/L/U=1-1156.
DR   PDB; 7PEQ; EM; 35.00 A; AC/BC/CC/DC=1-1156.
DR   PDB; 7R5J; EM; 50.00 A; K0/K1/K2/K3=1-1156.
DR   PDB; 7R5K; EM; 12.00 A; K0/K1/K2/K3=1-1156.
DR   PDBsum; 1XKS; -.
DR   PDBsum; 3CQC; -.
DR   PDBsum; 3CQG; -.
DR   PDBsum; 3I4R; -.
DR   PDBsum; 5A9Q; -.
DR   PDBsum; 7PEQ; -.
DR   PDBsum; 7R5J; -.
DR   PDBsum; 7R5K; -.
DR   AlphaFoldDB; Q8WUM0; -.
DR   EMDB; EMD-14321; -.
DR   EMDB; EMD-14322; -.
DR   SMR; Q8WUM0; -.
DR   BioGRID; 120864; 185.
DR   ComplexPortal; CPX-873; Nuclear pore complex.
DR   CORUM; Q8WUM0; -.
DR   IntAct; Q8WUM0; 72.
DR   MINT; Q8WUM0; -.
DR   STRING; 9606.ENSP00000261396; -.
DR   TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR   GlyGen; Q8WUM0; 5 sites, 1 O-linked glycan (5 sites).
DR   iPTMnet; Q8WUM0; -.
DR   PhosphoSitePlus; Q8WUM0; -.
DR   SwissPalm; Q8WUM0; -.
DR   BioMuta; NUP133; -.
DR   DMDM; 143811430; -.
DR   EPD; Q8WUM0; -.
DR   jPOST; Q8WUM0; -.
DR   MassIVE; Q8WUM0; -.
DR   MaxQB; Q8WUM0; -.
DR   PaxDb; 9606-ENSP00000261396; -.
DR   PeptideAtlas; Q8WUM0; -.
DR   ProteomicsDB; 74694; -.
DR   Pumba; Q8WUM0; -.
DR   Antibodypedia; 34676; 163 antibodies from 28 providers.
DR   DNASU; 55746; -.
DR   Ensembl; ENST00000261396.6; ENSP00000261396.3; ENSG00000069248.12.
DR   GeneID; 55746; -.
DR   KEGG; hsa:55746; -.
DR   MANE-Select; ENST00000261396.6; ENSP00000261396.3; NM_018230.3; NP_060700.2.
DR   UCSC; uc001htn.4; human.
DR   AGR; HGNC:18016; -.
DR   CTD; 55746; -.
DR   DisGeNET; 55746; -.
DR   GeneCards; NUP133; -.
DR   HGNC; HGNC:18016; NUP133.
DR   HPA; ENSG00000069248; Low tissue specificity.
DR   MalaCards; NUP133; -.
DR   MIM; 607613; gene.
DR   MIM; 618177; phenotype.
DR   MIM; 618349; phenotype.
DR   neXtProt; NX_Q8WUM0; -.
DR   OpenTargets; ENSG00000069248; -.
DR   Orphanet; 2065; Galloway-Mowat syndrome.
DR   Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR   PharmGKB; PA31847; -.
DR   VEuPathDB; HostDB:ENSG00000069248; -.
DR   eggNOG; KOG4121; Eukaryota.
DR   GeneTree; ENSGT00390000011529; -.
DR   HOGENOM; CLU_008593_0_0_1; -.
DR   InParanoid; Q8WUM0; -.
DR   OMA; RYTLHHK; -.
DR   OrthoDB; 4246256at2759; -.
DR   PhylomeDB; Q8WUM0; -.
DR   TreeFam; TF106141; -.
DR   PathwayCommons; Q8WUM0; -.
DR   Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR   Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR   Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR   Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR   Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR   Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR   Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR   Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR   Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR   Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR   Reactome; R-HSA-191859; snRNP Assembly.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR   Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR   Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR   Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR   Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR   Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR   Reactome; R-HSA-68877; Mitotic Prometaphase.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Reactome; R-HSA-9610379; HCMV Late Events.
DR   Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR   Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR   SignaLink; Q8WUM0; -.
DR   SIGNOR; Q8WUM0; -.
DR   BioGRID-ORCS; 55746; 799 hits in 1160 CRISPR screens.
