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 24-JAN-2024, entry version 158. 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 octameric 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 octamer 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 9606-ENSP00000268231; -. DR PeptideAtlas; Q8IYM1; -. DR ProteomicsDB; 71202; -. [Q8IYM1-1] DR ProteomicsDB; 71203; -. [Q8IYM1-2] DR Antibodypedia; 24423; 156 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 AGR; HGNC:26348; -. 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; 5396944at2759; -. DR PhylomeDB; Q8IYM1; -. DR TreeFam; TF101078; -. DR PathwayCommons; Q8IYM1; -. DR SignaLink; Q8IYM1; -. DR SIGNOR; Q8IYM1; -. DR BioGRID-ORCS; 124404; 9 hits in 1076 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 81 other cell types or tissues. DR ExpressionAtlas; Q8IYM1; baseline and differential. 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:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR CDD; cd01850; CDC_Septin; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR030379; G_SEPTIN_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR016491; Septin. DR PANTHER; PTHR18884; SEPTIN; 1. DR PANTHER; PTHR18884:SF66; SEPTIN-12; 1. DR Pfam; PF00735; Septin; 1. DR PIRSF; PIRSF006698; Septin; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51719; G_SEPTIN; 1. DR Genevisible; Q8IYM1; HS. 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 octameric 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 //