SEPT2_HUMAN
ID SEPT2_HUMAN Reviewed; 361 AA.
AC Q15019; B4DGE8; Q14132; Q53QU3; Q8IUK9; Q96CB0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Septin-2;
DE AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 5;
DE Short=NEDD-5;
GN Name=SEPTIN2 {ECO:0000312|HGNC:HGNC:7729};
GN Synonyms=DIFF6, KIAA0158, NEDD5, SEPT2;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8697812; DOI=10.1159/000134343;
RA Mori T., Miura K., Fujiwara T., Shin S., Inazawa J., Nakamura Y.;
RT "Isolation and mapping of a human gene (DIFF6) homologous to yeast CDC3,
RT CDC10, CDC11, and CDC12, and mouse Diff6.";
RL Cytogenet. Cell Genet. 73:224-227(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hu G.;
RT "Human homolog of mouse Nedd5 mRNA.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 51-66, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP PHOSPHORYLATION AT SER-218.
RX PubMed=15150837; DOI=10.1002/rcm.1453;
RA She Y.M., Huang Y.W., Zhang L., Trimble W.S.;
RT "Septin 2 phosphorylation: theoretical and mass spectrometric evidence for
RT the existence of a single phosphorylation site in vivo.";
RL Rapid Commun. Mass Spectrom. 18:1123-1130(2004).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=15915442; DOI=10.1002/path.1789;
RA Hall P.A., Jung K., Hillan K.J., Russell S.E.H.;
RT "Expression profiling the human septin gene family.";
RL J. Pathol. 206:269-278(2005).
RN [10]
RP INTERACTION WITH MAP4, AND COORDINATED EXPRESSION WITH SEPTIN2 AND SEPTIN7.
RX PubMed=16093351; DOI=10.1091/mbc.e05-03-0267;
RA Kremer B.E., Haystead T., Macara I.G.;
RT "Mammalian septins regulate microtubule stability through interaction with
RT the microtubule-binding protein MAP4.";
RL Mol. Biol. Cell 16:4648-4659(2005).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15774761; DOI=10.1126/science.1106823;
RA Spiliotis E.T., Kinoshita M., Nelson W.J.;
RT "A mitotic septin scaffold required for mammalian chromosome congression
RT and segregation.";
RL Science 307:1781-1785(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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 [13]
RP INTERACTION WITH SEPTIN6 AND SEPTIN7.
RX PubMed=16914550; DOI=10.1074/jbc.m605179200;
RA Low C., Macara I.G.;
RT "Structural analysis of septin 2, 6, and 7 complexes.";
RL J. Biol. Chem. 281:30697-30706(2006).
RN [14]
RP FUNCTION.
RX PubMed=17803907; DOI=10.1016/j.cell.2007.06.053;
RA Kremer B.E., Adang L.A., Macara I.G.;
RT "Septins regulate actin organization and cell-cycle arrest through nuclear
RT accumulation of NCK mediated by SOCS7.";
RL Cell 130:837-850(2007).
RN [15]
RP FUNCTION, AND COLOCALIZATION WITH POLYGLUTAMYLATED TUBULIN.
RX PubMed=18209106; DOI=10.1083/jcb.200710039;
RA Spiliotis E.T., Hunt S.J., Hu Q., Kinoshita M., Nelson W.J.;
RT "Epithelial polarity requires septin coupling of vesicle transport to
RT polyglutamylated microtubules.";
RL J. Cell Biol. 180:295-303(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [21]
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 [22]
RP PHOSPHORYLATION AT SER-218, MUTAGENESIS OF SER-218, AND TISSUE SPECIFICITY.
RX PubMed=19165576; DOI=10.1007/s11010-008-0020-2;
RA Yu W., Ding X., Chen F., Liu M., Shen S., Gu X., Yu L.;
RT "The phosphorylation of SEPT2 on Ser218 by casein kinase 2 is important to
RT hepatoma carcinoma cell proliferation.";
RL Mol. Cell. Biochem. 325:61-67(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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 [24]
RP INTERACTION WITH SEPTIN9, AND ROLE IN BACTERIAL INFECTION.
