SEPT4_PONAB
ID SEPT4_PONAB Reviewed; 478 AA.
AC Q5R6R7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Septin-4;
GN Name=SEPTIN4 {ECO:0000250|UniProtKB:O43236}; Synonyms=SEPT4;
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 (Probable). Pro-
CC apoptotic protein involved in LGR5-positive intestinal stem cell and
CC Paneth cell expansion in the intestines, via its interaction with XIAP
CC (By similarity). May also play a role in the regulation of cell fate in
CC the intestine (By similarity). Positive regulator of apoptosis involved
CC in hematopoietic stem cell homeostasis; via its interaction with XIAP
CC (By similarity). Negative regulator of repair and hair follicle
CC regeneration in response to injury, due to inhibition of hair follicle
CC stem cell proliferation, potentially via its interaction with XIAP (By
CC similarity). Plays an important role in male fertility and sperm
CC motility (By similarity). During spermiogenesis, essential for the
CC establishment of the annulus (a fibrous ring structure connecting the
CC midpiece and the principal piece of the sperm flagellum) which is a
CC requisite for the structural and mechanical integrity of the sperm (By
CC similarity). Involved in the migration of cortical neurons and the
CC formation of neuron leading processes during embryonic development (By
CC similarity). Required for dopaminergic metabolism in presynaptic
CC autoreceptors; potentially via activity as a presynaptic scaffold
CC protein (By similarity). {ECO:0000250|UniProtKB:P28661, 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. GTPase activity is required for filament
CC formation. Interacts with SEPTIN8 (By similarity). 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 (By similarity). Interacts with SEPTIN14 (via C-terminus) (By
CC similarity). Interacts with DYRK1A (By similarity). Interacts with
CC SLC6A3/DAT and SNCA/alpha-synuclein (By similarity). Interacts with
CC STX1A; in the striatum (By similarity). Interacts with XIAP (via BIR3
CC domain) following the induction of apoptosis (By similarity). Interacts
CC with AREL1 (via HECT domain); in the cytoplasm following induction of
CC apoptosis (By similarity). {ECO:0000250|UniProtKB:O43236,
CC ECO:0000250|UniProtKB:P28661}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28661}. Cell
CC projection, cilium, flagellum {ECO:0000250|UniProtKB:O43236}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:O43236}.
CC Cell projection, axon {ECO:0000250|UniProtKB:P28661}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:P28661}. Perikaryon
CC {ECO:0000250|UniProtKB:P28661}. Synapse {ECO:0000250|UniProtKB:O43236}.
CC Note=In platelets, found in areas surrounding alpha-granules (By
CC similarity). Found in the sperm annulus, a fibrous ring structure
CC connecting the midpiece and the principal piece of the sperm flagellum
CC (By similarity). Expressed and colocalized with SLC6A3 and SNCA in axon
CC terminals, especially at the varicosities (By similarity).
CC {ECO:0000250|UniProtKB:O43236, ECO:0000250|UniProtKB:P28661}.
CC -!- PTM: Ubiquitinated by AREL1. {ECO:0000250|UniProtKB:O43236}.
CC -!- PTM: Phosphorylated by DYRK1A. {ECO:0000250|UniProtKB:P28661}.
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; CR860418; CAH92543.1; -; mRNA.
DR RefSeq; NP_001126242.1; NM_001132770.1.
DR AlphaFoldDB; Q5R6R7; -.
DR SMR; Q5R6R7; -.
DR STRING; 9601.ENSPPYP00000009247; -.
DR GeneID; 100173213; -.
DR KEGG; pon:100173213; -.
DR CTD; 5414; -.
DR eggNOG; KOG2655; Eukaryota.
DR InParanoid; Q5R6R7; -.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0097227; C:sperm annulus; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0048515; P:spermatid differentiation; 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 Pfam; PF00735; 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; Cilium; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Differentiation; Flagellum; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Spermatogenesis;
KW Synapse; Ubl conjugation.
FT CHAIN 1..478
FT /note="Septin-4"
FT /id="PRO_0000230299"
FT DOMAIN 141..414
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 38..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..158
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 208..211
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 289..292
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 425..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 446..478
FT /evidence="ECO:0000255"
FT COMPBIAS 82..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 151..158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 185
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 290..298
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 363
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43236"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43236"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43236"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28661"
FT MOD_RES 434
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28661"
SQ SEQUENCE 478 AA; 55158 MW; C21515D1B13D0596 CRC64;
MDRSLGWQGN SVPEDRTEAG IKRFLEDTTD DGELSKFVKD FSGNESCHPP EAKTWASRPQ
VPEPRPQAPD LYDDDLEFRP PSWPQSSDNQ QYFCAPAPLS PSARPRSPWG KLDPYDSSED
DKEYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL VNSLFLTDLY RDRKLLGAEE
RIMQTVEITK HAVDIEEKGV RLRLTIVDTP GFGDAVNNTE CWKPVAEYID QQFEQYFRDE
SGLNRKNIQD NRVHCCLYFI SPFGHGLRPL DVEFMKALHQ RVNIVPILAK ADTLTPPEVD
RKKRKIREEI EHFGIKIYQF PDCDSDEDED FKLQDQALKE SIPFAVIGSN TVVEARGRRV
RGRLYPWGIV EVENPGHCDF VKLRTMLVRT HMQDLKDVTR ETHYENYRAQ CIQSMTRLVV
KERNRNKLTR ESGTDLPIPA VPPGTDPETE KLIREKDEEL RRMQEMLHKI QKQMKETY
