SEPT1_RAT
ID SEPT1_RAT Reviewed; 366 AA.
AC Q5EB96;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Septin-1 {ECO:0000305};
GN Name=Septin1 {ECO:0000250|UniProtKB:Q8WYJ6};
GN Synonyms=Sept1 {ECO:0000312|RGD:1307216};
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 [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP 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 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}.
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DR EMBL; BC089897; AAH89897.1; -; mRNA.
DR RefSeq; NP_001012478.1; NM_001012460.1.
DR AlphaFoldDB; Q5EB96; -.
DR SMR; Q5EB96; -.
DR STRING; 10116.ENSRNOP00000051893; -.
DR iPTMnet; Q5EB96; -.
DR PhosphoSitePlus; Q5EB96; -.
DR PaxDb; Q5EB96; -.
DR PRIDE; Q5EB96; -.
DR Ensembl; ENSRNOT00000055012; ENSRNOP00000051893; ENSRNOG00000017804.
DR GeneID; 293507; -.
DR KEGG; rno:293507; -.
DR UCSC; RGD:1307216; rat.
DR CTD; 1731; -.
DR RGD; 1307216; Sept1.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000161794; -.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; Q5EB96; -.
DR OMA; EMKGSIP; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q5EB96; -.
DR TreeFam; TF101079; -.
DR PRO; PR:Q5EB96; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017804; Expressed in thymus and 19 other tissues.
DR Genevisible; Q5EB96; RN.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0072687; C:meiotic spindle; ISO:RGD.
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; ISO:RGD.
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:RGD.
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; ISO:RGD.
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; ISO:RGD.
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_0000363219"
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:22673903"
FT MOD_RES 247
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q8WYJ6"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P42209"
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"
SQ SEQUENCE 366 AA; 42058 MW; D5C552D3716A0038 CRC64;
MDKEYVGFAA LPNQLHRKSV KKGFDFTLMV AGESGLGKST LINSLFLTNL YEDRQVPDAS
ARTTQTLTIE RRGVEIEEGG IKVKLTLVDT PGFGDSVDCS DCWLPVVRFI EEQFEQYLRD
ESGLNRKNIQ DSRVHCCLYF ISPFGRGLRP LDVAFLRAVH EKVNIIPVIG KADALLPRET
QVLKQKIRDQ LKEEEINIYQ FPECDSDEDE EFKKQNEEMK ENIPFAVVGS SEVVREGTRP
VRGRRYSWGT VEVENPHHCD FLNLRRMLVQ THLQDLKEVT HDLLYEGYRA RCLQSLARPG
ARDRASRSKL SRQSATEIPL PMLPLADTEK LIREKDEELR RMQEMLEKMQ AQMQQSQAQG
EQSDVL
