DYN1_RAT
ID DYN1_RAT Reviewed; 864 AA.
AC P21575;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Dynamin-1;
DE EC=3.6.5.5;
DE AltName: Full=B-dynamin;
DE AltName: Full=D100;
DE AltName: Full=Dynamin, brain;
GN Name=Dnm1; Synonyms=Dnm;
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] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=2144893; DOI=10.1038/347256a0;
RA Obar R.A., Collins C.A., Hammarback J.A., Shpetner H.S., Vallee R.B.;
RT "Molecular cloning of the microtubule-associated mechanochemical enzyme
RT dynamin reveals homology with a new family of GTP-binding proteins.";
RL Nature 347:256-261(1990).
RN [2]
RP PROTEIN SEQUENCE OF 5-15; 45-54; 67-87; 91-107; 116-157; 167-188; 257-266;
RP 300-315; 328-342; 400-415; 511-522 AND 584-594 (ISOFORM 1/2/3/4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PROTEIN SEQUENCE OF 343-364; 511-522 AND 797-838 (ISOFORM 1/2/4/5/6/8),
RP PROTEIN SEQUENCE OF 847-864 (ISOFORM 1/5), PHOSPHORYLATION AT SER-347;
RP SER-512; SER-774; SER-778; SER-822; SER-851 AND SER-857, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=17376771; DOI=10.1074/jbc.m609713200;
RA Graham M.E., Anggono V., Bache N., Larsen M.R., Craft G.E., Robinson P.J.;
RT "The in vivo phosphorylation sites of rat brain dynamin I.";
RL J. Biol. Chem. 282:14695-14707(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-581 (ISOFORM 5/6/7/8).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 668-864 (ISOFORM 1/5).
RC TISSUE=Brain, and Hypothalamus;
RG Amgen EST program;
RT "Amgen rat EST program.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH AMPH; BIN1 AND SYNJ1.
RX PubMed=9341169; DOI=10.1074/jbc.272.43.27239;
RA Micheva K.D., Kay B.K., McPherson P.S.;
RT "Synaptojanin forms two separate complexes in the nerve terminal.
RT Interactions with endophilin and amphiphysin.";
RL J. Biol. Chem. 272:27239-27245(1997).
RN [7]
RP INTERACTION WITH MYO1E.
RX PubMed=17257598; DOI=10.1016/j.febslet.2007.01.021;
RA Krendel M., Osterweil E.K., Mooseker M.S.;
RT "Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in
RT endocytosis.";
RL FEBS Lett. 581:644-650(2007).
RN [8]
RP INTERACTION WITH SH3GL1; SH3GL2 AND SH3GL3.
RC TISSUE=Brain;
RX PubMed=9238017; DOI=10.1073/pnas.94.16.8569;
RA Ringstad N., Nemoto Y., De Camilli P.;
RT "The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin
RT and dynamin via a Grb2-like Src homology 3 domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8569-8574(1997).
RN [9]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9725914; DOI=10.1091/mbc.9.9.2595;
RA Cao H., Garcia F., McNiven M.A.;
RT "Differential distribution of dynamin isoforms in mammalian cells.";
RL Mol. Biol. Cell 9:2595-2609(1998).
RN [10]
RP ROLE OF PHOSPHORYLATION.
RX PubMed=11672811; DOI=10.1016/s0166-2236(00)01930-5;
RA Cousin M.A., Robinson P.J.;
RT "The dephosphins: dephosphorylation by calcineurin triggers synaptic
RT vesicle endocytosis.";
RL Trends Neurosci. 24:659-665(2001).
RN [11]
RP INTERACTION WITH PHOCN.
RX PubMed=11872741; DOI=10.1074/jbc.m108818200;
RA Baillat G., Gaillard S., Castets F., Monneron A.;
RT "Interactions of phocein with nucleoside-diphosphate kinase, Eps15, and
RT Dynamin I.";
RL J. Biol. Chem. 277:18961-18966(2002).
