SEP12_RAT
ID SEP12_RAT Reviewed; 356 AA.
AC Q4V8G5;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Septin-12;
GN Name=Septin12 {ECO:0000250|UniProtKB:Q8IYM1};
GN Synonyms=Sept12 {ECO:0000312|RGD:1565511};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], HOMODIMERIZATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF SER-61.
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 [LARGE SCALE MRNA].
RC TISSUE=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).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in cytokinesis (Potential). Involved in spermatogenesis.
CC Involved in the morphogenesis of sperm heads and the elongation of
CC sperm tails probably implicating the association with alpha- and beta-
CC tubulins. Forms a filamentous structure with SEPTIN7, SEPTIN6, SEPTIN2
CC and probably SEPTIN4 at the sperm annulus which is required for the
CC structural integrity and motility of the sperm tail during postmeiotic
CC differentiation (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8IYM1, ECO:0000250|UniProtKB:Q9D451,
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 SEPTIN6 and SEPTIN11. Self-associates.
CC Component of a octomeric complex consisting of SEPTIN12, SEPTIN7,
CC SEPTIN6 and SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-
CC 6-4-4-6-7-12 and located in the sperm annulus; the octomer polymerizes
CC into filaments via the SEPTIN12 N- and C-termini; the SEPTIN12:SEPTIN7
CC association is mediated by the GTP-binding domains. Interacts with
CC SPAG4 and LMNB1. Associates with alpha- and beta-tubulins (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8IYM1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cell
CC projection, cilium, flagellum {ECO:0000250|UniProtKB:Q8IYM1,
CC ECO:0000250|UniProtKB:Q9D451, ECO:0000269|PubMed:17685441}. Note=At
CC interphase, forms a filamentous structure in the cytoplasm. During
CC anaphase, translocates to the central spindle region and to the midbody
CC during cytokinesis (By similarity). Found in the sperm annulus.
CC {ECO:0000250, ECO:0000269|PubMed:17685441}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis and epididymis.
CC Component of the sperm tail annulus (at protein level).
CC {ECO:0000269|PubMed:17685441}.
CC -!- DEVELOPMENTAL STAGE: In developing testis, expression increases
CC steadily until sexual maturity (approximately 49 days postpartum) where
CC it remains expressed at a relatively constant level.
CC {ECO:0000269|PubMed:17685441}.
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=AAH97401.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC097401; AAH97401.1; ALT_INIT; mRNA.
DR RefSeq; NP_001094335.1; NM_001100865.1.
DR AlphaFoldDB; Q4V8G5; -.
DR SMR; Q4V8G5; -.
DR IntAct; Q4V8G5; 1.
DR STRING; 10116.ENSRNOP00000057921; -.
DR PaxDb; Q4V8G5; -.
DR Ensembl; ENSRNOT00000061208; ENSRNOP00000057921; ENSRNOG00000003137.
DR GeneID; 363542; -.
DR KEGG; rno:363542; -.
DR UCSC; RGD:1565511; rat.
DR CTD; 124404; -.
DR RGD; 1565511; Sept12.
DR eggNOG; KOG1547; Eukaryota.
DR GeneTree; ENSGT00940000158310; -.
DR HOGENOM; CLU_017718_7_1_1; -.
DR InParanoid; Q4V8G5; -.
DR OMA; AHCEFLL; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q4V8G5; -.
DR TreeFam; TF101078; -.
DR PRO; PR:Q4V8G5; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003137; Expressed in testis and 2 other tissues.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
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:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS: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:0030317; P:flagellated sperm motility; ISO:RGD.
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 Cell cycle; Cell division; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Differentiation; Flagellum; GTP-binding; Nucleotide-binding;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..356
FT /note="Septin-12"
FT /id="PRO_0000312861"
FT DOMAIN 44..315
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..317
FT /note="Interaction with SEPTIN7"
FT /evidence="ECO:0000250|UniProtKB:Q8IYM1"
FT REGION 54..61
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 192..195
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 256..356
FT /note="Self-association (via N-terminus) to polymerize
FT octomeric septin 12-7-6-2/4-2/4-6-7-12 filaments"
FT /evidence="ECO:0000250|UniProtKB:Q8IYM1"
FT REGION 330..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 87
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 193..201
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MUTAGEN 61
FT /note="S->N: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:17685441"
SQ SEQUENCE 356 AA; 40799 MW; 598F80BE45A1F451 CRC64;
MDERRTPSPC SSRPSSPRTP PCEMFGPVGI EAVLDQLRIK AMKTGFEFNI MVVGQSGLGK
STMVNTLFKS KVWQSPAPNL DVPMPQTLEL HSVTHVIEEK GLKLKLTVTD TPGFGDQINN
DKCWDPILSY INQQYEQYLQ EELLITRQRH IPDTRVHCCV YFVPPTGHCL RPLDIEFLRR
LCRTVNVVPV IARADSLTIE ERDAFRSRIQ QNLKNHCIDV YPQQCFDEDI NDRLLNSKIR
EQIPFAVVGA DREHIVNGRC VLGRKTKWGI IEVENMAHCE FLLLRDLLIR SHLQDLKDIT
HNVHYENYRV LRLNESHVLP RGPGWVNLAP ASPGQLMAPG PEKVRKRSKD PRDDEC
