ID   SEP11_PONAB             Reviewed;         425 AA.
AC   Q5R8U3;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Septin-11;
GN   Name=SEPTIN11 {ECO:0000250|UniProtKB:Q9NVA2}; Synonyms=SEPT11;
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;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in
CC       cytokinesis (Potential). May play a role in the cytoarchitecture of
CC       neurons, including dendritic arborization and dendritic spines, and in
CC       GABAergic synaptic connectivity (By similarity). {ECO:0000250,
CC       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 (By similarity). Forms homooligomers (By
CC       similarity). GTPase activity is required for filament formation (By
CC       similarity). Interacts with SEPTIN7, SEPTIN9 and SEPTIN12 (By
CC       similarity). {ECO:0000250|UniProtKB:Q9NVA2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Synapse. Cell
CC       projection, dendritic spine. Cell projection, axon {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; CR859656; CAH91817.1; -; mRNA.
DR   RefSeq; NP_001127466.1; NM_001133994.1.
DR   AlphaFoldDB; Q5R8U3; -.
DR   SMR; Q5R8U3; -.
DR   STRING; 9601.ENSPPYP00000016596; -.
DR   PRIDE; Q5R8U3; -.
DR   GeneID; 100174539; -.
DR   KEGG; pon:100174539; -.
DR   CTD; 55752; -.
DR   eggNOG; KOG3859; Eukaryota.
DR   InParanoid; Q5R8U3; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; 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   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51719; G_SEPTIN; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cell projection; Coiled coil; Cytoplasm;
KW   Cytoskeleton; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Synapse.
FT   CHAIN           1..425
FT                   /note="Septin-11"
FT                   /id="PRO_0000173544"
FT   DOMAIN          38..304
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          48..55
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          100..103
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          183..186
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          399..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          320..413
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        399..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         48..55
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         184..192
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVA2"
SQ   SEQUENCE   425 AA;  49033 MW;  A007753857F2ABED CRC64;
     MVVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET GIGKSTLMDT
     LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD TVGFGDQINK DDSYKPIVEY
     IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP
     IIAKADTIAK NELHKFKSKI MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST
     EEVKIGNKMA KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC
     KLEEMGFKDT DPDSKPFSLQ ETYKAKRNEF LGELQKKEEE MRQMFVMRVK EKEAELKEAE
     KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVNNFQKKKA AAQLLQSQAQ QSGAQQTKKD
     KDKKK