SEP12_HUMAN
ID SEP12_HUMAN Reviewed; 358 AA.
AC Q8IYM1; Q0P6B0; Q1PBH0; Q96LL0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Septin-12;
GN Name=SEPTIN12 {ECO:0000312|HGNC:HGNC:26348}; Synonyms=SEPT12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING (ISOFORM
RP 1).
RX PubMed=17685441; DOI=10.1002/cm.20224;
RA Steels J.D., Estey M.P., Froese C.D., Reynaud D., Pace-Asciak C.,
RA Trimble W.S.;
RT "Sept12 is a component of the mammalian sperm tail annulus.";
RL Cell Motil. Cytoskeleton 64:794-807(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SEPTIN6 AND
RP SEPTIN11, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=18047794; DOI=10.5483/bmbrep.2007.40.6.973;
RA Ding X., Yu W., Liu M., Shen S., Chen F., Wan B., Yu L.;
RT "SEPT12 interacts with SEPT6 and this interaction alters the filament
RT structure of SEPT6 in Hela cells.";
RL J. Biochem. Mol. Biol. 40:973-978(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wang J.R., Xing X.W., Jiang X.Z., Tang Y.X., Yang J.F., Dai Y.B., Tan J.;
RT "Molecular cloning of septin 12 transcript variant 2 from human testis.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15915442; DOI=10.1002/path.1789;
RA Hall P.A., Jung K., Hillan K.J., Russell S.E.H.;
RT "Expression profiling the human septin gene family.";
RL J. Pathol. 206:269-278(2005).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=17967425; DOI=10.1016/j.febslet.2007.10.032;
RA Cao L., Ding X., Yu W., Yang X., Shen S., Yu L.;
RT "Phylogenetic and evolutionary analysis of the septin protein family in
RT metazoan.";
RL FEBS Lett. 581:5526-5532(2007).
RN [9]
RP HOMODIMERIZATION, INTERACTION WITH SEPTIN11, GTP-BINDING, AND MUTAGENESIS
RP OF GLY-56.
RX PubMed=18443421;
RA Ding X., Yu W., Liu M., Shen S., Chen F., Cao L., Wan B., Yu L.;
RT "GTP binding is required for SEPT12 to form filaments and to interact with
RT SEPT11.";
RL Mol. Cells 25:385-389(2008).
RN [10]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=20801438; DOI=10.1016/j.fertnstert.2010.07.1064;
RA Lin Y.H., Chou C.K., Hung Y.C., Yu I.S., Pan H.A., Lin S.W., Kuo P.L.;
RT "SEPT12 deficiency causes sperm nucleus damage and developmental arrest of
RT preimplantation embryos.";
RL Fertil. Steril. 95:363-365(2011).
RN [11]
RP SUBCELLULAR LOCATION, VARIANTS SPGF10 MET-89 AND ASN-197, AND
RP CHARACTERIZATION OF VARIANTS SPGF10 MET-89 AND ASN-197.
RX PubMed=22275165; DOI=10.1002/humu.22028;
RA Kuo Y.C., Lin Y.H., Chen H.I., Wang Y.Y., Chiou Y.W., Lin H.H., Pan H.A.,
RA Wu C.M., Su S.M., Hsu C.C., Kuo P.L.;
RT "SEPT12 mutations cause male infertility with defective sperm annulus.";
RL Hum. Mutat. 33:710-719(2012).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=24213608; DOI=10.3390/ijms141122102;
RA Kuo P.L., Chiang H.S., Wang Y.Y., Kuo Y.C., Chen M.F., Yu I.S., Teng Y.N.,
RA Lin S.W., Lin Y.H.;
RT "SEPT12-microtubule complexes are required for sperm head and tail
RT formation.";
RL Int. J. Mol. Sci. 14:22102-22116(2013).
RN [13]
RP FUNCTION, SUBUNIT, AND CHARACTERIZATION OF VARIANTS SPGF10 MET-89 AND
RP ASN-197.
RX PubMed=25588830; DOI=10.1242/jcs.158998;
RA Kuo Y.C., Shen Y.R., Chen H.I., Lin Y.H., Wang Y.Y., Chen Y.R., Wang C.Y.,
RA Kuo P.L.;
RT "SEPT12 orchestrates the formation of mammalian sperm annulus by organizing
RT core octomeric complexes with other SEPT proteins.";
RL J. Cell Sci. 128:923-934(2015).
RN [14]
RP INTERACTION WITH SPAG4 AND LMNB1, SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION OF VARIANTS SPGF10 MET-89 AND ASN-197.
