SEP14_MOUSE
ID SEP14_MOUSE Reviewed; 430 AA.
AC Q9DA97; E9QMM2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Septin-14 {ECO:0000312|MGI:MGI:1921472};
GN Name=Septin14 {ECO:0000312|MGI:MGI:1921472};
GN Synonyms=Sept14 {ECO:0000312|MGI:MGI:1921472};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-430.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, INTERACTION WITH SEPTIN4, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20181826; DOI=10.1091/mbc.e09-10-0869;
RA Shinoda T., Ito H., Sudo K., Iwamoto I., Morishita R., Nagata K.;
RT "Septin 14 is involved in cortical neuronal migration via interaction with
RT Septin 4.";
RL Mol. Biol. Cell 21:1324-1334(2010).
RN [5]
RP INTERACTION WITH ACTN4, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=33228246; DOI=10.3390/biomedicines8110518;
RA Lin Y.H., Huang C.Y., Ke C.C., Wang Y.Y., Lai T.H., Liu H.C., Ku W.C.,
RA Chan C.C., Lin Y.H.;
RT "ACTN4 Mediates SEPT14 Mutation-Induced Sperm Head Defects.";
RL Biomedicines 8:0-0(2020).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (Probable). Involved in
CC the migration of cortical neurons and the formation of neuron leading
CC processes during embryonic development (PubMed:20181826). Plays a role
CC in sperm head formation during spermiogenesis, potentially via
CC facilitating localization of ACTN4 to cell filaments (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZU15, ECO:0000269|PubMed:20181826,
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. GTPase activity is required for filament
CC formation. Interacts with ACTN4 (PubMed:33228246). Interacts with
CC SEPTIN9 (By similarity). Interacts (via C-terminus) with SEPTIN4
CC (PubMed:20181826). {ECO:0000250|UniProtKB:Q6ZU15,
CC ECO:0000269|PubMed:20181826, ECO:0000269|PubMed:33228246}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20181826}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33228246}. Cell projection,
CC axon {ECO:0000269|PubMed:20181826}. Cell projection, dendrite
CC {ECO:0000269|PubMed:20181826}. Perikaryon
CC {ECO:0000269|PubMed:20181826}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:33228246}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:Q6ZU15}. Note=Colocalizes with actin
CC stress fibers (By similarity). Expressed in the perinuclear rim and
CC manchette structure in early elongating spermatids during
CC spermiogenesis (PubMed:33228246). {ECO:0000250|UniProtKB:Q6ZU15,
CC ECO:0000269|PubMed:33228246}.
CC -!- TISSUE SPECIFICITY: Expressed in the testis and brain including the
CC cerebrum, hippocampus and cerebellum (at protein level).
CC {ECO:0000269|PubMed:20181826}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the cerebral cortex from 15.5 dpc
CC reaching maximum expression at 17.5 dpc, expression remains robust
CC until P30 (PubMed:20181826). Expressed in early elongating spermatids
CC during spermiogenesis (PubMed:33228246). {ECO:0000269|PubMed:20181826,
CC ECO:0000269|PubMed:33228246}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24381.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AC120413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK006043; BAB24381.1; ALT_SEQ; mRNA.
DR RefSeq; NP_083102.1; NM_028826.1.
DR AlphaFoldDB; Q9DA97; -.
DR SMR; Q9DA97; -.
DR BioGRID; 216586; 2.
DR STRING; 10090.ENSMUSP00000044272; -.
DR iPTMnet; Q9DA97; -.
DR PhosphoSitePlus; Q9DA97; -.
DR jPOST; Q9DA97; -.
DR MaxQB; Q9DA97; -.
DR PaxDb; Q9DA97; -.
DR PeptideAtlas; Q9DA97; -.
DR PRIDE; Q9DA97; -.
DR ProteomicsDB; 256778; -.
DR Antibodypedia; 56888; 97 antibodies from 20 providers.
DR Ensembl; ENSMUST00000042266; ENSMUSP00000044272; ENSMUSG00000034219.
DR GeneID; 74222; -.
DR KEGG; mmu:74222; -.
DR CTD; 346288; -.
DR MGI; MGI:1921472; Septin14.
DR VEuPathDB; HostDB:ENSMUSG00000034219; -.
DR eggNOG; KOG3859; Eukaryota.
DR GeneTree; ENSGT00940000161752; -.
DR InParanoid; Q9DA97; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9DA97; -.
DR TreeFam; TF101080; -.
DR BioGRID-ORCS; 74222; 1 hit in 47 CRISPR screens.
DR PRO; PR:Q9DA97; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9DA97; protein.
DR Bgee; ENSMUSG00000034219; Expressed in animal zygote and 6 other tissues.
DR ExpressionAtlas; Q9DA97; baseline and differential.
DR Genevisible; Q9DA97; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; 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:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; 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 PIRSF; PIRSF006698; 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; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; GTP-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..430
FT /note="Septin-14"
FT /id="PRO_0000294426"
FT DOMAIN 48..313
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 58..65
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 193..196
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 367..430
FT /note="Required for interaction with SEPTIN4. Required for
FT migration of cortical neurons during corticogenesis"
FT /evidence="ECO:0000269|PubMed:20181826"
FT COILED 329..410
FT /evidence="ECO:0000255"
FT BINDING 58..65
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 194..202
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 270
FT /note="Missing (in Ref. 2; BAB24381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 49811 MW; 769580BADF745878 CRC64;
MAEKPTNTSV PIPGSEDPQK ENIRCLSTLG HFGFECLPTQ LVNKSIQKGF SFNILCVGET
GIGKTTLINT LFNTNLKETK SSHFYSKVGL TVKTYELLER NIPLRLTVVK TVGYGDQINK
EASYQPVVDY LDAQFEAYLQ EELKIKRSLA DYHDSRIHVC LYFITPTGHS LKSLDLLTMK
SIDRRVNIIP LIAKADSLSK NDLQRFKNNI MSELNSNGIQ IYQFQVDDEA SAQVNSSGLL
PFAVVGSMEE VKVGKRMVRG RHYPWGVLQE VENENHCDFV KLRDLLLSTN MEDLKDQTHT
QHYECYRSNR LQKLGFSDTG PDNRPVSFQE MYEAKRREFH NQCQKEEEEL KQTFMQRVKE
KELTFKDAEK ELQDKFEHLK RIQQEEILKL EEERRKLEEQ IIDFYKMKAA SESAQAQVCT
NIKKDKDRKK
