ID SEPT5_HUMAN Reviewed; 369 AA. AC Q99719; O15251; Q96MY5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 28-JAN-2026, entry version 208. DE RecName: Full=Septin-5; DE AltName: Full=Cell division control-related protein 1; DE Short=CDCrel-1; DE AltName: Full=Peanut-like protein 1; GN Name=SEPTIN5 {ECO:0000312|HGNC:HGNC:9164}; Synonyms=PNUTL1, SEPT5; 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] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9022087; DOI=10.1172/jci119188; RA Zieger B., Hashimoto Y., Ware J.; RT "Alternative expression of platelet glycoprotein Ib(beta) mRNA from an RT adjacent 5' gene with an imperfect polyadenylation signal sequence."; RL J. Clin. Invest. 99:520-525(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Heart; RX PubMed=9385360; DOI=10.1007/s004390050576; RA McKie J., Sutherland H., Harvey E., Kim U.J., Scambler P.J.; RT "A human gene similar to Drosophila melanogaster peanut maps to the RT DiGeorge syndrome region of 22q11."; RL Hum. Genet. 101:6-12(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Brain; RX PubMed=9611266; DOI=10.1016/s0378-1119(98)00146-2; RA Yagi M., Zieger B., Roth G.J., Ware J.; RT "Structure and expression of the human septin gene HCDCREL-1."; RL Gene 212:229-236(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [7] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [9] RP PROTEIN SEQUENCE OF 23-36; 42-71; 82-90; 182-190; 297-308 AND 325-343, AND RP 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 [10] RP INTERACTION WITH SEPTIN8, AND TISSUE SPECIFICITY. RX PubMed=12023038; DOI=10.1016/s0014-5793(02)02749-7; RA Blaeser S., Jersch K., Hainmann I., Wunderle D., Zgaga-Griesz A., Busse A., RA Zieger B.; RT "Human septin-septin interaction: CDCrel-1 partners with KIAA0202."; RL FEBS Lett. 519:169-172(2002). RN [11] RP IDENTIFICATION IN A COMPLEX WITH STX4, AND PHOSPHORYLATION. RX PubMed=11880646; DOI=10.1073/pnas.052715199; RA Dent J., Kato K., Peng X.-R., Martinez C., Cattaneo M., Poujol C., RA Nurden P., Nurden A., Trimble W.S., Ware J.; RT "A prototypic platelet septin and its participation in secretion."; RL Proc. Natl. Acad. Sci. U.S.A. 99:3064-3069(2002). RN [12] RP POSSIBLE INVOLVEMENT IN PRKN. RX PubMed=14530399; DOI=10.1073/pnas.2132992100; RA Dong Z., Ferger B., Paterna J.-C., Vogel D., Furler S., Osinde M., RA Feldon J., Bueeler H.; RT "Dopamine-dependent neurodegeneration in rats induced by viral vector- RT mediated overexpression of the parkin target protein, CDCrel-1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12438-12443(2003). RN [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-327, 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 [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-327, AND RP IDENTIFICATION BY MASS 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 (By similarity). May CC play a role in cytokinesis (Potential). May play a role in platelet CC secretion (By similarity). {ECO:0000250, 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. GTPase activity is required for filament CC formation (By similarity). Interacts with SEPTIN2 and SEPTIN5. In CC platelets, associated with a complex containing STX4. Interacts with CC PRKN; this interaction leads to SEPTIN5 ubiquitination and degradation CC (By similarity). Interacts with DYRK1A (By similarity). Interacts with CC STX1A; in the cerebellar cortex (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:Q9Z2Q6}. CC -!