SEPT9_RAT
ID SEPT9_RAT Reviewed; 564 AA.
AC Q9QZR6; Q9QZJ7; Q9QZJ8; Q9QZP9;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Septin-9;
DE AltName: Full=Eighth septin;
DE AltName: Full=Eseptin;
DE AltName: Full=Septin-like protein;
DE Short=SLP;
GN Name=Septin9 {ECO:0000250|UniProtKB:Q9UHD8};
GN Synonyms=Sept9 {ECO:0000312|RGD:708523};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY,
RP ALTERNATIVE SPLICING, AND MUTAGENESIS OF GLY-288.
RC TISSUE=Brain;
RX PubMed=10371165; DOI=10.1016/s0014-5793(99)00559-1;
RA Fung E.T., Scheller R.H.;
RT "Identification of a novel alternatively spliced septin.";
RL FEBS Lett. 451:203-208(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND ALTERNATIVE SPLICING.
RC TISSUE=Mesangial cell;
RX PubMed=10944462; DOI=10.1006/bbrc.2000.3287;
RA Jackisch B.O., Hausser H., Schaefer L., Kappler J., Muller H.W., Kresse H.;
RT "Alternative exon usage of rat septins.";
RL Biochem. Biophys. Res. Commun. 275:180-188(2000).
RN [3]
RP PROTEIN SEQUENCE OF 292-300, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SEPTIN7.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [6]
RP TISSUE SPECIFICITY.
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 [7]
RP INTERACTION WITH SEPTIN14.
RX PubMed=17922164; DOI=10.1007/s00335-007-9065-x;
RA Peterson E.A., Kalikin L.M., Steels J.D., Estey M.P., Trimble W.S.,
RA Petty E.M.;
RT "Characterization of a SEPT9 interacting protein, SEPT14, a novel testis-
RT specific septin.";
RL Mamm. Genome 18:796-807(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-67, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
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).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and associate with cellular membranes, actin
CC filaments, and microtubules. GTPase activity is required for filament
CC formation. Interacts with SEPTIN2, SEPTIN6, SEPTIN7, SEPTIN11 and
CC SEPTIN14. Interacts with RTKN and ARHGEF18 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10944462, ECO:0000269|PubMed:15485874}. Note=In
CC embryonic fibroblasts, associated with actin stress fibers. No apparent
CC co-distribution with microtubules, but some colocalization with
CC vimentin filaments in the perinuclear region.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=SLP-a;
CC IsoId=Q9QZR6-1; Sequence=Displayed;
CC Name=2; Synonyms=SLP-b;
CC IsoId=Q9QZR6-2; Sequence=VSP_012345;
CC Name=3; Synonyms=E-septin long form;
CC IsoId=Q9QZR6-3; Sequence=VSP_012344;
CC Name=4; Synonyms=E-septin short form;
CC IsoId=Q9QZR6-4; Sequence=VSP_012343;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, mainly in the perikarya and
CC processes of astrocytes in the cerebellum, dentate gyrus and corpus
CC callosum (at protein level). In the sciatic nerve, highly expressed in
CC Schwann cells (at protein level). Isoforms are differentially expressed
CC in testes, kidney, liver, heart, spleen and brain. Undetectable in
CC skeletal muscle. {ECO:0000269|PubMed:10371165,
CC ECO:0000269|PubMed:10944462, ECO:0000269|PubMed:17546647}.
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 ---------------------------------------------------------------------------
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; AF180525; AAF01206.1; -; mRNA.
DR EMBL; AF180526; AAF01207.1; -; mRNA.
DR EMBL; AF170253; AAF03376.1; -; mRNA.
DR EMBL; AF173899; AAF03391.1; -; mRNA.
DR PIR; JC7365; JC7365.
DR RefSeq; NP_001106969.1; NM_001113497.1.
DR RefSeq; NP_114025.2; NM_031837.2.
DR RefSeq; NP_789826.2; NM_176856.2.
DR AlphaFoldDB; Q9QZR6; -.
DR SMR; Q9QZR6; -.
DR BioGRID; 249831; 2.
DR IntAct; Q9QZR6; 5.
DR STRING; 10116.ENSRNOP00000003891; -.
DR ChEMBL; CHEMBL2176803; -.
DR iPTMnet; Q9QZR6; -.
DR PhosphoSitePlus; Q9QZR6; -.
DR jPOST; Q9QZR6; -.
DR PeptideAtlas; Q9QZR6; -.
DR PRIDE; Q9QZR6; -.
DR GeneID; 83788; -.
DR KEGG; rno:83788; -.
DR CTD; 10801; -.
DR RGD; 708523; Sept9.
DR eggNOG; KOG1547; Eukaryota.
DR InParanoid; Q9QZR6; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9QZR6; -.
DR PRO; PR:Q9QZR6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005930; C:axoneme; ISO:RGD.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
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:1902857; P:positive regulation of non-motile cilium assembly; ISO:RGD.
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; IPR030645; SEPT9.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF47; PTHR18884:SF47; 1.
DR Pfam; PF00735; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..564
FT /note="Septin-9"
FT /id="PRO_0000173537"
FT DOMAIN 275..546
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 38..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..292
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 342..345
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 424..427
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COMPBIAS 91..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 285..292
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 425..433
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80UG5"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 125
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 258
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD8"
FT VAR_SEQ 1..231
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10371165"
FT /id="VSP_012343"
FT VAR_SEQ 1..160
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10371165"
FT /id="VSP_012344"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10944462"
FT /id="VSP_012345"
FT MUTAGEN 288
FT /note="G->V: Abolishes the GTP binding."
FT /evidence="ECO:0000269|PubMed:10371165"
FT CONFLICT 230
FT /note="V -> G (in Ref. 1; AAF01206)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="E -> ED (in Ref. 1; AAF01206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 63792 MW; B45160157F986C0C CRC64;
MERDRITALK RSFEVEEIEP PNSTPPRRVQ TPLLRATVAS SSQKFQDLGV KNSEPAARLV
DTLSQRSPKP SLRRVDLAGA KAPEPMSRRT ELSIDISSKQ VESTASTPGP SRFGLKRAEV
LGHKTPEPVP RRTEITIVKP QESGLRRVET PASKAPEGSA MPVTDAAPKR VEIQVPKPAE
APNCPLPPQT LENSEAPMSQ LQSRLEPRPP VTEVPYRNQE DSEVAPSCVV DMADNPRDAM
LKQAPVSRNE KAPVDFGYVG IDSILEQMRR KAMKQGFEFN IMVVGQSGLG KSTLINTLFK
SKISRKSVQP ISEERIPKTI EIKSITHDIE EKGVRMKLTV IDTPGFGDHI NNENCWQPIM
KFINDQYEKY LQEEVNINRK KRIPDTRVHC CLYFIPATGH SLRPLDIEFM KRLSKVVNIV
PVIAKADTLT LEERVYFKQR ITSDLLSNGI DVYPQKEFDE AEDRLVNEKF REMIPFAVVG
SDHEYQVNGK RILGRKTKWG TIEVENTTHC EFAYLRDLLI RTHMQNIKDI TSNIHFEAYR
VKRLNEGNSA MANGIEKEPE TQEM