RN [12]
RP PHOSPHORYLATION BY CDK5.
RX PubMed=12855954; DOI=10.1038/ncb1020;
RA Tan T.C., Valova V.A., Malladi C.S., Graham M.E., Berven L.A., Jupp O.J.,
RA Hansra G., McClure S.J., Sarcevic B., Boadle R.A., Larsen M.R.,
RA Cousin M.A., Robinson P.J.;
RT "Cdk5 is essential for synaptic vesicle endocytosis.";
RL Nat. Cell Biol. 5:701-710(2003).
RN [13]
RP REVIEW ON FUNCTION.
RX PubMed=15649133; DOI=10.1042/bss0720087;
RA Smillie K.J., Cousin M.A.;
RT "Dynamin I phosphorylation and the control of synaptic vesicle
RT endocytosis.";
RL Biochem. Soc. Symp. 72:87-97(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-851 AND SER-857, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 6-304.
RX PubMed=16141317; DOI=10.1073/pnas.0506491102;
RA Reubold T.F., Eschenburg S., Becker A., Leonard M., Schmid S.L.,
RA Vallee R.B., Kull F.J., Manstein D.J.;
RT "Crystal structure of the GTPase domain of rat dynamin 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13093-13098(2005).
CC -!- FUNCTION: Microtubule-associated force-producing protein involved in
CC producing microtubule bundles and able to bind and hydrolyze GTP. Most
CC probably involved in vesicular trafficking processes. Involved in
CC receptor-mediated endocytosis (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC -!- SUBUNIT: Interacts with CAV1 and SH3GLB1. Interacts with SNX9.
CC Interacts with SNX33 (via SH3 domain) (By similarity). Interacts with
CC PHOCN. Interacts with PACSIN1, PACSIN2 and PACSIN3 (By similarity).
CC Binds SH3GL1, SH3GL2 and SH3GL3. Interacts with MYO1E (via SH3 domain).
CC Interacts with UNC119; leading to a decrease of DNM1 GTPase activity
CC (By similarity). Interacts with DIAPH1 (By similarity). Interacts with
CC AMPH, BIN1 AND SYNJ1 (PubMed:9341169). {ECO:0000250|UniProtKB:Q05193,
CC ECO:0000269|PubMed:9341169}.
CC -!- INTERACTION:
CC P21575; O08838: Amph; NbExp=3; IntAct=EBI-80070, EBI-80080;
CC P21575; O08839: Bin1; NbExp=2; IntAct=EBI-80070, EBI-80095;
CC P21575; P21575: Dnm1; NbExp=7; IntAct=EBI-80070, EBI-80070;
CC P21575; P62994: Grb2; NbExp=3; IntAct=EBI-80070, EBI-401775;
CC P21575; Q9Z0W5: Pacsin1; NbExp=4; IntAct=EBI-80070, EBI-1550185;
CC P21575; Q63787: Pik3r1; NbExp=2; IntAct=EBI-80070, EBI-518443;
CC P21575; O35179: Sh3gl2; NbExp=6; IntAct=EBI-80070, EBI-1149197;
CC P21575; O35180: Sh3gl3; NbExp=2; IntAct=EBI-80070, EBI-1149266;
CC P21575; Q6IN36: Wipf1; NbExp=2; IntAct=EBI-80070, EBI-6986245;
CC P21575; Q6XZF7: DNMBP; Xeno; NbExp=3; IntAct=EBI-80070, EBI-2483419;
CC P21575; Q12965: MYO1E; Xeno; NbExp=2; IntAct=EBI-80070, EBI-4279548;
CC P21575; Q5TCZ1-2; Xeno; NbExp=2; IntAct=EBI-80070, EBI-7014859;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9725914}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9725914}. Note=Microtubule-
CC associated (PubMed:9725914). Isoform-specific localization
CC (PubMed:9725914). {ECO:0000269|PubMed:9725914}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:9725914}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm. Golgi apparatus
CC {ECO:0000269|PubMed:9725914}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=aa;
CC IsoId=P21575-1; Sequence=Displayed;
CC Name=2; Synonyms=ab;
CC IsoId=P21575-2; Sequence=VSP_034037;
CC Name=3; Synonyms=ac;
CC IsoId=P21575-3; Sequence=VSP_034034, VSP_034035;
CC Name=4; Synonyms=ad;
CC IsoId=P21575-4; Sequence=VSP_034036;
CC Name=5; Synonyms=ba;
CC IsoId=P21575-5; Sequence=VSP_034033;
CC Name=6; Synonyms=bb;
CC IsoId=P21575-6; Sequence=VSP_034033, VSP_034037;
CC Name=7; Synonyms=bc;
CC IsoId=P21575-7; Sequence=VSP_034033, VSP_034034, VSP_034035;
CC Name=8; Synonyms=bd;
CC IsoId=P21575-8; Sequence=VSP_034033, VSP_034036;
CC -!- TISSUE SPECIFICITY: Brain-specific (peripheral sensory neurons).