- INTERACTION: CC Q99719; P05067: APP; NbExp=3; IntAct=EBI-373345, EBI-77613; CC Q99719; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-373345, EBI-742054; CC Q99719; P43356: MAGEA2B; NbExp=4; IntAct=EBI-373345, EBI-5650739; CC Q99719; O75376: NCOR1; NbExp=3; IntAct=EBI-373345, EBI-347233; CC Q99719; Q8N488: RYBP; NbExp=3; IntAct=EBI-373345, EBI-752324; CC Q99719; Q8WYJ6: SEPTIN1; NbExp=15; IntAct=EBI-373345, EBI-693002; CC Q99719; Q9P0V9: SEPTIN10; NbExp=8; IntAct=EBI-373345, EBI-3943788; CC Q99719; Q9NVA2: SEPTIN11; NbExp=14; IntAct=EBI-373345, EBI-957999; CC Q99719; Q8IYM1: SEPTIN12; NbExp=9; IntAct=EBI-373345, EBI-2585067; CC Q99719; Q15019: SEPTIN2; NbExp=7; IntAct=EBI-373345, EBI-741220; CC Q99719; Q15019-3: SEPTIN2; NbExp=7; IntAct=EBI-373345, EBI-11525407; CC Q99719; Q99719: SEPTIN5; NbExp=3; IntAct=EBI-373345, EBI-373345; CC Q99719; Q14141: SEPTIN6; NbExp=11; IntAct=EBI-373345, EBI-745901; CC Q99719; Q16181: SEPTIN7; NbExp=5; IntAct=EBI-373345, EBI-2009373; CC Q99719; Q92599: SEPTIN8; NbExp=7; IntAct=EBI-373345, EBI-958021; CC Q99719; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-373345, EBI-742688; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton CC {ECO:0000250}. Note=In platelets, found in areas surrounding alpha- CC granules. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99719-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99719-2; Sequence=VSP_042689, VSP_042690; CC -!- TISSUE SPECIFICITY: Expressed at high levels in the CNS, as well as in CC heart and platelets (at protein level). {ECO:0000269|PubMed:12023038, CC ECO:0000269|PubMed:15915442}. CC -!- PTM: Phosphorylated by DYRK1A (By similarity). In platelets, CC phosphorylated in response to thrombin, phorbol-12-myristate-13-acetate CC and collagen. {ECO:0000250|UniProtKB:Q9Z2Q6, CC ECO:0000269|PubMed:11880646}. CC -!- MISCELLANEOUS: In a heterologous system, SEPTIN5 overexpression has CC been shown to exert dopamine-dependent neurotoxicity. As wild-type CC PRKN, but not familial-linked PRKN mutants, ubiquitinates mouse SEPTIN5 CC and promotes its degradation, it has been suggested that a deficiency CC in SEPTIN5 degradation may contribute to the development of early onset CC Parkinson disease 2 (PARK2). 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 -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/220/hCDCRel-1"; 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; U74628; AAB93438.1; -; mRNA. DR EMBL; Y11593; CAA72332.1; -; mRNA. DR EMBL; AF006988; AAC39779.1; -; Genomic_DNA. DR EMBL; CR456545; CAG30431.1; -; mRNA. DR EMBL; AK056273; BAB71133.1; -; mRNA. DR EMBL; AC000093; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471176; EAX03032.1; -; Genomic_DNA. DR EMBL; BC025261; AAH25261.1; -; mRNA. DR CCDS; CCDS13764.1; -. [Q99719-1] DR CCDS; CCDS56224.1; -. [Q99719-2] DR RefSeq; NP_001009939.1; NM_001009939.3. [Q99719-2] DR RefSeq; NP_002679.2; NM_002688.5. [Q99719-1] DR PDB; 6WCU; X-ray; 1.80 A; A/B=340-369. DR PDBsum; 6WCU; -. DR AlphaFoldDB; Q99719; -. DR SMR; Q99719; -. DR BioGRID; 111414; 54. DR CORUM; Q99719; -. DR DIP; DIP-31201N; -. DR FunCoup; Q99719; 258. DR IntAct; Q99719; 45. DR MINT; Q99719; -. DR STRING; 9606.ENSP00000391311; -. DR ChEMBL; CHEMBL5465347; -. DR GlyGen; Q99719; 1 site. DR iPTMnet; Q99719; -. DR PhosphoSitePlus; Q99719; -. DR SwissPalm; Q99719; -. DR BioMuta; SEPT5; -. DR DMDM; 6685760; -. DR jPOST; Q99719; -. DR MassIVE; Q99719; -. DR PaxDb; 9606-ENSP00000391311; -. DR PeptideAtlas; Q99719; -. DR ProteomicsDB; 78433; -. [Q99719-1] DR ProteomicsDB; 78434; -. [Q99719-2] DR Pumba; Q99719; -. DR Antibodypedia; 4242; 253 antibodies from 36 providers. DR DNASU; 5413; -. DR Ensembl; ENST00000438754.6; ENSP00000394541.2; ENSG00000184702.21. [Q99719-2] DR Ensembl; ENST00000455784.7; ENSP00000391311.2; ENSG00000184702.21. [Q99719-1] DR GeneID; 5413; -. DR KEGG; hsa:5413; -. DR MANE-Select; ENST00000455784.7; ENSP00000391311.2; NM_002688.6; NP_002679.2. DR UCSC; uc002zpw.2; human. [Q99719-1] DR AGR; HGNC:9164; -. DR ClinPGx; PA33486; -. DR CTD; 5413; -. DR DisGeNET; 5413; -. DR GeneCards; SEPTIN5; -. DR HGNC; HGNC:9164; SEPTIN5. DR HPA; ENSG00000184702; Tissue enhanced (brain). DR MIM; 602724; gene. DR OpenTargets; ENSG00000184702; -. DR VEuPathDB; HostDB:ENSG00000184702; -. DR eggNOG; KOG2655; Eukaryota. DR GeneTree; ENSGT00940000159913; -. DR HOGENOM; CLU_017718_0_0_1; -. DR InParanoid; Q99719; -. DR OMA; YSHARNG; -. DR OrthoDB; 416553at2759; -. DR PAN-GO; Q99719; 10 GO annotations based on evolutionary models. DR PhylomeDB; Q99719; -. DR PathwayCommons; Q99719; -. DR SignaLink; Q99719; -. DR SIGNOR; Q99719; -. DR