RX PubMed=19145258; DOI=10.1371/journal.pone.0004196;
RA Mostowy S., Nam Tham T., Danckaert A., Guadagnini S., Boisson-Dupuis S.,
RA Pizarro-Cerda J., Cossart P.;
RT "Septins regulate bacterial entry into host cells.";
RL PLoS ONE 4:E4196-E4196(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP 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 [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-190, 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP 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 [28]
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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211 AND SER-218, AND
RP IDENTIFICATION 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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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 [32]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25588830; DOI=10.1242/jcs.158998;
RA Kuo Y.C., Shen Y.R., Chen H.I., Lin Y.H., Wang Y.Y., Chen Y.R., Wang C.Y.,
RA Kuo P.L.;
RT "SEPT12 orchestrates the formation of mammalian sperm annulus by organizing
RT core octomeric complexes with other SEPT proteins.";
RL J. Cell Sci. 128:923-934(2015).
RN [33]
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 [34]
RP INTERACTION WITH DZIP1L.
RX PubMed=28530676; DOI=10.1038/ng.3871;
RA Lu H., Galeano M.C.R., Ott E., Kaeslin G., Kausalya P.J., Kramer C.,
RA Ortiz-Bruechle N., Hilger N., Metzis V., Hiersche M., Tay S.Y.,
RA Tunningley R., Vij S., Courtney A.D., Whittle B., Wuehl E., Vester U.,
RA Hartleben B., Neuber S., Frank V., Little M.H., Epting D.,
RA Papathanasiou P., Perkins A.C., Wright G.D., Hunziker W., Gee H.Y.,
RA Otto E.A., Zerres K., Hildebrandt F., Roy S., Wicking C., Bergmann C.;
RT "Mutations in DZIP1L, which encodes a ciliary-transition-zone protein,
RT cause autosomal recessive polycystic kidney disease.";
RL Nat. Genet. 49:1025-1034(2017).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-315 IN COMPLEXES WITH GTP,
RP ELECTRON MICROSCOPY, MUTAGENESIS OF PHE-156; TRP-260 AND HIS-270, AND
RP SUBUNIT.
RX PubMed=17637674; DOI=10.1038/nature06052;
RA Sirajuddin M., Farkasovsky M., Hauer F., Kuehlmann D., Macara I.G.,
RA Weyand M., Stark H., Wittinghofer A.;
RT "Structural insight into filament formation by mammalian septins.";
RL Nature 449:311-315(2007).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-320 IN COMPLEX WITH GDP, AND
RP SUBUNIT.
RG Structural genomics consortium (SGC);
RT "Human septin 2 in complex with GDP.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. Forms a filamentous
CC structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the
CC sperm annulus which is required for the structural integrity and
CC motility of the sperm tail during postmeiotic differentiation
CC (PubMed:25588830). Required for normal organization of the actin
CC cytoskeleton. Plays a role in the biogenesis of polarized columnar-
CC shaped epithelium by maintaining polyglutamylated microtubules, thus
CC facilitating efficient vesicle transport, and by impeding MAP4 binding
CC to tubulin. Required for the progression through mitosis. Forms a
CC scaffold at the midplane of the mitotic splindle required to maintain
CC CENPE localization at kinetochores and consequently chromosome
CC congression. During anaphase, may be required for chromosome
CC segregation and spindle elongation. Plays a role in ciliogenesis and
CC collective cell movements. In cilia, required for the integrity of the
CC diffusion barrier at the base of the primary cilium that prevents
CC diffusion of transmembrane proteins between the cilia and plasma
CC membranes: probably acts by regulating the assembly of the tectonic-
CC like complex (also named B9 complex) by localizing TMEM231 protein. May
CC play a role in the internalization of 2 intracellular microbial
CC pathogens, Listeria monocytogenes and Shigella flexneri.
CC {ECO:0000269|PubMed:15774761, ECO:0000269|PubMed:17803907,
CC ECO:0000269|PubMed:18209106, ECO:0000269|PubMed:19145258,
CC ECO:0000305|PubMed:25588830}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and associate with cellular membranes, actin
CC filaments and microtubules (PubMed:17637674, PubMed:25588830, Ref.36).
CC GTPase activity is required for filament formation. Filaments are
CC assembled from asymmetrical heterotrimers, composed of SEPTIN2, SEPTIN6
CC and SEPTIN7 that associate head-to-head to form a hexameric unit
CC (PubMed:16093351, PubMed:16914550). Interaction between SEPTIN2 and
CC SEPTIN7 seems indirect. Interacts with SEPTIN5 (By similarity).
