SEPT7_RAT
ID SEPT7_RAT Reviewed; 436 AA.
AC Q9WVC0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Septin-7;
DE AltName: Full=CDC10 protein homolog;
GN Name=Septin7 {ECO:0000250|UniProtKB:Q16181};
GN Synonyms=Cdc10, Sept7 {ECO:0000312|RGD:620469};
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].
RC STRAIN=Sprague-Dawley;
RA Walikonis R.S., Jensen O., Mann M., Kennedy M.B.;
RT "Identification of postsynaptic density proteins by MALDI-TOF mass
RT spectrometry (Abstract #713.1).";
RL Abstr. - Soc. Neurosci. 24:1801-1801(1998).
RN [2]
RP PROTEIN SEQUENCE OF 137-146 AND 186-194, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SEPTIN2; SEPTIN7; SEPTIN8;
RP SEPTIN9 AND SEPTIN11.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; THR-227 AND SER-333, 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. Required for normal
CC organization of the actin cytoskeleton. Required for normal progress
CC through mitosis. Involved in cytokinesis. Required for normal
CC association of CENPE with the kinetochore. Plays a role in ciliogenesis
CC and collective cell movements. Forms a filamentous structure with
CC SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus
CC which is required for the structural integrity and motility of the
CC sperm tail during postmeiotic differentiation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
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. Filaments are assembled from asymmetrical heterotrimers,
CC composed of SEPTIN2, SEPTIN6 and SEPTIN7 that associate head-to-head to
CC form a hexameric unit. Within the trimer, directly interacts with
CC SEPTIN6, while interaction with SEPTIN2 seems indirect. In the absence
CC of SEPTIN6, forms homodimers. Interacts directly with CENPE and links
CC CENPE to septin filaments composed of SEPTIN2, SEPTIN6 and SEPTIN7.
CC Interacts with SEPTIN5. Component of a septin core octomeric complex
CC consisting of SEPTIN12, SEPTIN7, SEPTIN6 and SEPTIN2 or SEPTIN4 in the
CC order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm
CC annulus; the SEPTIN12:SEPTIN7 association is mediated by the respective
CC GTP-binding domains (By similarity). Interacts with SEPTIN2, SEPTIN7,
CC SEPTIN8, SEPTIN9 and SEPTIN11 (PubMed:15485874). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q16181, ECO:0000269|PubMed:15485874}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15485874}.
CC Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Cleavage furrow {ECO:0000250}.
CC Midbody {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q16181}. Note=Distributed throughout the
CC cytoplasm in prometaphase cells. Associated with the spindle during
CC metaphase. Associated with the central spindle and at the cleavage
CC furrow in anaphase cells. Detected at the midbody in telophase (By
CC similarity). Associated with actin stress fibers. According to
CC PubMed:15485874, also found in the nucleus. Found in the sperm annulus
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
CC -!- MISCELLANEOUS: Coordinated expression with SEPTIN2 and SEPTIN6.
CC {ECO:0000250}.
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}.
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DR EMBL; AF142759; AAD37861.1; -; mRNA.
DR RefSeq; NP_072138.2; NM_022616.2.
DR AlphaFoldDB; Q9WVC0; -.
DR SMR; Q9WVC0; -.
DR BioGRID; 249132; 5.
DR CORUM; Q9WVC0; -.
DR IntAct; Q9WVC0; 5.
DR MINT; Q9WVC0; -.
DR STRING; 10116.ENSRNOP00000008839; -.
DR iPTMnet; Q9WVC0; -.
DR PhosphoSitePlus; Q9WVC0; -.
DR SwissPalm; Q9WVC0; -.
DR jPOST; Q9WVC0; -.
DR PaxDb; Q9WVC0; -.
DR PRIDE; Q9WVC0; -.
DR GeneID; 64551; -.
DR KEGG; rno:64551; -.
DR UCSC; RGD:620469; rat.
DR CTD; 989; -.
DR RGD; 620469; Sept7.
DR eggNOG; KOG2655; Eukaryota.
DR InParanoid; Q9WVC0; -.
DR PhylomeDB; Q9WVC0; -.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR PRO; PR:Q9WVC0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0097730; C:non-motile cilium; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0032156; C:septin cytoskeleton; ISO:RGD.
DR GO; GO:0032160; C:septin filament array; ISO:RGD.
DR GO; GO:0005940; C:septin ring; ISO:RGD.
DR GO; GO:0097227; C:sperm annulus; ISO:RGD.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
DR GO; GO:0045202; C:synapse; 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:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0048668; P:collateral sprouting; ISO:RGD.
DR GO; GO:0030865; P:cortical cytoskeleton organization; ISO:RGD.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISO:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; ISO:RGD.
DR GO; GO:0099173; P:postsynapse organization; IDA:SynGO.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0031270; P:pseudopodium retraction; ISO:RGD.
DR GO; GO:0016476; P:regulation of embryonic cell shape; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 InterPro; IPR008115; Septin7.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01742; SEPTIN7.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cell projection; Centromere;
KW Chromosome; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation;
KW Direct protein sequencing; Flagellum; GTP-binding; Kinetochore; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT CHAIN 2..436
FT /note="Septin-7"
FT /id="PRO_0000173532"
FT DOMAIN 46..315
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 46..316
FT /note="Interaction with SEPTIN12"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT REGION 56..63
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 112..115
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 193..196
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 377..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..436
FT /evidence="ECO:0000255"
FT COMPBIAS 377..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 194..202
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT MOD_RES 29
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O55131"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 372
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O55131"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT MOD_RES 425
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
SQ SEQUENCE 436 AA; 50508 MW; 666DC3C1F0880404 CRC64;
MSVSARSAAA EERSVNCSTM AQPKNLEGYV GFANLPNQVY RKSVKRGFEF TLMVVGESGL
GKSTLINSLF LTDLYSPEYP GPSHRIKKTV QVEQSKVLIK EGGVQLLLTI VDTPGFGDAV
DNSNCWQPVI DYIDSKFEDY LNAESRVNRR QMPDNRVQCC LYFIAPSGHG LKPLDIEFMK
RLHEKVNIIP LIAKADTLTP EECQQFKKQI MKEIQGHKIK IYEFPETDDE EENKLVKKIK
DRLPLAVVGS NTIIEVNGKR VRGRQYPWGV AEVENGEHCD FTILRNMLIR THMQDLKDVT
NNVHYENYRS RKLAAVTYNG VDNNKNKGQL TKSPLAQMEE ERREHVAKMK KMEMEMEQVF
EMKVKEKVQK LKDSEAELQR RHEQMKKNLE AQHKELEEKR RQFEEEKANW EAQQRILEQQ
NSSRTLEKNK KKGKIF