Agora; ENSG00000184702; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 5413; 25 hits in 1085 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; SEPT5; human. DR GeneWiki; SEPT5; -. DR GenomeRNAi; 5413; -. DR Pharos; Q99719; Tbio. DR PRO; PR:Q99719; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q99719; protein. DR Bgee; ENSG00000184702; Expressed in right frontal lobe and 115 other cell types or tissues. DR ExpressionAtlas; Q99719; baseline and differential. DR GO; GO:0032153; C:cell division site; IBA:GO_Central. DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0031105; C:septin complex; ISS:UniProtKB. DR GO; GO:0005940; C:septin ring; IBA:GO_Central. DR GO; GO:0008021; C:synaptic vesicle; 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:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central. DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc. DR GO; GO:0030534; P:adult behavior; ISS:UniProtKB. DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central. DR GO; GO:0008104; P:intracellular protein localization; IBA:GO_Central. DR GO; GO:0017157; P:regulation of exocytosis; IMP:UniProtKB. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; TAS:ParkinsonsUK-UCL. DR GO; GO:0035176; P:social behavior; ISS:UniProtKB. DR GO; GO:0016080; P:synaptic vesicle targeting; TAS:UniProtKB. DR CDD; cd01850; CDC_Septin; 1. DR FunFam; 3.40.50.300:FF:000064; Septin 4; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR030379; G_SEPTIN_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR016491; Septin. DR PANTHER; PTHR18884; SEPTIN; 1. DR Pfam; PF00735; Septin; 1. DR PIRSF; PIRSF006698; Septin; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51719; G_SEPTIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Coiled coil; KW Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding; KW Methylation; Nucleotide-binding; Phosphoprotein; Proteomics identification; KW Reference proteome. FT CHAIN 1..369 FT /note="Septin-5" FT /id="PRO_0000173521" FT DOMAIN 41..314 FT /note="Septin-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 51..58 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 108..111 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 189..192 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT COILED 338..369 FT /evidence="ECO:0000255" FT BINDING 51..58 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 85 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 111 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 190..198 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 248 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 263 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 13 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Z2Q6" FT MOD_RES 168 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9Z2Q6" FT MOD_RES 225 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 327 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 336 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Z2Q6" FT VAR_SEQ 1..18 FT /note="MSTGLRYKSKLATPEDKQ -> MDSLAAPQDRLVEQLLSPRTQAQRRLK FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042689" FT VAR_SEQ 272..369 FT /note="VENQAHCDFVKLRNMLIRTHMHDLKDVTCDVHYENYRAHCIQQMTSKLTQDS FT RMESPIPILPLPTPDAETEKLIRMKDEELRRMQEMLQRMKQQMQDQ -> GALRLREAA FT QHAHPHAYARPQGRDVRRALRELPRALHPADDQQTDPGQPHGEPHPDPAAAHPGRRD FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042690" FT CONFLICT 224 FT /note="D -> N (in Ref. 2; CAA72332)" FT /evidence="ECO:0000305" FT HELIX 341..367 FT /evidence="ECO:0007829|PDB:6WCU" SQ SEQUENCE 369 AA; 42777 MW; 47054765DEA10D33 CRC64; MSTGLRYKSK LATPEDKQDI DKQYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL VHSLFLTDLY KDRKLLSAEE RISQTVEILK HTVDIEEKGV KLKLTIVDTP GFGDAVNNTE CWKPITDYVD QQFEQYFRDE SGLNRKNIQD NRVHCCLYFI SPFGHGLRPV DVGFMKALHE KVNIVPLIAK ADCLVPSEIR KLKERIREEI DKFGIHVYQF PECDSDEDED FKQQDRELKE SAPFAVIGSN TVVEAKGQRV RGRLYPWGIV EVENQAHCDF VKLRNMLIRT HMHDLKDVTC DVHYENYRAH CIQQMTSKLT QDSRMESPIP ILPLPTPDAE TEKLIRMKDE ELRRMQEMLQ RMKQQMQDQ //