CC Interaction with SEPTIN4 not detected (By similarity). Interacts with
CC SEPTIN9 (PubMed:19145258). Component of a septin core octomeric complex
CC consisting of SEPTIN12, SEPTIN7, SEPTIN6 and SEPTIN2 or SEPTIN4 in the
CC order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm
CC annulus (PubMed:16093351, PubMed:16914550). Interacts with MAP4.
CC Interacts with DZIP1L (PubMed:28530676). {ECO:0000250|UniProtKB:P42208,
CC ECO:0000269|PubMed:16093351, ECO:0000269|PubMed:16914550,
CC ECO:0000269|PubMed:17637674, ECO:0000269|PubMed:19145258,
CC ECO:0000269|PubMed:25588830, ECO:0000269|PubMed:28530676,
CC ECO:0000269|Ref.36}.
CC -!- INTERACTION:
CC Q15019; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-741220, EBI-742388;
CC Q15019; Q8IYM1: SEPTIN12; NbExp=7; IntAct=EBI-741220, EBI-2585067;
CC Q15019; Q99719: SEPTIN5; NbExp=4; IntAct=EBI-741220, EBI-373345;
CC Q15019; Q14141: SEPTIN6; NbExp=11; IntAct=EBI-741220, EBI-745901;
CC Q15019-1; Q15019-1: SEPTIN2; NbExp=2; IntAct=EBI-5279816, EBI-5279816;
CC Q15019-2; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-10983222, EBI-357085;
CC Q15019-3; P05067: APP; NbExp=3; IntAct=EBI-11525407, EBI-77613;
CC Q15019-3; Q8N8Y2: ATP6V0D2; NbExp=3; IntAct=EBI-11525407, EBI-3923949;
CC Q15019-3; A0A0A0MR97: BAZ2B; NbExp=3; IntAct=EBI-11525407, EBI-11985607;
CC Q15019-3; Q99719: SEPTIN5; NbExp=7; IntAct=EBI-11525407, EBI-373345;
CC Q15019-3; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-11525407, EBI-12018146;
CC Q15019-3; O14656-2: TOR1A; NbExp=3; IntAct=EBI-11525407, EBI-25847109;
CC Q15019-3; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-11525407, EBI-607755;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15774761}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15774761}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:15774761}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:15774761}. Cleavage furrow
CC {ECO:0000269|PubMed:15774761}. Midbody {ECO:0000269|PubMed:15774761}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:15774761}. Cell projection,
CC cilium membrane {ECO:0000250}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:25588830}. Note=In metaphase cells, localized
CC within the microtubule spindle. At the metaphase plate, in close
CC apposition to the kinetochores of the congressed chromosomes. In cells
CC undergoing cytokinesis, localized to the midbody, the ingressing
CC cleavage furrow, and the central spindle. During bacterial infection,
CC displays a collar shape structure next to actin at the pole of invading
CC bacteria. In epithelial cells, colocalizes with polyglutamylated
CC tubulin around the trans-Golgi network, as well as juxatnuclear and
CC proximal Golgi apparatus. Localizes at the base of the cilia near the
CC morphological distinction between the cilia and plasma membranes. Found
CC in the sperm annulus (PubMed:25588830). {ECO:0000269|PubMed:25588830}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15019-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15019-2; Sequence=VSP_038271;
CC Name=3;
CC IsoId=Q15019-3; Sequence=VSP_055176;
CC -!- TISSUE SPECIFICITY: Widely expressed. Up-regulated in liver cancer.
CC {ECO:0000269|PubMed:15915442, ECO:0000269|PubMed:19165576}.
CC -!- MISCELLANEOUS: Coordinated expression with SEPTIN6 and SEPTIN7.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY14718.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA09928.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SEPT2ID44125ch2q37.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D63878; BAA09928.2; ALT_INIT; mRNA.
DR EMBL; D28540; BAA05893.1; -; mRNA.
DR EMBL; AF038404; AAB92377.1; -; mRNA.
DR EMBL; AK294563; BAG57759.1; -; mRNA.
DR EMBL; AC005104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104841; AAY14718.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC014455; AAH14455.1; -; mRNA.
