NU133_HUMAN
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 03-AUG-2022, entry version 191.
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 PDBsum; 1XKS; -.
DR PDBsum; 3CQC; -.
DR PDBsum; 3CQG; -.
DR PDBsum; 3I4R; -.
DR PDBsum; 5A9Q; -.
DR PDBsum; 7PEQ; -.
DR AlphaFoldDB; Q8WUM0; -.
DR SMR; Q8WUM0; -.
DR BioGRID; 120864; 139.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR CORUM; Q8WUM0; -.
DR IntAct; Q8WUM0; 70.
DR MINT; Q8WUM0; -.
DR STRING; 9606.ENSP00000261396; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q8WUM0; 1 site, 1 O-linked glycan (1 site).
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; Q8WUM0; -.
DR PeptideAtlas; Q8WUM0; -.
DR PRIDE; Q8WUM0; -.
DR ProteomicsDB; 74694; -.
DR Antibodypedia; 34676; 140 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 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; 51227at2759; -.
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; 771 hits in 1081 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 207 other tissues.
DR Genevisible; Q8WUM0; HS.
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; IC: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; 2.130.10.10; -; 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; PTHR13405; 1.
DR Pfam; PF03177; Nucleoporin_C; 1.
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