CC {ECO:0000269|PubMed:9725914}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neurons after maturation.
CC -!- PTM: Constitutively phosphorylated by CDK5 in nerve terminals and
CC dephosphorylated by calcineurin when synaptic vesicle endocytosis (SVE)
CC is stimulated by depolarization-dependent calcium influx.
CC {ECO:0000269|PubMed:12855954, ECO:0000269|PubMed:17376771}.
CC -!- MISCELLANEOUS: [Isoform 2]: Localized to numerous punctate spots of
CC various sizes distributed along the plasma membrane and throughout the
CC cytoplasm. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Diffuse cytoplasmic distribution with some
CC localization to the Golgi apparatus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
CC -!- CAUTION: Absence of tyrosine and threonine phosphorylation is
CC demonstrated in PubMed:17376771. However, tyrosine and threonine
CC phosphorylation may still occur in different experimental conditions.
CC {ECO:0000305}.
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DR EMBL; X54531; CAA38397.1; -; mRNA.
DR EMBL; CO398357; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CB583951; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CB708564; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S11508; S11508.
DR RefSeq; NP_542420.1; NM_080689.4. [P21575-2]
DR PDB; 2AKA; X-ray; 1.90 A; B=6-304.
DR PDB; 3ZVR; X-ray; 3.10 A; A=1-752.
DR PDBsum; 2AKA; -.
DR PDBsum; 3ZVR; -.
DR AlphaFoldDB; P21575; -.
DR BMRB; P21575; -.
DR SMR; P21575; -.
DR BioGRID; 250837; 31.
DR CORUM; P21575; -.
DR DIP; DIP-30978N; -.
DR IntAct; P21575; 19.
DR MINT; P21575; -.
DR STRING; 10116.ENSRNOP00000047444; -.
DR BindingDB; P21575; -.
DR ChEMBL; CHEMBL1075191; -.
DR iPTMnet; P21575; -.
DR PhosphoSitePlus; P21575; -.
DR World-2DPAGE; 0004:P21575; -.
DR jPOST; P21575; -.
DR PaxDb; P21575; -.
DR PRIDE; P21575; -.
DR Ensembl; ENSRNOT00000064039; ENSRNOP00000060845; ENSRNOG00000033835. [P21575-2]
DR Ensembl; ENSRNOT00000102787; ENSRNOP00000091634; ENSRNOG00000033835. [P21575-6]
DR GeneID; 140694; -.
DR KEGG; rno:140694; -.
DR UCSC; RGD:71096; rat. [P21575-1]
DR CTD; 1759; -.
DR RGD; 71096; Dnm1.
DR VEuPathDB; HostDB:ENSRNOG00000033835; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155214; -.
DR HOGENOM; CLU_008964_1_0_1; -.
DR InParanoid; P21575; -.
DR OMA; MQMVQTF; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; P21575; -.