DR EMBL; BC033559; AAH33559.1; -; mRNA.
DR CCDS; CCDS2548.1; -. [Q15019-1]
DR CCDS; CCDS63195.1; -. [Q15019-3]
DR CCDS; CCDS74682.1; -. [Q15019-2]
DR RefSeq; NP_001008491.1; NM_001008491.2. [Q15019-1]
DR RefSeq; NP_001008492.1; NM_001008492.2. [Q15019-1]
DR RefSeq; NP_001269901.1; NM_001282972.1. [Q15019-2]
DR RefSeq; NP_001269902.1; NM_001282973.1. [Q15019-3]
DR RefSeq; NP_001307958.1; NM_001321029.1.
DR RefSeq; NP_001307959.1; NM_001321030.1. [Q15019-1]
DR RefSeq; NP_001307960.1; NM_001321031.1. [Q15019-1]
DR RefSeq; NP_001307961.1; NM_001321032.1. [Q15019-1]
DR RefSeq; NP_001307962.1; NM_001321033.1. [Q15019-1]
DR RefSeq; NP_001307963.1; NM_001321034.1. [Q15019-1]
DR RefSeq; NP_001307964.1; NM_001321035.1. [Q15019-1]
DR RefSeq; NP_004395.1; NM_004404.4. [Q15019-1]
DR RefSeq; NP_006146.1; NM_006155.2. [Q15019-1]
DR RefSeq; XP_016859694.1; XM_017004205.1. [Q15019-1]
DR RefSeq; XP_016859695.1; XM_017004206.1.
DR PDB; 2QA5; X-ray; 3.40 A; A/B=1-315.
DR PDB; 2QAG; X-ray; 4.00 A; A=1-361.
DR PDB; 2QNR; X-ray; 2.60 A; A/B=22-320.
DR PDB; 6UPA; X-ray; 2.51 A; A=35-308.
DR PDB; 6UPQ; X-ray; 1.86 A; A=36-308.
DR PDB; 6UPR; X-ray; 2.30 A; A=36-308.
DR PDB; 7M6J; EM; 3.60 A; A/F=35-308.
DR PDBsum; 2QA5; -.
DR PDBsum; 2QAG; -.
DR PDBsum; 2QNR; -.
DR PDBsum; 6UPA; -.
DR PDBsum; 6UPQ; -.
DR PDBsum; 6UPR; -.
DR PDBsum; 7M6J; -.
DR AlphaFoldDB; Q15019; -.
DR SMR; Q15019; -.
DR BioGRID; 110812; 147.
DR CORUM; Q15019; -.
DR DIP; DIP-38220N; -.
DR IntAct; Q15019; 63.
DR MINT; Q15019; -.
DR STRING; 9606.ENSP00000479861; -.
DR GlyGen; Q15019; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15019; -.
DR MetOSite; Q15019; -.
DR PhosphoSitePlus; Q15019; -.
DR SwissPalm; Q15019; -.
DR BioMuta; SEPT2; -.
DR DMDM; 2500769; -.
DR OGP; Q15019; -.
DR EPD; Q15019; -.
DR jPOST; Q15019; -.
DR MassIVE; Q15019; -.
DR MaxQB; Q15019; -.
DR PaxDb; Q15019; -.
DR PeptideAtlas; Q15019; -.
DR PRIDE; Q15019; -.
DR ProteomicsDB; 60368; -. [Q15019-1]
DR ProteomicsDB; 60369; -. [Q15019-2]
DR TopDownProteomics; Q15019-1; -. [Q15019-1]
DR Antibodypedia; 2911; 459 antibodies from 39 providers.
DR DNASU; 4735; -.
DR Ensembl; ENST00000360051.7; ENSP00000353157.3; ENSG00000168385.18. [Q15019-1]
DR Ensembl; ENST00000391971.7; ENSP00000375832.2; ENSG00000168385.18. [Q15019-1]
DR Ensembl; ENST00000391973.6; ENSP00000375834.2; ENSG00000168385.18. [Q15019-1]
DR Ensembl; ENST00000401990.5; ENSP00000385109.1; ENSG00000168385.18. [Q15019-3]
DR Ensembl; ENST00000402092.6; ENSP00000385172.2; ENSG00000168385.18. [Q15019-1]
DR Ensembl; ENST00000616972.4; ENSP00000479861.1; ENSG00000168385.18. [Q15019-2]
DR GeneID; 4735; -.
