SEPT1_MOUSE
ID SEPT1_MOUSE Reviewed; 366 AA.
AC P42209; B2RU74;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Septin-1 {ECO:0000305};
DE AltName: Full=Differentiation protein 6;
DE Short=Protein Diff6;
DE AltName: Full=Peanut-like protein 3;
GN Name=Septin1 {ECO:0000312|MGI:MGI:1858916};
GN Synonyms=Diff6 {ECO:0000312|MGI:MGI:1858916},
GN Pnutl3 {ECO:0000312|MGI:MGI:1858916}, Sept1 {ECO:0000312|MGI:MGI:1858916};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=2174398; DOI=10.1016/0378-1119(90)90372-x;
RA Nottenburg C., Gallatin W.M., St John T.;
RT "Lymphocyte HEV adhesion variants differ in the expression of multiple gene
RT sequences.";
RL Gene 95:279-284(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-247 AND THR-250, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 can associate with cellular membranes, actin
CC filaments and microtubules. GTPase activity is required for filament
CC formation (By similarity). Interacts with AURKB (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Midbody {ECO:0000250}. Note=Remains at the
CC centrosomes and the nearby microtubules throughout mitosis. Localizes
CC to the midbody during cytokinesis (By similarity). {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37803.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M37030; AAA37803.1; ALT_FRAME; mRNA.
DR EMBL; BC140998; AAI40999.1; -; mRNA.
DR EMBL; BC145081; AAI45082.1; -; mRNA.
DR CCDS; CCDS40141.1; -.
DR PIR; JU0319; JU0319.
DR RefSeq; NP_059489.2; NM_017461.2.
DR AlphaFoldDB; P42209; -.
DR SMR; P42209; -.
DR BioGRID; 207602; 1.
DR IntAct; P42209; 1.
DR STRING; 10090.ENSMUSP00000101921; -.
DR iPTMnet; P42209; -.
DR PhosphoSitePlus; P42209; -.
DR REPRODUCTION-2DPAGE; P42209; -.
DR EPD; P42209; -.
DR jPOST; P42209; -.
DR MaxQB; P42209; -.
DR PaxDb; P42209; -.
DR PeptideAtlas; P42209; -.
DR PRIDE; P42209; -.
DR ProteomicsDB; 255379; -.
DR Antibodypedia; 27233; 274 antibodies from 31 providers.
DR DNASU; 54204; -.
DR Ensembl; ENSMUST00000106314; ENSMUSP00000101921; ENSMUSG00000000486.
DR GeneID; 54204; -.
DR KEGG; mmu:54204; -.
DR UCSC; uc009juq.1; mouse.
DR CTD; 1731; -.
DR MGI; MGI:1858916; Septin1.
DR VEuPathDB; HostDB:ENSMUSG00000000486; -.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000161794; -.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; P42209; -.
DR OMA; EMKGSIP; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; P42209; -.
DR TreeFam; TF101079; -.
DR BioGRID-ORCS; 54204; 0 hits in 48 CRISPR screens.
DR ChiTaRS; Sept1; mouse.
DR PRO; PR:P42209; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P42209; protein.
DR Bgee; ENSMUSG00000000486; Expressed in granulocyte and 107 other tissues.
DR ExpressionAtlas; P42209; baseline and differential.
DR Genevisible; P42209; MM.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0072687; C:meiotic spindle; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:MGI.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
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:MGI.
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:0051311; P:meiotic metaphase plate congression; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0007056; P:spindle assembly involved in female meiosis; IMP:MGI.
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 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 Cell cycle; Cell division; Cytoplasm; Cytoskeleton; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..366
FT /note="Septin-1"
FT /id="PRO_0000173514"
FT DOMAIN 22..295
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 32..39
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 89..92
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 170..173
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 347..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 171..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 306
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q8WYJ6"
FT MOD_RES 314
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q8WYJ6"
FT CONFLICT 99
FT /note="C -> F (in Ref. 1; AAA37803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 42020 MW; AB619C08D8C74184 CRC64;
MDKEYVGFAA LPNQLHRKSV KKGFDFTLMV AGESGLGKST LINSLFLTNL YEDRQVPDAS
ARTAQTLTIE RRGVEIEEGG IKVKLTLVDT PGFGDSVDCS DCWLPVVRFI EEQFEQYLRD
ESGLNRKNIQ DSRVHCCLYF ISPFGRGLRP LDVAFLRAVH EKVNIIPVIG KADALMPRET
QALKQKIRDQ LKEEEINIYQ FPECDSDEDE EFKKQNEEMK ENIPFAVVGS CEVVRDGTRP
VRGRRYSWGT VEVENPHHCD FLNLRRMLVQ THLQDLKEVT HDLLYEGYRA RCLQSLARPG
ARDRASRSKL SRQSATEIPL PMLPLADTEK LIREKDEELR RMQEMLEKMQ AQMQQSQAQG
EQSDVL