DR   ChiTaRS; NUP133; human.
DR   EvolutionaryTrace; Q8WUM0; -.
DR   GeneWiki; NUP133; -.
DR   GenomeRNAi; 55746; -.
DR   Pharos; Q8WUM0; Tbio.
DR   PRO; PR:Q8WUM0; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q8WUM0; Protein.
DR   Bgee; ENSG00000069248; Expressed in secondary oocyte and 209 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR   GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IDA:UniProtKB.
DR   GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR   GO; GO:0072006; P:nephron development; IMP:UniProtKB.
DR   GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR   GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR   GO; GO:0006999; P:nuclear pore organization; IMP:UniProtKB.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal.
DR   GO; GO:0048339; P:paraxial mesoderm development; IEA:Ensembl.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR   GO; GO:0061053; P:somite development; IEA:Ensembl.
DR   GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR   DisProt; DP02164; -.
DR   Gene3D; 1.20.58.1380; -; 1.
DR   Gene3D; 1.25.40.700; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   IDEAL; IID00219; -.
DR   InterPro; IPR007187; Nucleoporin_Nup133/Nup155_C.
DR   InterPro; IPR037624; Nup133-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR13405; NUCLEAR PORE COMPLEX PROTEIN NUP133; 1.
DR   PANTHER; PTHR13405:SF11; NUCLEAR PORE COMPLEX PROTEIN NUP133; 1.
DR   Pfam; PF03177; Nucleoporin_C; 1.
DR   SUPFAM; SSF117289; Nucleoporin domain; 1.
DR   Genevisible; Q8WUM0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Centromere; Chromosome; Disease variant;
KW   Epilepsy; Intellectual disability; Kinetochore; Methylation;
KW   mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Translocation; Transport.
FT   CHAIN           1..1156
FT                   /note="Nuclear pore complex protein Nup133"
FT                   /id="PRO_0000204838"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         17
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         28
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         30
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0G9"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         480
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         489
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0G9"
FT   MOD_RES         493
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0G9"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0G9"
FT   MOD_RES         755
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         787
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0G9"
FT   MOD_RES         1133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         106
FT                   /note="T -> P (in dbSNP:rs428231)"
FT                   /id="VAR_030829"
FT   VARIANT         231
FT                   /note="R -> G (in NPHS18; decreased function in
FT                   nephrogenesis; unable to fully rescue morpholino-induced
FT                   nephrogenesis defects in Xenopus; dbSNP:rs1558108130)"
FT                   /evidence="ECO:0000269|PubMed:30179222"
FT                   /id="VAR_081359"
FT   VARIANT         294
FT                   /note="I -> V (in dbSNP:rs11805194)"
FT                   /id="VAR_030830"
FT   VARIANT         326
FT                   /note="G -> V (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035854"
FT   VARIANT         406
FT                   /note="Q -> R (in dbSNP:rs1065674)"
FT                   /id="VAR_030831"
FT   VARIANT         448
FT                   /note="G -> R (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035855"
FT   VARIANT         974
FT                   /note="S -> R (in NPHS18; loss of function in
FT                   nephrogenesis; unable to rescue morpholino-induced
FT                   nephrogenesis defects in Xenopus; decreased interaction
FT                   with NUP107; dbSNP:rs1558091788)"
FT                   /evidence="ECO:0000269|PubMed:30179222"
FT                   /id="VAR_081360"
FT   VARIANT         1055
FT                   /note="L -> S (in NPHS18; loss of function in
FT                   nephrogenesis; unable to rescue morpholino-induced
FT                   nephrogenesis defects in Xenopus; dbSNP:rs376476266)"
FT                   /evidence="ECO:0000269|PubMed:30179222"
FT                   /id="VAR_081361"
FT   CONFLICT        61
FT                   /note="R -> G (in Ref. 1; BAA91829)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="P -> S (in Ref. 1; BAA91829)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        345
FT                   /note="L -> F (in Ref. 3; AAH20107)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        626
FT                   /note="S -> N (in Ref. 1; BAA91829)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        928
FT                   /note="F -> L (in Ref. 1; BAA91885)"
FT                   /evidence="ECO:0000305"
FT   STRAND          77..83
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   HELIX           90..98
