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Database: UniProt
Entry: D3ZT07_RAT
LinkDB: D3ZT07_RAT
Original site: D3ZT07_RAT 
ID   D3ZT07_RAT              Unreviewed;       380 AA.
AC   D3ZT07;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN   Name=Septin5 {ECO:0000313|Ensembl:ENSRNOP00000042895.5,
GN   ECO:0000313|RGD:621763}; Synonyms=Sept5 {ECO:0000313|RGD:621763};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000042895.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000042895.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000042895.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000042895.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000042895.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase.
CC       {ECO:0000256|PIRNR:PIRNR006698}.
CC   -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC       that form filaments. {ECO:0000256|PIRNR:PIRNR006698}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. Septin GTPase family.
CC       {ECO:0000256|PIRNR:PIRNR006698, ECO:0000256|RuleBase:RU004560}.
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DR   AlphaFoldDB; D3ZT07; -.
DR   IntAct; D3ZT07; 1.
DR   Ensembl; ENSRNOT00000051680.7; ENSRNOP00000042895.5; ENSRNOG00000029912.7.
DR   RGD; 621763; Septin5.
DR   VEuPathDB; HostDB:ENSRNOG00000029912; -.
DR   GeneTree; ENSGT00940000159913; -.
DR   HOGENOM; CLU_017718_0_0_1; -.
DR   OMA; TNMYLRS; -.
DR   TreeFam; TF101079; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000029912; Expressed in frontal cortex and 20 other cell types or tissues.
DR   ExpressionAtlas; D3ZT07; baseline and differential.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0017157; P:regulation of exocytosis; IEA:Ensembl.
DR   CDD; cd01850; CDC_Septin; 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   PANTHER; PTHR18884:SF68; SEPTIN-5; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|PIRNR:PIRNR006698};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR006698-
KW   2}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR006698-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN          41..325
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   SITE            163
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006698-2"
SQ   SEQUENCE   380 AA;  44043 MW;  DDDBBF29E5F1C8A4 CRC64;
     MSTGLRYKSK LATPEDKQDI DKQYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL
     VHSLFLTDLY KDRKLLSAEE RINQTVEILK HTVDIEEKGV KLKLTIVDTP GFGDAVNNFE
     CWKPITDYVD QQFEQYFRDE SGLNRKNIQD NRVHCCLYFI SPFGHGLRPV DVGFMKALHE
     KVNIVPLIAK ADCLVPSEIR KLKDRIREEI DKFGIHVYQF PECDSDEDED FKQQDRELKT
     RLGWVLAPPQ ESAPFAVIGS NTVVEAKGQR VRGRLYPWGI VEVENQAHCD FVKLRNMLIR
     THMHDLKDVT CDVHYENYRA HCIQQMTSKL TQDSRMESPI PILPLPTPDS ETEKLIRMKD
     EELRRMQEML QKMKQQMQDQ
//
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