SEP11_HUMAN
ID SEP11_HUMAN Reviewed; 429 AA.
AC Q9NVA2; B7Z7Z6; E9KL32; Q4W5G1; Q7L4N1; Q96SP1; Q9UFY9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Septin-11;
GN Name=SEPTIN11 {ECO:0000312|HGNC:HGNC:25589}; Synonyms=SEPT11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epididymis;
RX PubMed=20736409; DOI=10.1074/mcp.m110.001719;
RA Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C.,
RA Jin S., Liu J., Zhu P., Liu Y.;
RT "Systematic mapping and functional analysis of a family of human epididymal
RT secretory sperm-located proteins.";
RL Mol. Cell. Proteomics 9:2517-2528(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma, and Testis;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-337.
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PROTEIN SEQUENCE OF 2-14 (ISOFORM 1), AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 15-34; 55-79; 84-93; 96-110; 176-184; 309-336; 387-397
RP AND 400-418, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP FUNCTION, MUTAGENESIS OF GLY-48, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15196925; DOI=10.1016/j.febslet.2004.05.030;
RA Hanai N., Nagata K., Kawajiri A., Shiromizu T., Saitoh N., Hasegawa Y.,
RA Murakami S., Inagaki M.;
RT "Biochemical and cell biological characterization of a mammalian septin,
RT Sept11.";
RL FEBS Lett. 568:83-88(2004).
RN [10]
RP INTERACTION WITH SEPTIN7 AND SEPTIN9.
RX PubMed=15485874; DOI=10.1074/jbc.m406153200;
RA Nagata K., Asano T., Nozawa Y., Inagaki M.;
RT "Biochemical and cell biological analyses of a mammalian septin complex,
RT Sept7/9b/11.";
RL J. Biol. Chem. 279:55895-55904(2004).
RN [11]
RP CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
RX PubMed=14999297; DOI=10.1038/sj.leu.2403334;
RA Kojima K., Sakai I., Hasegawa A., Niiya H., Azuma T., Matsuo Y., Fujii N.,
RA Tanimoto M., Fujita S.;
RT "FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line
RT CNLBC1 derived from chronic neutrophilic leukemia in transformation with
RT t(4;11)(q21;q23).";
RL Leukemia 18:998-1005(2004).
RN [12]
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 [13]
RP SUBCELLULAR LOCATION.
RX PubMed=17546647; DOI=10.1002/humu.20554;
RA Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.;
RT "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are
RT associated with altered interactions with SEPT4/SEPT11 and resistance to
RT Rho/Rhotekin-signaling.";
RL Hum. Mutat. 28:1005-1013(2007).
RN [14]
RP INTERACTION WITH SEPTIN12.
RX PubMed=18047794; DOI=10.5483/bmbrep.2007.40.6.973;
RA Ding X., Yu W., Liu M., Shen S., Chen F., Wan B., Yu L.;
RT "SEPT12 interacts with SEPT6 and this interaction alters the filament
RT structure of SEPT6 in Hela cells.";
RL J. Biochem. Mol. Biol. 40:973-978(2007).
RN [15]
RP ROLE IN BACTERIAL INFECTION.
RX PubMed=19234302; DOI=10.1074/jbc.m900231200;
RA Mostowy S., Danckaert A., Tham T.N., Machu C., Guadagnini S.,
RA Pizarro-Cerda J., Cossart P.;
RT "Septin 11 restricts InlB-mediated invasion by Listeria.";
RL J. Biol. Chem. 284:11613-11621(2009).
RN [16]
RP INTERACTION WITH SEPTIN9, AND SUBCELLULAR LOCATION.
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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in
CC cytokinesis (Potential). May play a role in the cytoarchitecture of
CC neurons, including dendritic arborization and dendritic spines, and in
CC GABAergic synaptic connectivity (By similarity). During Listeria
CC monocytogenes infection, not required for the bacterial entry process,
CC but restricts its efficacy. {ECO:0000250, ECO:0000269|PubMed:15196925,
CC ECO:0000269|PubMed:19234302, ECO:0000305}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and can associate with cellular membranes, actin
CC filaments and microtubules. Forms homooligomers. GTPase activity is
CC required for filament formation. Interacts with SEPTIN7, SEPTIN9 and
CC SEPTIN12. {ECO:0000269|PubMed:15485874, ECO:0000269|PubMed:18047794,
CC ECO:0000269|PubMed:19145258}.
CC -!- INTERACTION:
CC Q9NVA2; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-957999, EBI-10269566;
CC Q9NVA2; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-957999, EBI-693002;
CC Q9NVA2; Q99719: SEPTIN5; NbExp=10; IntAct=EBI-957999, EBI-373345;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Synapse. Cell
CC projection, dendritic spine. Cell projection, axon {ECO:0000250}.
CC Note=Partly colocalizes with stress fibers and microtubules. During
CC bacterial infection, displays a collar shape structure next to actin at
CC the pole of invading bacteria.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NVA2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVA2-2; Sequence=VSP_038320;
CC -!- TISSUE SPECIFICITY: Widely expressed, except in leukocytes.
CC {ECO:0000269|PubMed:15196925, ECO:0000269|PubMed:15915442}.
CC -!- DISEASE: Note=A chromosomal aberration involving SEPTIN11 may be a
CC cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23)
CC with KMT2A/MLL1.
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=BAB55250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB53741.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; GU727629; ADU87631.1; -; mRNA.
DR EMBL; AK001711; BAA91853.1; -; mRNA.
DR EMBL; AK027633; BAB55250.1; ALT_INIT; mRNA.
DR EMBL; AK302700; BAH13782.1; -; mRNA.
DR EMBL; AC104687; AAY40922.1; -; Genomic_DNA.
