SEPT2_PONAB
ID SEPT2_PONAB Reviewed; 361 AA.
AC Q5RA66; Q5R7I0;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Septin-2;
GN Name=SEPTIN2 {ECO:0000250|UniProtKB:Q15019}; Synonyms=SEPT2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. 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 (By similarity). Interaction between SEPTIN2 and
CC SEPTIN7 seems indirect. Interacts with SEPTIN5 (By similarity).
CC Interaction with SEPTIN4 not detected (By similarity). Interacts with
CC SEPTIN9. Component of a septin core octomeric complex consisting of
CC SEPTIN12, SEPTIN7, SEPTIN6 and SEPTIN2 or SEPTIN4 in the order 12-7-6-
CC 2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm annulus.
CC Interacts with MAP4. Interacts with DZIP1L (By similarity).
CC {ECO:0000250|UniProtKB:P42208, ECO:0000250|UniProtKB:Q15019}.
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 SEPTIN6 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; CR857766; CAH90031.1; -; mRNA.
DR EMBL; CR859154; CAH91344.1; -; mRNA.
DR EMBL; CR860136; CAH92280.1; -; mRNA.
DR RefSeq; NP_001124967.1; NM_001131495.1.
DR RefSeq; XP_009236628.1; XM_009238353.1.
DR RefSeq; XP_009236629.1; XM_009238354.1.
DR RefSeq; XP_009236630.1; XM_009238355.1.
DR RefSeq; XP_009236631.1; XM_009238356.1.
DR RefSeq; XP_009236632.1; XM_009238357.1.
DR RefSeq; XP_009236633.1; XM_009238358.1.
DR RefSeq; XP_009236634.1; XM_009238359.1.
DR AlphaFoldDB; Q5RA66; -.
DR SMR; Q5RA66; -.
DR STRING; 9601.ENSPPYP00000014937; -.
DR Ensembl; ENSPPYT00000015536; ENSPPYP00000014937; ENSPPYG00000013353.
DR GeneID; 100171840; -.
DR KEGG; pon:100171840; -.
DR CTD; 4735; -.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000155098; -.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; Q5RA66; -.
DR OMA; EASHAEI; -.
DR OrthoDB; 845354at2759; -.
DR TreeFam; TF101079; -.
DR Proteomes; UP000001595; Chromosome 2B.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Cell membrane; Cell projection;
KW Cilium; Cytoplasm; Cytoskeleton; Differentiation; Flagellum; GTP-binding;
KW Membrane; Mitosis; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Spermatogenesis.
FT CHAIN 1..361
FT /note="Septin-2"
FT /id="PRO_0000230298"
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:0000250|UniProtKB:Q15019"
FT CONFLICT 197
FT /note="K -> Q (in Ref. 1; CAH92280)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="M -> T (in Ref. 1; CAH92280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 41503 MW; 12CCBBE3081E992F CRC64;
MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT
DLYPERVIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS
YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV
IAKADTLTLK ERERLKKRIL DEIEEHNIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV
GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR
SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DGDGGSLGHH
V