RX PubMed=25775403; DOI=10.1371/journal.pone.0120722;
RA Yeh C.H., Kuo P.L., Wang Y.Y., Wu Y.Y., Chen M.F., Lin D.Y., Lai T.H.,
RA Chiang H.S., Lin Y.H.;
RT "SEPT12/SPAG4/LAMINB1 complexes are required for maintaining the integrity
RT of the nuclear envelope in postmeiotic male germ cells.";
RL PLoS ONE 10:E0120722-E0120722(2015).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity).
CC Involved in spermatogenesis. Involved in the morphogenesis of sperm
CC heads and the elongation of sperm tails probably implicating the
CC association with alpha- and beta-tubulins (PubMed:24213608). Forms a
CC filamentous structure with SEPTIN7, SEPTIN6, SEPTIN2 and probably
CC SEPTIN4 at the sperm annulus which is required for the structural
CC integrity and motility of the sperm tail during postmeiotic
CC differentiation (PubMed:25588830). May play a role in cytokinesis
CC (Potential). {ECO:0000250, ECO:0000269|PubMed:24213608,
CC ECO:0000269|PubMed:25588830, 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 (By similarity). Interacts with SEPTIN6 and SEPTIN11. Self-
CC associates. Component of a septin core octomeric complex consisting of
CC SEPTIN12, SEPTIN7, SEPTIN6 and SEPTIN2 or SEPTIN4 in the order 12-7-6-
CC 2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm annulus; the
CC octomer polymerizes into filaments via the SEPTIN12 N- and C-termini;
CC the SEPTIN12:SEPTIN7 association is mediated by the respective GTP-
CC binding domains (PubMed:25588830). Interacts with SPAG4 and LMNB1
CC (PubMed:25775403). Associates with alpha- and beta-tubulins
CC (PubMed:24213608). {ECO:0000250, ECO:0000269|PubMed:18047794,
CC ECO:0000269|PubMed:18443421, ECO:0000269|PubMed:24213608,
CC ECO:0000269|PubMed:25588830}.
CC -!- INTERACTION:
CC Q8IYM1; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-2585067, EBI-748350;
CC Q8IYM1; Q8WYJ6: SEPTIN1; NbExp=12; IntAct=EBI-2585067, EBI-693002;
CC Q8IYM1; Q8IYM1: SEPTIN12; NbExp=5; IntAct=EBI-2585067, EBI-2585067;
CC Q8IYM1; Q15019: SEPTIN2; NbExp=7; IntAct=EBI-2585067, EBI-741220;
CC Q8IYM1; O43236: SEPTIN4; NbExp=5; IntAct=EBI-2585067, EBI-1047513;
CC Q8IYM1; Q99719: SEPTIN5; NbExp=7; IntAct=EBI-2585067, EBI-373345;
CC Q8IYM1; Q14141: SEPTIN6; NbExp=14; IntAct=EBI-2585067, EBI-745901;
CC Q8IYM1; Q16181: SEPTIN7; NbExp=17; IntAct=EBI-2585067, EBI-2009373;
CC Q8IYM1; Q9NPE6: SPAG4; NbExp=6; IntAct=EBI-2585067, EBI-10819434;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18047794}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:18047794}. Nucleus {ECO:0000269|PubMed:25775403}.
CC Cell projection, cilium, flagellum {ECO:0000269|PubMed:22275165}.
CC Note=At interphase, forms a filamentous structure in the cytoplasm.
CC During anaphase, translocates to the central spindle region and to the
CC midbody during cytokinesis. Found in the sperm annulus. Colocalized
CC with SPAG4 at the nuclear periphery in round spermatids, at sperm neck
CC in elongated spermatids and at midpiece regions in ejaculated
CC spermatozoa. {ECO:0000269|PubMed:18047794, ECO:0000269|PubMed:20801438,
CC ECO:0000269|PubMed:22275165, ECO:0000269|PubMed:25775403}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IYM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IYM1-2; Sequence=VSP_029918;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in lymph node.
CC {ECO:0000269|PubMed:15915442, ECO:0000269|PubMed:17967425}.
CC -!- DEVELOPMENTAL STAGE: At the first step of spermiogenesis concentrated
CC around the acrosome. Afterwards expressed between the edge of the
CC acrosome and the perinuclear mantle of the manchette. Next, encircles
CC the upper site of the acrosome and forms the rim of the sperm nucleus.
CC With the formation of mitochondria and mature spermatozoa, localized at
CC the neck and annulus regions. {ECO:0000269|PubMed:20801438}.