DR KEGG; hsa:4735; -.
DR MANE-Select; ENST00000391971.7; ENSP00000375832.2; NM_004404.5; NP_004395.1.
DR UCSC; uc002wbc.5; human. [Q15019-1]
DR CTD; 4735; -.
DR DisGeNET; 4735; -.
DR GeneCards; SEPTIN2; -.
DR HGNC; HGNC:7729; SEPTIN2.
DR HPA; ENSG00000168385; Low tissue specificity.
DR MIM; 601506; gene.
DR neXtProt; NX_Q15019; -.
DR OpenTargets; ENSG00000168385; -.
DR PharmGKB; PA31535; -.
DR VEuPathDB; HostDB:ENSG00000168385; -.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000155098; -.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; Q15019; -.
DR OMA; EASHAEI; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q15019; -.
DR TreeFam; TF101079; -.
DR PathwayCommons; Q15019; -.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR SignaLink; Q15019; -.
DR SIGNOR; Q15019; -.
DR BioGRID-ORCS; 4735; 26 hits in 1016 CRISPR screens.
DR ChiTaRS; SEPT2; human.
DR EvolutionaryTrace; Q15019; -.
DR GeneWiki; SEPT2; -.
DR GenomeRNAi; 4735; -.
DR Pharos; Q15019; Tbio.
DR PRO; PR:Q15019; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q15019; protein.
DR Bgee; ENSG00000168385; Expressed in ventricular zone and 204 other tissues.
DR ExpressionAtlas; Q15019; baseline and differential.
DR Genevisible; Q15019; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005930; C:axoneme; IDA:GO_Central.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0097730; C:non-motile cilium; IDA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0097227; C:sperm annulus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR InterPro; IPR008113; Septin2.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01740; SEPTIN2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Cell membrane; Cell projection; Centromere; Chromosome; Cilium; Cytoplasm;
KW Cytoskeleton; Differentiation; Direct protein sequencing; Flagellum;
KW GTP-binding; Kinetochore; Membrane; Mitosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Spermatogenesis.
FT CHAIN 1..361
FT /note="Septin-2"
FT /id="PRO_0000173515"
FT DOMAIN 34..306
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 44..51
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 101..104
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 182..185
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 260..270
FT /note="Important for dimerization"
FT BINDING 44..51
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 183..191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 241
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 256
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT SITE 156
FT /note="Important for dimerization"
FT MOD_RES 17
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P42208"
FT MOD_RES 190
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 211
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15150837,
FT ECO:0000269|PubMed:19165576, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1
FT /note="M -> MPWISEGRATRPCLRVPSARRGDEGLHQRDEASQKM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038271"
FT VAR_SEQ 72
FT /note="A -> AALNTRKTLLW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8590280"
FT /id="VSP_055176"
FT MUTAGEN 156
FT /note="F->D: Loss of dimerization."
FT /evidence="ECO:0000269|PubMed:17637674"
FT MUTAGEN 218
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:19165576"
FT MUTAGEN 260
FT /note="W->A: Loss of dimerization."
FT /evidence="ECO:0000269|PubMed:17637674"
FT MUTAGEN 270
FT /note="H->D: Loss of dimerization."
FT /evidence="ECO:0000269|PubMed:17637674"
FT CONFLICT 69
FT /note="P -> S (in Ref. 6; AAH14455)"
FT /evidence="ECO:0000305"
FT CONFLICT 360..361
FT /note="HV -> TCKVMCTYKKSEKTLSWIKKKTFQMHDPAVCFQSLGGCHPHFNSTC
FT A (in Ref. 2; BAA05893)"
FT /evidence="ECO:0000305"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:2QA5"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:6UPQ"
FT TURN 103..107
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6UPQ"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 116..134
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:6UPQ"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 189..205
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 249..258
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:6UPQ"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 273..293
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:6UPQ"
SQ SEQUENCE 361 AA; 41487 MW; 12CCBBE30806F92F CRC64;
MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT
DLYPERVIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS
YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV
IAKADTLTLK ERERLKKRIL DEIEEHNIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV
GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR
SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DGDGGALGHH
V