DR BRENDA; 3.6.5.5; 5301.
DR Reactome; R-RNO-190873; Gap junction degradation.
DR Reactome; R-RNO-196025; Formation of annular gap junctions.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-437239; Recycling pathway of L1.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; P21575; -.
DR PRO; PR:P21575; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000033835; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; P21575; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030117; C:membrane coat; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0043196; C:varicosity; IDA:RGD.
DR GO; GO:0031749; F:D2 dopamine receptor binding; IPI:RGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IDA:RGD.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0007032; P:endosome organization; ISO:RGD.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IMP:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:RGD.
DR GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; IMP:RGD.
DR GO; GO:0031623; P:receptor internalization; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:RGD.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IMP:RGD.
DR GO; GO:1904645; P:response to amyloid-beta; IEP:RGD.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:RGD.
DR GO; GO:1901998; P:toxin transport; ISO:RGD.
DR CDD; cd08771; DLP_1; 1.
DR DisProt; DP02617; -.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027741; DNM1.
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 InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR PANTHER; PTHR11566:SF32; PTHR11566:SF32; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SMART; SM00233; PH; 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.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Endocytosis; Golgi apparatus; GTP-binding;
KW Hydrolase; Methylation; Microtubule; Motor protein; Nitration;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..864
FT /note="Dynamin-1"
FT /id="PRO_0000206565"
FT DOMAIN 28..294
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 519..625
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 659..750
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 38..45
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 64..66
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 136..139
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 205..208
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 235..238
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 767..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 136..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 205..208
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 80
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 125
FT /note="3'-nitrotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 125
FT /note="Phosphotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 354
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771"
FT MOD_RES 796
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771,
FT ECO:0007744|PubMed:22673903"
FT VAR_SEQ 407..444
FT /note="LAFEATVKKQVQKLKEPSIKCVDMVVSELTSTIRKCSE -> MAFETIVKKQ
FT VKKIREPCLKCVDMVISELISTVRQCTK (in isoform 5, isoform 6,
FT isoform 7 and isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_034033"
FT VAR_SEQ 766..814
FT /note="QSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPP ->
FT AHVQPHAAAPSPRRAPSPARVAGPCSWASACWIRPGGGSPRALQAGGFP (in
FT isoform 3 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_034034"
FT VAR_SEQ 815..864
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_034035"
FT VAR_SEQ 845..864
FT /note="SRSGQASPSRPESPRPPFDL -> RITISDP (in isoform 2 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:2144893"
FT /id="VSP_034037"
FT VAR_SEQ 845..864
FT /note="SRSGQASPSRPESPRPPFDL -> SQPIGSGKSVPS (in isoform 4
FT and isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_034036"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:2AKA"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2AKA"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2AKA"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:2AKA"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 274..303
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 326..344
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 369..375
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 381..394
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 404..418
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 421..442
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 450..483
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 520..531
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 540..555
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 570..575
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 584..590
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 600..609
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 610..622
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 654..688
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 690..699
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 701..707
FT /evidence="ECO:0007829|PDB:3ZVR"
FT TURN 711..715
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 719..742
FT /evidence="ECO:0007829|PDB:3ZVR"
SQ SEQUENCE 864 AA; 97295 MW; 02EC9B533CC2EC83 CRC64;
MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLV LQLVNSTTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI
NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD
LANSDALKIA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL
QSQLLSIEKE VDEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA
RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDLAFE ATVKKQVQKL
KEPSIKCVDM VVSELTSTIR KCSEKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID
IELAYMNTNH EDFIGFANAQ QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE
YWFVLTAENL SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY
RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS MDPQLERQVE
TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE LLANLYSCGD QNTLMEESAE
QAQRRDEMLR MYHALKEALS IIGDINTTTV STPMPPPVDD SWLQVQSVPA GRRSPTSSPT
PQRRAPAVPP ARPGSRGPAP GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP
PGVPSRSGQA SPSRPESPRP PFDL
