SEPT4_RAT
ID SEPT4_RAT Reviewed; 459 AA.
AC A0A096MJN4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Septin-4 {ECO:0000312|RGD:1308781};
DE AltName: Full=Apoptosis-related protein in the TGF-beta signaling pathway {ECO:0000250|UniProtKB:O43236};
DE Short=Arts {ECO:0000250|UniProtKB:O43236};
DE AltName: Full=Bradeion beta {ECO:0000250|UniProtKB:O43236};
DE AltName: Full=Brain protein H5 {ECO:0000250|UniProtKB:P28661};
DE AltName: Full=CE5B3 beta {ECO:0000250|UniProtKB:O43236};
DE AltName: Full=Cell division control-related protein 2 {ECO:0000250|UniProtKB:O43236};
DE Short=hCDCREL-2 {ECO:0000250|UniProtKB:O43236};
DE AltName: Full=Peanut-like protein 2 {ECO:0000250|UniProtKB:O43236};
GN Name=Septin4 {ECO:0000312|RGD:1308781};
GN Synonyms=Arts {ECO:0000250|UniProtKB:O43236},
GN Bh5 {ECO:0000250|UniProtKB:P28661}, Gm11492 {ECO:0000250|UniProtKB:P28661},
GN Pnut12 {ECO:0000250|UniProtKB:P28661}, Sep4 {ECO:0000250|UniProtKB:P28661},
GN Sept4 {ECO:0000312|RGD:1308781};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP INTERACTION WITH DYRK1A.
RX PubMed=18938227; DOI=10.1016/j.neuroscience.2008.09.034;
RA Sitz J.H., Baumgaertel K., Haemmerle B., Papadopoulos C., Hekerman P.,
RA Tejedor F.J., Becker W., Lutz B.;
RT "The Down syndrome candidate dual-specificity tyrosine phosphorylation-
RT regulated kinase 1A phosphorylates the neurodegeneration-related septin
RT 4.";
RL Neuroscience 157:596-605(2008).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. Pro-apoptotic protein
CC involved in LGR5-positive intestinal stem cell and Paneth cell
CC expansion in the intestines, via its interaction with XIAP (By
CC similarity). May also play a role in the regulation of cell fate in the
CC intestine (By similarity). Positive regulator of apoptosis involved in
CC hematopoietic stem cell homeostasis; via its interaction with XIAP (By
CC 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}.
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 (PubMed:18938227). Interacts with
CC SLC6A3/DAT and SNCA/alpha-synuclein. Interacts with STX1A; in the
CC striatum. Interacts with XIAP (via BIR3 domain) following the induction
CC of apoptosis. Interacts with AREL1 (via HECT domain); in the cytoplasm
CC following induction of apoptosis (By similarity).
CC {ECO:0000250|UniProtKB:O43236, ECO:0000250|UniProtKB:P28661,
CC ECO:0000269|PubMed:18938227}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28661}. Cell
CC projection, cilium, flagellum {ECO:0000250|UniProtKB:P28661}.
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}. Note=Found in the sperm annulus, a
CC fibrous ring structure connecting the midpiece and the principal piece
CC of the sperm flagellum (By similarity). In platelets, found in areas
CC surrounding alpha-granules (By similarity). Expressed and colocalized
CC with SLC6A3 and SNCA in axon terminals, especially at the varicosities
CC (By similarity). {ECO:0000250|UniProtKB:O43236,
CC ECO:0000250|UniProtKB:P28661}.
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; AABR07030186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017452610.1; XM_017597121.1.
DR AlphaFoldDB; A0A096MJN4; -.
DR SMR; A0A096MJN4; -.
DR jPOST; A0A096MJN4; -.
DR Ensembl; ENSRNOT00000076026; ENSRNOP00000068198; ENSRNOG00000007367.
DR GeneID; 287606; -.
DR CTD; 5414; -.
DR RGD; 1308781; Septin4.
DR GeneTree; ENSGT00940000157152; -.
DR HOGENOM; CLU_017718_0_1_1; -.
DR OrthoDB; 845354at2759; -.
DR Reactome; R-RNO-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-RNO-111469; SMAC, XIAP-regulated apoptotic response.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000007367; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; A0A096MJN4; baseline and differential.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0031514; C:motile cilium; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; ISO:RGD.
DR GO; GO:0031105; C:septin complex; ISO:RGD.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0097227; C:sperm annulus; ISO:RGD.
DR GO; GO:0036126; C:sperm flagellum; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISO:RGD.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; ISO:RGD.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0048240; P:sperm capacitation; ISO:RGD.
DR GO; GO:0030382; P:sperm mitochondrion organization; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; ISO:RGD.
DR GO; GO:0048515; P:spermatid differentiation; ISO:RGD.
DR GO; GO:0048729; P:tissue morphogenesis; ISO:RGD.
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 1: Evidence at protein 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.
FT CHAIN 1..459
FT /note="Septin-4"
FT /id="PRO_0000454924"
FT DOMAIN 122..395
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 18..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..139
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 189..192
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 270..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 410..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..459
FT /evidence="ECO:0000255"
FT BINDING 132..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 166
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 271..279
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 329
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28661"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28661"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28661"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28661"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28661"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28661"
FT MOD_RES 415
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28661"
SQ SEQUENCE 459 AA; 53083 MW; AAF376992B6E7A65 CRC64;
MIKHFLEDNS DDAELSKFVK DFPGSEPCHP TESKTRVARP QILEPRPQSP DLCDDDVEFR
ATLWSQPSDS QQYFCPPAPL SPSSRPRSPW GKLDPYDSSE DDKEYVGFAT LPNQVHRKSV
KKGFDFTLMV AGESGLGKST LVNSLFLTDL YRDRKLLGAE ERIMQTVEIT KHAVDIEEKG
VRLRLTIVDT PGFGDAVNNT ECWRPVAEYI DQQFEQYFRD ESGLNRKNIQ DNRVHCCLYF
ISPFGHGLRP LDVEFMKALH QRVNIVPILA KADTLTPSEV DRKKCKIREE IEHFGIKIYQ
FPDCDSDEDE DFKLQDQALK ESIPFAVIGS NTVVEARGRR VRGRLYPWGI VEVENPGHCD
FVKLRTMLVR THMQDLKDVT RETHYENYRA QCIQSMTRLV VKERNRNKLT RESGTDFPIP
AVPPGTDPET EKLIREKDEE LRRMQEMLHK IQRQMKETH