CC -!- DISEASE: Spermatogenic failure 10 (SPGF10) [MIM:614822]: An infertility
CC disorder caused by spermatogenesis defects. It results in decreased
CC sperm motility, concentration, and multiple sperm structural defects.
CC The most prominent feature is a defective sperm annulus, a ring
CC structure that demarcates the midpiece and the principal piece of the
CC sperm tail. {ECO:0000269|PubMed:22275165, ECO:0000269|PubMed:25588830,
CC ECO:0000269|PubMed:25775403}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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=AAH24017.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ456996; ABE68946.1; -; mRNA.
DR EMBL; DQ517531; ABF61438.1; -; mRNA.
DR EMBL; EF620906; ABR10901.1; -; mRNA.
DR EMBL; AK058139; BAB71681.1; -; mRNA.
DR EMBL; CH471112; EAW85265.1; -; Genomic_DNA.
DR EMBL; BC024017; AAH24017.1; ALT_INIT; mRNA.
DR EMBL; BC035619; AAH35619.1; -; mRNA.
DR CCDS; CCDS10522.1; -. [Q8IYM1-1]
DR CCDS; CCDS53987.1; -. [Q8IYM1-2]
DR RefSeq; NP_001147930.1; NM_001154458.2. [Q8IYM1-2]
DR RefSeq; NP_653206.2; NM_144605.4. [Q8IYM1-1]
DR RefSeq; XP_006720909.1; XM_006720846.2. [Q8IYM1-1]
DR PDB; 6MQ9; X-ray; 1.86 A; A/B/C/D=46-320.
DR PDB; 6MQB; X-ray; 2.12 A; A=46-320.
DR PDB; 6MQK; X-ray; 2.19 A; A/B/C/D=46-320.
DR PDB; 6MQL; X-ray; 2.17 A; A=46-320.
DR PDBsum; 6MQ9; -.
DR PDBsum; 6MQB; -.
DR PDBsum; 6MQK; -.
DR PDBsum; 6MQL; -.
DR AlphaFoldDB; Q8IYM1; -.
DR SMR; Q8IYM1; -.
DR BioGRID; 125863; 27.
DR IntAct; Q8IYM1; 20.
DR STRING; 9606.ENSP00000268231; -.
DR iPTMnet; Q8IYM1; -.
DR PhosphoSitePlus; Q8IYM1; -.
DR BioMuta; SEPT12; -.
DR DMDM; 74750767; -.
DR MassIVE; Q8IYM1; -.
DR PaxDb; Q8IYM1; -.
DR PeptideAtlas; Q8IYM1; -.
DR PRIDE; Q8IYM1; -.
DR ProteomicsDB; 71202; -. [Q8IYM1-1]
DR ProteomicsDB; 71203; -. [Q8IYM1-2]
DR Antibodypedia; 24423; 151 antibodies from 22 providers.
DR DNASU; 124404; -.
DR Ensembl; ENST00000268231.13; ENSP00000268231.8; ENSG00000140623.14. [Q8IYM1-1]
DR Ensembl; ENST00000396693.9; ENSP00000379922.4; ENSG00000140623.14. [Q8IYM1-2]
DR GeneID; 124404; -.
DR KEGG; hsa:124404; -.
DR MANE-Select; ENST00000268231.13; ENSP00000268231.8; NM_144605.5; NP_653206.2.
DR UCSC; uc002cxq.4; human. [Q8IYM1-1]
DR CTD; 124404; -.
DR DisGeNET; 124404; -.
DR GeneCards; SEPTIN12; -.
DR HGNC; HGNC:26348; SEPTIN12.
DR HPA; ENSG00000140623; Tissue enriched (testis).
DR MalaCards; SEPTIN12; -.
DR MIM; 611562; gene.
DR MIM; 614822; phenotype.
DR neXtProt; NX_Q8IYM1; -.
DR OpenTargets; ENSG00000140623; -.
DR Orphanet; 276234; Non-syndromic male infertility due to sperm motility disorder.
DR PharmGKB; PA162402916; -.
DR VEuPathDB; HostDB:ENSG00000140623; -.
DR eggNOG; KOG1547; Eukaryota.
DR GeneTree; ENSGT00940000158310; -.
DR HOGENOM; CLU_017718_7_1_1; -.
DR InParanoid; Q8IYM1; -.
DR OMA; AHCEFLL; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q8IYM1; -.
DR TreeFam; TF101078; -.
DR PathwayCommons; Q8IYM1; -.
DR SignaLink; Q8IYM1; -.
DR SIGNOR; Q8IYM1; -.
