SEPT2_CHICK
ID SEPT2_CHICK Reviewed; 349 AA.
AC Q5ZMH1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Septin-2;
GN Name=SEPTIN2 {ECO:0000250|UniProtKB:Q15019}; Synonyms=SEPT2;
GN ORFNames=RCJMB04_2a21;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal
CC organization of the actin cytoskeleton. Plays a role in the biogenesis
CC of polarized columnar-shaped epithelium by maintaining polyglutamylated
CC microtubules, thus facilitating efficient vesicle transport, and by
CC impeding MAP4 binding to tubulin. Required for the progression through
CC mitosis. Forms a scaffold at the midplane of the mitotic splindle
CC required to maintain CENPE localization at kinetochores and
CC consequently chromosome congression. During anaphase, may be required
CC for chromosome segregation and spindle elongation. Plays a role in
CC ciliogenesis and collective cell movements. In cilia, required for the
CC integrity of the diffusion barrier at the base of the primary cilium
CC that prevents diffusion of transmembrane proteins between the cilia and
CC plasma membranes (By similarity). {ECO:0000250}.
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. Can form heterooligomers with other family members and form
CC filaments (By similarity). {ECO:0000250}.
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}.
CC Note=Localizes at the base of the cilia near the morphological
CC distinction between the cilia and plasma membranes. {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; AJ719413; CAG31072.1; -; mRNA.
DR RefSeq; NP_001006182.1; NM_001006182.1.
DR RefSeq; XP_015130724.1; XM_015275238.1.
DR RefSeq; XP_015130725.1; XM_015275239.1.
DR AlphaFoldDB; Q5ZMH1; -.
DR SMR; Q5ZMH1; -.
DR STRING; 9031.ENSGALP00000002520; -.
DR PaxDb; Q5ZMH1; -.
DR Ensembl; ENSGALT00000002523; ENSGALP00000002520; ENSGALG00000001652.
DR Ensembl; ENSGALT00000089697; ENSGALP00000060286; ENSGALG00000001652.
DR GeneID; 416777; -.
DR KEGG; gga:416777; -.
DR CTD; 416777; -.
DR VEuPathDB; HostDB:geneid_416777; -.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000164668; -.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; Q5ZMH1; -.
DR OMA; AKFKRNI; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q5ZMH1; -.
DR PRO; PR:Q5ZMH1; -.
DR Proteomes; UP000000539; Chromosome 15.
DR Bgee; ENSGALG00000001652; Expressed in ovary and 14 other tissues.
DR ExpressionAtlas; Q5ZMH1; baseline and differential.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
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:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB.
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 Cell cycle; Cell division; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; GTP-binding; Membrane; Mitosis; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..349
FT /note="Septin-2"
FT /id="PRO_0000363220"
FT DOMAIN 33..305
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 43..50
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 181..184
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 259..269
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT BINDING 43..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 77
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 182..190
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT SITE 155
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
SQ SEQUENCE 349 AA; 40225 MW; FE60AE649E6F728D CRC64;
MSQSGEKVKF SDSAGYVGFA NLPNQVHRKS VKKGFEFTLM VVGESGLGKS TLINSLFLTD
LYPERYIPGA AEKIERTVQI EASTVEIEER GVKLRLTVVD TPGYGDAINS QDCFKTIIQY
IDNQFERYLH DESGLNRRHI IDNRVHCCFY FISPFGHGLK PLDVEFMKAL HGKVNIVPVI
AKADTLTLKE RERLKRRVLD EISEHGIRIY QLPDADSDED EEFKEQTRVL KASIPFAVIG
SNQLIEVKGK KIRGRLYPWG VVEVENPEHN DFLKLRTMLV THMQDLQEVT QDLHYENFRS
ERLKRTGKPV EEEVVDKDRI LQQKEAELRR MQEMIAQMQA QMRMKPGDD