DR EMBL; AC111196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05805.1; -; Genomic_DNA.
DR EMBL; BC008083; AAH08083.3; -; mRNA.
DR EMBL; BC063615; AAH63615.1; -; mRNA.
DR EMBL; AL110300; CAB53741.2; ALT_SEQ; mRNA.
DR CCDS; CCDS34018.1; -. [Q9NVA2-1]
DR CCDS; CCDS77931.1; -. [Q9NVA2-2]
DR RefSeq; NP_001293076.1; NM_001306147.1. [Q9NVA2-2]
DR RefSeq; NP_060713.1; NM_018243.3. [Q9NVA2-1]
DR RefSeq; XP_016863889.1; XM_017008400.1. [Q9NVA2-2]
DR PDB; 6UPQ; X-ray; 1.86 A; B=40-306.
DR PDBsum; 6UPQ; -.
DR AlphaFoldDB; Q9NVA2; -.
DR SMR; Q9NVA2; -.
DR BioGRID; 120870; 83.
DR CORUM; Q9NVA2; -.
DR DIP; DIP-36161N; -.
DR IntAct; Q9NVA2; 17.
DR STRING; 9606.ENSP00000264893; -.
DR GlyGen; Q9NVA2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVA2; -.
DR PhosphoSitePlus; Q9NVA2; -.
DR SwissPalm; Q9NVA2; -.
DR BioMuta; SEPT11; -.
DR DMDM; 50401687; -.
DR OGP; Q9NVA2; -.
DR UCD-2DPAGE; Q9NVA2; -.
DR EPD; Q9NVA2; -.
DR jPOST; Q9NVA2; -.
DR MassIVE; Q9NVA2; -.
DR MaxQB; Q9NVA2; -.
DR PaxDb; Q9NVA2; -.
DR PeptideAtlas; Q9NVA2; -.
DR PRIDE; Q9NVA2; -.
DR ProteomicsDB; 82771; -. [Q9NVA2-1]
DR ProteomicsDB; 82772; -. [Q9NVA2-2]
DR Antibodypedia; 24838; 203 antibodies from 28 providers.
DR DNASU; 55752; -.
DR Ensembl; ENST00000264893.11; ENSP00000264893.6; ENSG00000138758.12. [Q9NVA2-1]
DR Ensembl; ENST00000510515.5; ENSP00000422896.1; ENSG00000138758.12. [Q9NVA2-2]
DR GeneID; 55752; -.
DR KEGG; hsa:55752; -.
DR MANE-Select; ENST00000264893.11; ENSP00000264893.6; NM_018243.4; NP_060713.1.
DR UCSC; uc003hkj.4; human. [Q9NVA2-1]
DR CTD; 55752; -.
DR DisGeNET; 55752; -.
DR GeneCards; SEPTIN11; -.
DR HGNC; HGNC:25589; SEPTIN11.
DR HPA; ENSG00000138758; Low tissue specificity.
DR MIM; 612887; gene.
DR neXtProt; NX_Q9NVA2; -.
DR OpenTargets; ENSG00000138758; -.
DR PharmGKB; PA128394688; -.
DR VEuPathDB; HostDB:ENSG00000138758; -.
DR eggNOG; KOG3859; Eukaryota.
DR GeneTree; ENSGT00940000160196; -.
DR InParanoid; Q9NVA2; -.
DR OMA; NGFIFNI; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9NVA2; -.
DR TreeFam; TF101080; -.
DR PathwayCommons; Q9NVA2; -.
DR SignaLink; Q9NVA2; -.
DR BioGRID-ORCS; 55752; 9 hits in 1020 CRISPR screens.
DR ChiTaRS; SEPT11; human.
DR GeneWiki; SEPT11; -.
DR GenomeRNAi; 55752; -.
DR Pharos; Q9NVA2; Tbio.
DR PRO; PR:Q9NVA2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NVA2; protein.
DR Bgee; ENSG00000138758; Expressed in ventricular zone and 210 other tissues.
DR ExpressionAtlas; Q9NVA2; baseline and differential.
DR Genevisible; Q9NVA2; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
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 Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
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 projection; Chromosomal rearrangement; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..429
FT /note="Septin-11"
FT /id="PRO_0000173542"
FT DOMAIN 38..304
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 48..55
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 100..103
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 183..186
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 398..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..415
FT /evidence="ECO:0000255"
FT COMPBIAS 399..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 184..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12665801"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..9
FT /note="MAVAVGRPS -> MEERKPAHVLRSFKYAAFM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038320"
FT MUTAGEN 48
FT /note="G->A: High reduction in GTPase activity. No effect
FT on GTP-binding. Loss of filament formation."
FT /evidence="ECO:0000269|PubMed:15196925"
FT CONFLICT 142
FT /note="Y -> H (in Ref. 5; CAB53741)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="R -> H (in Ref. 5; CAB53741)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="E -> G (in Ref. 5; CAB53741)"
FT /evidence="ECO:0000305"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6UPQ"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 115..132
FT /evidence="ECO:0007829|PDB:6UPQ"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:6UPQ"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:6UPQ"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:6UPQ"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:6UPQ"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:6UPQ"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:6UPQ"
FT HELIX 293..298
FT /evidence="ECO:0007829|PDB:6UPQ"
SQ SEQUENCE 429 AA; 49398 MW; D467F1F315FFD028 CRC64;
MAVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET GIGKSTLMDT
LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD TVGFGDQINK DDSYKPIVEY
IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP
IIAKADTIAK NELHKFKSKI MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST
EEVKIGNKMA KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC
KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK EKEAELKEAE
KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVNNFQKKKA AAQLLQSQAQ QSGAQQTKKD
KDKKNASFT
