SEPT7_PANTR
ID SEPT7_PANTR Reviewed; 434 AA.
AC Q5R1W1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Septin-7;
DE AltName: Full=CDC10 protein homolog;
DE Flags: Fragment;
GN Name=SEPTIN7 {ECO:0000250|UniProtKB:Q16181}; Synonyms=CDC10, SEPT7;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RA Hirai M., Sakate R., Hida M., Sugano S., Hayasaka I., Suto Y., Osada N.,
RA Hashimoto K.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal
CC organization of the actin cytoskeleton. Required for normal progress
CC through mitosis. Involved in cytokinesis. Required for normal
CC association of CENPE with the kinetochore. Plays a role in ciliogenesis
CC and collective cell movements. Forms a filamentous structure with
CC SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus
CC which is required for the structural integrity and motility of the
CC sperm tail during postmeiotic differentiation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
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. Within the trimer, directly interacts with
CC SEPTIN6, while interaction with SEPTIN2 seems indirect. In the absence
CC of SEPTIN6, forms homodimers. Interacts directly with CENPE and links
CC CENPE to septin filaments composed of SEPTIN2, SEPTIN6 and SEPTIN7.
CC Interacts with SEPTIN5, SEPTIN8, SEPTIN9 and SEPTIN11. Component of a
CC septin core octomeric complex consisting of SEPTIN12, SEPTIN7, SEPTIN6
CC and SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-
CC 7-12 and located in the sperm annulus; the SEPTIN12:SEPTIN7 association
CC is mediated by the respective GTP-binding domains (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Chromosome, centromere, kinetochore
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage
CC furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasm, cytoskeleton,
CC cilium axoneme {ECO:0000250}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q16181}. Note=Distributed throughout the
CC cytoplasm in prometaphase cells. Associated with the spindle during
CC metaphase. Associated with the central spindle and at the cleavage
CC furrow in anaphase cells. Detected at the midbody in telophase (By
CC similarity). Associated with actin stress fibers. Found in the sperm
CC annulus (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
CC -!- MISCELLANEOUS: Coordinated expression with SEPTIN2 and SEPTIN6.
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; AB188286; BAD74037.1; -; mRNA.
DR RefSeq; NP_001009103.2; NM_001009103.2.
DR RefSeq; NP_001184050.1; NM_001197121.1.
DR AlphaFoldDB; Q5R1W1; -.
DR SMR; Q5R1W1; -.
DR STRING; 9598.ENSPTRP00000054670; -.
DR PaxDb; Q5R1W1; -.
DR GeneID; 463349; -.
DR KEGG; ptr:463349; -.
DR CTD; 989; -.
DR eggNOG; KOG2655; Eukaryota.
DR InParanoid; Q5R1W1; -.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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:0016476; P:regulation of embryonic cell shape; 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; IPR008115; Septin7.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01742; SEPTIN7.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Cell projection; Centromere;
KW Chromosome; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation;
KW Flagellum; GTP-binding; Kinetochore; Mitosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Spermatogenesis.
FT CHAIN <1..434
FT /note="Septin-7"
FT /id="PRO_0000173530"
FT DOMAIN 44..313
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 44..314
FT /note="Interaction with SEPTIN12"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT REGION 54..61
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 110..113
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 191..194
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 377..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 329..434
FT /evidence="ECO:0000255"
FT COMPBIAS 377..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 192..200
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 27
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O55131"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55131"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT MOD_RES 370
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O55131"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT MOD_RES 423
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16181"
FT NON_TER 1
SQ SEQUENCE 434 AA; 50290 MW; CB00032C247F9940 CRC64;
SARSAAAEER SVNSSTMVAQ QKNLEGYVGF ANLPNQVYRK SVKRGFEFTL MVVGESGLGK
STLINSLFLT DLYSPEYPGP SHRIKKTVQV EQSKVLIKEG GVQLLLTIVD TPGFGDAVDN
SNCWQPVIDY IDSKFEDYLN AESRVNRRQM PDNRVQCCLY FIAPSGHGLK PLDIEFMKRL
HEKVNIIPLI AKADTLTPEE CQQFKKQIMK EIQEHKIKIY EFPETDDEEE NKLVKKIKDR
LPLAVVGSNT IIEVNGKRVR GRQYPWGVAE VENGEHCDFT ILRNMLIRTH MQDLKDVTNN
VHYENYRSRK LAAVTYNGVD NNKNKGQLTK SPLAQMEEER REHVAKMKKM EMEMEQVFEM
KVKEKVQKLK DSEAELQRRH EQMKKNLEAQ HKGLEEKRRQ FEDEKANWEA QQRILEQQNS
SRTLEKNKKK GKIF
