SEPT2_RAT
ID SEPT2_RAT Reviewed; 361 AA.
AC Q91Y81;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Septin-2;
DE AltName: Full=Vascular endothelial cell specific protein 11;
GN Name=Septin2 {ECO:0000250|UniProtKB:Q15019};
GN Synonyms=Sept2 {ECO:0000312|RGD:620056}, Vesp11;
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 TISSUE=Liver;
RA Aoki T., Toyoda H., Nishimoto S., Tawara J., Komurasak T.;
RT "Identification of VESP11, a vascular endothelial cell specific protein.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 51-66 AND 117-139, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP 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-218, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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. Forms a filamentous
CC structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the
CC sperm annulus which is required for the structural integrity and
CC motility of the sperm tail during postmeiotic differentiation (By
CC similarity). Required for normal organization of the actin
CC cytoskeleton. Plays a role in the biogenesis of polarized columnar-
CC shaped epithelium by maintaining polyglutamylated microtubules, thus
CC facilitating efficient vesicle transport, and by impeding MAP4 binding
CC to tubulin. Required for the progression through mitosis. Forms a
CC scaffold at the midplane of the mitotic splindle required to maintain
CC CENPE localization at kinetochores and consequently chromosome
CC congression. During anaphase, may be required for chromosome
CC segregation and spindle elongation. Plays a role in ciliogenesis and
CC collective cell movements. In cilia, required for the integrity of the
CC diffusion barrier at the base of the primary cilium that prevents
CC diffusion of transmembrane proteins between the cilia and plasma
CC membranes: probably acts by regulating the assembly of the tectonic-
CC like complex (also named B9 complex) by localizing TMEM231 protein (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q15019}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and associate with cellular membranes, actin
CC filaments and microtubules (By similarity). GTPase activity is required
CC for filament formation (By similarity). Septin filaments are assembled
CC from asymmetrical heterotrimers, composed of SEPTIN2, SEPTIN6 and
CC SEPTIN7 that associate head-to-head to form a hexameric unit (By
CC similarity). Interaction between SEPTIN2 and SEPTIN7 seems indirect
CC (PubMed:15485874). Interacts also with SEPTIN9 and SEPTIN5 (By
CC similarity). Interaction with SEPTIN4 not detected (By similarity).
CC Component of a septin core octomeric complex consisting of SEPTIN12,
CC SEPTIN7, SEPTIN6 and SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12
CC or 12-7-6-4-4-6-7-12 and located in the sperm annulus (By similarity).
CC Interacts with MAP4 (By similarity). Interacts with DZIP1L (By
CC similarity). {ECO:0000250|UniProtKB:P42208,
CC ECO:0000250|UniProtKB:Q15019, ECO:0000269|PubMed:15485874}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage
CC furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasm, cell cortex
CC {ECO:0000250}. Cell projection, cilium membrane {ECO:0000250}. Cell
CC projection, cilium, flagellum {ECO:0000250|UniProtKB:Q15019}. Note=In
CC metaphase cells, localized within the microtubule spindle. At the
CC metaphase plate, in close apposition to the kinetochores of the
CC congressed chromosomes. In cells undergoing cytokinesis, localized to
CC the midbody, the ingressing cleavage furrow, and the central spindle.
CC Localizes at the base of the cilia near the morphological distinction
CC between the cilia and plasma membranes. Found in the sperm annulus (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q15019}.
CC -!- MISCELLANEOUS: Coordinated expression with SEPTIN2 and SEPTIN7.
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; AB027561; BAB47151.1; -; mRNA.
DR EMBL; BC081745; AAH81745.1; -; mRNA.
DR RefSeq; NP_476489.1; NM_057148.2.
DR RefSeq; XP_006245574.1; XM_006245512.3.
DR RefSeq; XP_006245576.1; XM_006245514.1.
DR AlphaFoldDB; Q91Y81; -.
DR SMR; Q91Y81; -.
DR BioGRID; 250737; 2.
DR IntAct; Q91Y81; 4.
DR MINT; Q91Y81; -.
DR STRING; 10116.ENSRNOP00000024261; -.
DR iPTMnet; Q91Y81; -.
DR PhosphoSitePlus; Q91Y81; -.
DR World-2DPAGE; 0004:Q91Y81; -.
DR jPOST; Q91Y81; -.
DR PaxDb; Q91Y81; -.
DR PRIDE; Q91Y81; -.
DR GeneID; 117515; -.
DR KEGG; rno:117515; -.
DR UCSC; RGD:620056; rat.
DR CTD; 4735; -.
DR RGD; 620056; Sept2.
DR VEuPathDB; HostDB:ENSRNOG00000017952; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; Q91Y81; -.
DR OMA; EASHAEI; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q91Y81; -.
DR TreeFam; TF101079; -.
DR PRO; PR:Q91Y81; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000017952; Expressed in lung and 20 other tissues.
DR Genevisible; Q91Y81; RN.
DR GO; GO:0005930; C:axoneme; ISO:RGD.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; ISO:RGD.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0000145; C:exocyst; IDA:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0097730; C:non-motile cilium; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0031105; C:septin complex; ISO:RGD.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0097227; C:sperm annulus; ISO:RGD.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; 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; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IMP: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:0002036; P:regulation of L-glutamate import across plasma membrane; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0007224; P:smoothened signaling pathway; 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; IPR008113; Septin2.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01740; SEPTIN2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cell membrane; Cell projection;
KW Cilium; Cytoplasm; Cytoskeleton; Differentiation;
KW Direct protein sequencing; Flagellum; GTP-binding; Membrane; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Spermatogenesis.
FT CHAIN 1..361
FT /note="Septin-2"
FT /id="PRO_0000270208"
FT DOMAIN 34..306
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 44..51
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 101..104
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 182..185
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 260..270
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT BINDING 44..51
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 183..191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT SITE 156
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT MOD_RES 17
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P42208"
FT MOD_RES 190
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15019"
FT MOD_RES 211
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15019"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
SQ SEQUENCE 361 AA; 41593 MW; C4B9335F18098641 CRC64;
MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT
DLYPERIIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN SRDCFKTIIS
YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV
IAKADTLTLK ERERLKKRIL DEIEEHSIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV
GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR
SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DTDSSTLGHH
V
