SDLCA_SOYBN
ID SDLCA_SOYBN Reviewed; 610 AA.
AC Q39821;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Dynamin-related protein 12A;
DE AltName: Full=Phragmoplastin;
DE AltName: Full=Soybean dynamin-like protein 12A;
DE Short=SDL12A;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Prize; TISSUE=Root nodule;
RX PubMed=8631291; DOI=10.1002/j.1460-2075.1996.tb00405.x;
RA Gu X., Verma D.P.S.;
RT "Phragmoplastin, a dynamin-like protein associated with cell plate
RT formation in plants.";
RL EMBO J. 15:695-704(1996).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9061948; DOI=10.2307/3870538;
RA Gu X., Verma D.P.S.;
RT "Dynamics of phragmoplastin in living cells during cell plate formation and
RT uncoupling of cell elongation from the plane of cell division.";
RL Plant Cell 9:157-169(1997).
RN [3]
RP INTERACTION WITH CALS1.
RX PubMed=11283334; DOI=10.2307/3871338;
RA Hong Z., Delauney A.J., Verma D.P.S.;
RT "A cell plate-specific callose synthase and its interaction with
RT phragmoplastin.";
RL Plant Cell 13:755-768(2001).
RN [4]
RP INTERACTION WITH UGT1.
RX PubMed=11283335; DOI=10.2307/3871339;
RA Hong Z., Zhang Z., Olson J.M., Verma D.P.S.;
RT "A novel UDP-glucose transferase is part of the callose synthase complex
RT and interacts with phragmoplastin at the forming cell plate.";
RL Plant Cell 13:769-779(2001).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF LYS-47.
RX PubMed=14750520; DOI=10.1023/b:plan.0000006936.50532.3a;
RA Hong Z., Geisler-Lee C.J., Zhang Z., Verma D.P.S.;
RT "Phragmoplastin dynamics: multiple forms, microtubule association and their
RT roles in cell plate formation in plants.";
RL Plant Mol. Biol. 53:297-312(2003).
CC -!- FUNCTION: Microtubule-associated force-producing protein that is
CC targeted to the forming cell plate during cytokinesis. May be involved
CC in attaching Golgi-derived vesicles to microtubules which direct
CC vesicles to the forming cell plate during cytokinesis. Possesses
CC intrinsic GTPase activity in vitro. {ECO:0000269|PubMed:14750520,
CC ECO:0000269|PubMed:8631291, ECO:0000269|PubMed:9061948}.
CC -!- SUBUNIT: May homooligomerize and heterooligomerize. May interact with
CC CALS1 and UGT1. {ECO:0000269|PubMed:9061948}.
CC -!- INTERACTION:
CC Q39821; Q9LR44: UGT75B1; Xeno; NbExp=2; IntAct=EBI-1765815, EBI-1765823;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:9061948}. Note=Localized in the forming cell plate
CC during cytokinesis (at protein level). {ECO:0000269|PubMed:9061948}.
CC -!- TISSUE SPECIFICITY: Expressed in seedling root tips and root elongation
CC zones, young root nodules and young leaves.
CC {ECO:0000269|PubMed:8631291}.
CC -!- MISCELLANEOUS: The term phragmoplastin refers to the location of the
CC protein to the phragmoplast across the whole width of the newly formed
CC cell plate, unlike phragmoplast microtubules which are concentrated on
CC the periphery of the forming plate.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; U25547; AAB05992.1; -; mRNA.
DR PIR; S63667; S63667.
DR RefSeq; NP_001235175.1; NM_001248246.1.
DR AlphaFoldDB; Q39821; -.
DR SMR; Q39821; -.
DR IntAct; Q39821; 2.
DR STRING; 3847.GLYMA05G36840.1; -.
DR PRIDE; Q39821; -.
DR GeneID; 547855; -.
DR KEGG; gmx:547855; -.
DR eggNOG; KOG0446; Eukaryota.
DR OrthoDB; 264244at2759; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; 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:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..610
FT /note="Dynamin-related protein 12A"
FT /id="PRO_0000334586"
FT DOMAIN 31..300
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 518..610
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 41..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 67..69
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 142..145
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 211..214
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 241..244
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT BINDING 44..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P42697"
FT BINDING 212..217
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P42697"
FT BINDING 242..245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P42697"
FT MUTAGEN 47
FT /note="K->M: Dominant negative. Loss of GTPase activity and
FT reduced transport of vesicles to the cell plate."
FT /evidence="ECO:0000269|PubMed:14750520"
SQ SEQUENCE 610 AA; 68356 MW; 62AF611E6A615F15 CRC64;
MENLISLVNK IQRACTALGD HGENSALPTL WDSLPAIAVV GGQSSGKSSV LESVVGKDFL
PRGSGIVTRR PLVLQLHKID EGSREYAEFL HLPRKRFTDF VAVRKEIQDE TDRETGRTKQ
ISSVPIHLSI YSPNVVNLTL IDLPGLTKVA VEGQPDSIVK DIEDMVRSYI EKPNCIILAI
SPANQDLATS DAIKISREVD PTGDRTIGVL TKIDLMDKGT DAVDILEGRA YRLKFPWIGV
VNRSQQDINK NVDMIAARRR EREYFNSTPE YKHLANRMGS EHLAKMLSKH LETVIKSKIP
GIQSLINKTI AELEAELTRL GKPVAADAGG KLYAIMEICR SFDQIFKDHL DGVRPGGDKI
YNVFDNQLPA ALKRLQFDKQ LSMENIRKLI TEADGYQPHL IAPEQGYRRL IESSLITIRG
PAESAVDAVH SLLKDLVHKA MSETLDLKQY PGLRVEVGAA SVDSLERMRD ESKRATLQLV
DMECGYLTVD FFRKLPQDVD KGGNPTHSIC DRYNDSYLRR IGTTILSYVN MVCATLRHSI
PKSIVYCQVR EAKRSLLDHF FTELGKMEIK RLSSLLNEDP AIMERRSALA KRLELYRSAQ
AEIDAVAWSK