DR BioGRID-ORCS; 124404; 8 hits in 1013 CRISPR screens.
DR GenomeRNAi; 124404; -.
DR Pharos; Q8IYM1; Tbio.
DR PRO; PR:Q8IYM1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8IYM1; protein.
DR Bgee; ENSG00000140623; Expressed in left testis and 80 other tissues.
DR ExpressionAtlas; Q8IYM1; baseline and differential.
DR Genevisible; Q8IYM1; HS.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0097227; C:sperm annulus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
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 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 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW Cell projection; Cilium; Cytoplasm; Cytoskeleton; Differentiation;
KW Disease variant; Flagellum; GTP-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..358
FT /note="Septin-12"
FT /id="PRO_0000312860"
FT DOMAIN 46..317
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..319
FT /note="Interaction with SEPTIN7"
FT /evidence="ECO:0000269|PubMed:25588830"
FT REGION 56..63
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 112..115
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 194..197
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 258..358
FT /note="Self-association (via N-terminus) to polymerize
FT octomeric septin 12-7-6-2/4-2/4-6-7-12 filaments"
FT BINDING 56..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 195..203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 125..170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17685441,
FT ECO:0000303|PubMed:18047794"
FT /id="VSP_029918"
FT VARIANT 89
FT /note="T -> M (in SPGF10; results in significantly reduced
FT GTP hydrolysis; disrupts interaction with SEPTIN7, SEPTIN6
FT and SEPTIN2; decreases interaction with SPAG4;
FT dbSNP:rs199696526)"
FT /evidence="ECO:0000269|PubMed:22275165,
FT ECO:0000269|PubMed:25588830, ECO:0000269|PubMed:25775403"
FT /id="VAR_068097"
FT VARIANT 197
FT /note="D -> N (in SPGF10; results in significantly reduced
FT GTP hydrolysis due to impaired GTP binding; disrupts
FT interaction with SEPTIN7, SEPTIN6 and SEPTIN2; absence of
FT SEPTIN12, SEPTIN7, SEPTIN6, SEPTIN2 and SEPTIN4 from the
FT sperm annulus; disrupts interaction with LMNB1;
FT dbSNP:rs371195126)"
FT /evidence="ECO:0000269|PubMed:22275165,
FT ECO:0000269|PubMed:25588830, ECO:0000269|PubMed:25775403"
FT /id="VAR_068098"
FT VARIANT 213
FT /note="Q -> R (in dbSNP:rs6500633)"
FT /id="VAR_057176"
FT MUTAGEN 56
FT /note="G->N: Abolishes binding to GTP and to SEPTIN11, and
FT also abolishes the ability of SEPTIN12 to form filamentous
FT structures."
FT /evidence="ECO:0000269|PubMed:18443421"
FT CONFLICT 22
FT /note="P -> T (in Ref. 6; AAH24017)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="V -> M (in Ref. 4; BAB71681)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="H -> L (in Ref. 6; AAH24017)"
FT /evidence="ECO:0000305"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:6MQ9"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:6MQ9"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:6MQ9"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:6MQ9"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6MQ9"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:6MQ9"
FT HELIX 127..147
FT /evidence="ECO:0007829|PDB:6MQ9"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6MQ9"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:6MQ9"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:6MQ9"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:6MQ9"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:6MQ9"
FT HELIX 201..217
FT /evidence="ECO:0007829|PDB:6MQ9"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:6MQ9"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:6MQ9"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6MQ9"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:6MQ9"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:6MQ9"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:6MQ9"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:6MQ9"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:6MQ9"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:6MQ9"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:6MQ9"
SQ SEQUENCE 358 AA; 40748 MW; 31968F366DEFB4FD CRC64;
MDPLRRSPSP CLSSQPSSPS TPPCEMLGPV GIEAVLDQLK IKAMKMGFEF NIMVVGQSGL
GKSTMVNTLF KSKVWKSNPP GLGVPTPQTL QLHSLTHVIE EKGVKLKLTV TDTPGFGDQI
NNDNCWDPIL GYINEQYEQY LQEEILITRQ RHIPDTRVHC CVYFVPPTGH CLRPLDIEFL
QRLCRTVNVV PVIARADSLT MEEREAFRRR IQQNLRTHCI DVYPQMCFDE DINDKILNSK
LRDRIPFAVV GADQEHLVNG RCVLGRKTKW GIIEVENMAH CEFPLLRDLL IRSHLQDLKD
ITHNIHYENY RVIRLNESHL LPRGPGWVNL APASPGQLTT PRTFKVCRGA HDDSDDEF
