SEPT5_HUMAN
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 03-AUG-2022, entry version 191.
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=13; IntAct=EBI-373345, EBI-693002;
CC Q99719; Q9P0V9: SEPTIN10; NbExp=6; IntAct=EBI-373345, EBI-3943788;
CC Q99719; Q9NVA2: SEPTIN11; NbExp=10; IntAct=EBI-373345, EBI-957999;
CC Q99719; Q8IYM1: SEPTIN12; NbExp=7; IntAct=EBI-373345, EBI-2585067;
CC Q99719; Q15019: SEPTIN2; NbExp=4; 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=9; IntAct=EBI-373345, EBI-745901;
CC Q99719; Q92599: SEPTIN8; NbExp=6; 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="http://atlasgeneticsoncology.org/Genes/hCDCRel-1ID220.html";
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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_001009939.2. [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; 45.
DR DIP; DIP-31201N; -.
DR IntAct; Q99719; 30.
DR MINT; Q99719; -.
DR STRING; 9606.ENSP00000391311; -.
DR iPTMnet; Q99719; -.
DR PhosphoSitePlus; Q99719; -.
DR SwissPalm; Q99719; -.
DR BioMuta; SEPT5; -.
DR DMDM; 6685760; -.
DR UCD-2DPAGE; Q99719; -.
DR EPD; Q99719; -.
DR jPOST; Q99719; -.
DR MassIVE; Q99719; -.
DR MaxQB; Q99719; -.
DR PaxDb; Q99719; -.
DR PeptideAtlas; Q99719; -.
DR PRIDE; Q99719; -.
DR ProteomicsDB; 78433; -. [Q99719-1]
DR ProteomicsDB; 78434; -. [Q99719-2]
DR Antibodypedia; 4242; 238 antibodies from 35 providers.
DR DNASU; 5413; -.
DR Ensembl; ENST00000438754.6; ENSP00000394541.2; ENSG00000184702.20. [Q99719-2]
DR Ensembl; ENST00000455784.7; ENSP00000391311.2; ENSG00000184702.20. [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 CTD; 5413; -.
DR DisGeNET; 5413; -.
DR GeneCards; SEPTIN5; -.
DR HGNC; HGNC:9164; SEPTIN5.
DR HPA; ENSG00000184702; Tissue enhanced (brain).
DR MIM; 602724; gene.
DR neXtProt; NX_Q99719; -.
DR OpenTargets; ENSG00000184702; -.
DR PharmGKB; PA33486; -.
DR VEuPathDB; HostDB:ENSG00000184702; -.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000159913; -.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; Q99719; -.
DR OMA; VNCEDSW; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q99719; -.
DR TreeFam; TF101079; -.
DR PathwayCommons; Q99719; -.
DR SignaLink; Q99719; -.
DR BioGRID-ORCS; 5413; 25 hits in 1022 CRISPR screens.
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 113 other tissues.
DR ExpressionAtlas; Q99719; baseline and differential.
DR Genevisible; Q99719; HS.
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: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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030647; SEPT5.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF68; PTHR18884:SF68; 1.
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; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW Methylation; Nucleotide-binding; Phosphoprotein; 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