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          113..119
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          122..127
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   HELIX           134..136
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          139..143
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          156..160
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          172..178
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          183..188
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          197..200
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          209..215
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   TURN            216..218
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          219..224
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          229..234
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          240..244
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          274..280
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   TURN            281..284
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          285..299
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          304..311
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   HELIX           312..325
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   HELIX           331..335
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          339..348
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          351..359
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          363..365
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          367..375
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          386..390
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   HELIX           400..402
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          406..408
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          412..420
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          422..429
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          440..443
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   HELIX           446..448
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          451..457
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          460..465
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   TURN            466..468
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   STRAND          469..475
FT                   /evidence="ECO:0007829|PDB:1XKS"
FT   HELIX           936..942
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   HELIX           946..959
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   HELIX           964..980
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   HELIX           985..1006
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   HELIX           1012..1015
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   STRAND          1020..1023
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   HELIX           1028..1034
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   HELIX           1045..1051
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   TURN            1052..1057
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   HELIX           1067..1079
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   HELIX           1096..1102
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   HELIX           1125..1128
FT                   /evidence="ECO:0007829|PDB:3CQC"
FT   HELIX           1142..1155
FT                   /evidence="ECO:0007829|PDB:3CQC"
SQ   SEQUENCE   1156 AA;  128979 MW;  78B733E353824577 CRC64;
     MFPAAPSPRT PGTGSRRGPL AGLGPGSTPR TASRKGLPLG SAVSSPVLFS PVGRRSSLSS
     RGTPTRMFPH HSITESVNYD VKTFGSSLPV KVMEALTLAE VDDQLTINID EGGWACLVCK
     EKLIIWKIAL SPITKLSVCK ELQLPPSDFH WSADLVALSY SSPSGEAHST QAVAVMVATR
     EGSIRYWPSL AGEDTYTEAF VDSGGDKTYS FLTAVQGGSF ILSSSGSQLI RLIPESSGKI
     HQHILPQGQG MLSGIGRKVS SLFGILSPSS DLTLSSVLWD RERSSFYSLT SSNISKWELD
     DSSEKHAYSW DINRALKENI TDAIWGSESN YEAIKEGVNI RYLDLKQNCD GLVILAAAWH
     SADNPCLIYY SLITIEDNGC QMSDAVTVEV TQYNPPFQSE DLILCQLTVP NFSNQTAYLY
     NESAVYVCST GTGKFSLPQE KIVFNAQGDS VLGAGACGGV PIIFSRNSGL VSITSRENVS
     ILAEDLEGSL ASSVAGPNSE SMIFETTTKN ETIAQEDKIK LLKAAFLQYC RKDLGHAQMV
     VDELFSSHSD LDSDSELDRA VTQISVDLMD DYPASDPRWA ESVPEEAPGF SNTSLIILHQ
     LEDKMKAHSF LMDFIHQVGL FGRLGSFPVR GTPMATRLLL CEHAEKLSAA IVLKNHHSRL
     SDLVNTAILI ALNKREYEIP SNLTPADVFF REVSQVDTIC ECLLEHEEQV LRDAPMDSIE
     WAEVVINVNN ILKDMLQAAS HYRQNRNSLY RREESLEKEP EYVPWTATSG PGGIRTVIIR
     QHEIVLKVAY PQADSNLRNI VTEQLVALID CFLDGYVSQL KSVDKSSNRE RYDNLEMEYL
     QKRSDLLSPL LSLGQYLWAA SLAEKYCDFD ILVQMCEQTD NQSRLQRYMT QFADQNFSDF
     LFRWYLEKGK RGKLLSQPIS QHGQLANFLQ AHEHLSWLHE INSQELEKAH ATLLGLANME
     TRYFAKKKTL LGLSKLAALA SDFSEDMLQE KIEEMAEQER FLLHQETLPE QLLAEKQLNL
     SAMPVLTAPQ LIGLYICEEN RRANEYDFKK ALDLLEYIDE EEDININDLK LEILCKALQR
     DNWSSSDGKD DPIEVSKDSI FVKILQKLLK DGIQLSEYLP EVKDLLQADQ LGSLKSNPYF
     EFVLKANYEY YVQGQI
//