DYN2_RAT
ID DYN2_RAT Reviewed; 870 AA.
AC P39052;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Dynamin-2;
DE EC=3.6.5.5;
GN Name=Dnm2; Synonyms=Dyn2;
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] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Brain;
RX PubMed=8308025; DOI=10.1016/s0021-9258(17)41812-6;
RA Sontag J.-M., Fykse E.M., Ushkaryov Y., Liu J.-P., Robinson P.J.,
RA Suedhof T.C.;
RT "Differential expression and regulation of multiple dynamins.";
RL J. Biol. Chem. 269:4547-4554(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=Sprague-Dawley;
RX PubMed=8290576; DOI=10.1073/pnas.91.2.644;
RA Cook T.A., Urrutia R., McNiven M.A.;
RT "Identification of dynamin 2, an isoform ubiquitously expressed in rat
RT tissues.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:644-648(1994).
RN [3]
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 [4]
RP INTERACTION WITH SH3BP4.
RX PubMed=16325581; DOI=10.1016/j.cell.2005.10.021;
RA Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P.,
RA Tacchetti C., Di Fiore P.P.;
RT "TTP specifically regulates the internalization of the transferrin
RT receptor.";
RL Cell 123:875-888(2005).
RN [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-231 AND TYR-597, AND
RP MUTAGENESIS OF TYR-231 AND TYR-597.
RX PubMed=19995918; DOI=10.1128/mcb.00330-09;
RA Cao H., Chen J., Krueger E.W., McNiven M.A.;
RT "SRC-mediated phosphorylation of dynamin and cortactin regulates the
RT 'constitutive' endocytosis of transferrin.";
RL Mol. Cell. Biol. 30:781-792(2010).
RN [7]
RP PHOSPHORYLATION AT SER-764 BY CDK1, MUTAGENESIS OF SER-764, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Lung;
RX PubMed=21195118; DOI=10.1016/j.bbamcr.2010.12.018;
RA Chircop M., Sarcevic B., Larsen M.R., Malladi C.S., Chau N., Zavortink M.,
RA Smith C.M., Quan A., Anggono V., Hains P.G., Graham M.E., Robinson P.J.;
RT "Phosphorylation of dynamin II at serine-764 is associated with
RT cytokinesis.";
RL Biochim. Biophys. Acta 1813:1689-1699(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CTTN AND ACTN1.
RX PubMed=21210813; DOI=10.1111/j.1471-4159.2011.07169.x;
RA Kurklinsky S., Chen J., McNiven M.A.;
RT "Growth cone morphology and spreading are regulated by a dynamin-cortactin
RT complex at point contacts in hippocampal neurons.";
RL J. Neurochem. 117:48-60(2011).
CC -!- FUNCTION: Microtubule-associated force-producing protein involved in
CC producing microtubule bundles and able to bind and hydrolyze GTP. Plays
CC a role in the regulation of neuron morphology, axon growth and
CC formation of neuronal growth cones (PubMed:21210813). Plays an
CC important role in vesicular trafficking processes, in particular
CC endocytosis (PubMed:19995918). Involved in cytokinesis
CC (PubMed:21195118). Regulates maturation of apoptotic cell corpse-
CC containing phagosomes by recruiting PIK3C3 to the phagosome membrane
CC (By similarity). {ECO:0000250|UniProtKB:P39054,
CC ECO:0000269|PubMed:19995918, ECO:0000269|PubMed:21195118,
CC ECO:0000269|PubMed:21210813}.
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 MYOF (By similarity). Interacts with CTTN and
CC ACTN1 (PubMed:21210813). Interacts with SHANK1, SHANK2 and NOSTRIN (By
CC similarity). Interacts with SH3BP4 (PubMed:16325581). Interacts with
CC SNX9 (By similarity). Interacts with SNX18 (By similarity). Interacts
CC with SNX33 (via SH3 domain) (By similarity). Interacts with MYO1E (via
CC SH3 domain) (PubMed:17257598). Interacts with PSTPIP1 (By similarity).
CC Interacts with CTNND2 (By similarity). May interact with PIK3C3 (By
CC similarity). May be a component of a complex composed of RAB5A (in GDP-
CC bound form), DYN2 and PIK3C3 (By similarity). Interacts with BIN1 (By
CC similarity). {ECO:0000250|UniProtKB:P39054,
CC ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:16325581,
CC ECO:0000269|PubMed:17257598, ECO:0000269|PubMed:21210813}.
CC -!- INTERACTION:
CC P39052; O08838: Amph; NbExp=2; IntAct=EBI-349613, EBI-80080;
CC P39052; Q9P0V3: SH3BP4; Xeno; NbExp=5; IntAct=EBI-349613, EBI-1049513;
CC P39052; Q96B97: SH3KBP1; Xeno; NbExp=4; IntAct=EBI-349613, EBI-346595;
CC P39052; Q9BX66: SORBS1; Xeno; NbExp=5; IntAct=EBI-349613, EBI-433642;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21210813}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21210813}. Cell junction
CC {ECO:0000269|PubMed:21210813}. Postsynaptic density
CC {ECO:0000250|UniProtKB:P50570}. Synapse {ECO:0000250|UniProtKB:P50570}.
CC Midbody {ECO:0000269|PubMed:21195118, ECO:0000269|PubMed:9725914}.
CC Membrane, clathrin-coated pit {ECO:0000269|PubMed:19995918}. Cell
CC projection, phagocytic cup {ECO:0000250|UniProtKB:P39054}. Cytoplasmic
CC vesicle, phagosome membrane {ECO:0000250|UniProtKB:P39054}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P39054}. Note=Microtubule-
CC associated. Also found in the postsynaptic density of neuronal cells
CC (By similarity). Colocalizes with CTTN at the basis of filopodia in
CC hippocampus neuron growth zones (PubMed:21210813). Co-localizes with
CC PIK3C3 and RAB5A to the nascent phagosome (By similarity).
CC {ECO:0000250|UniProtKB:P39054, ECO:0000250|UniProtKB:P50570}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle, clathrin-coated
CC vesicle. Membrane, clathrin-coated pit.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=ba, IIBA;
CC IsoId=P39052-1; Sequence=Displayed;
CC Name=2; Synonyms=aa;
CC IsoId=P39052-2; Sequence=VSP_001327;
CC Name=3; Synonyms=bb, IIC;
CC IsoId=P39052-3; Sequence=VSP_001328;
CC Name=4; Synonyms=ab;
CC IsoId=P39052-4; Sequence=VSP_001327, VSP_001328;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Brain expression is
CC restricted to glial cells and fibroblasts. Highest levels in the
CC testis. {ECO:0000269|PubMed:9725914}.
CC -!- PTM: Phosphorylation at Ser-764 by CDK1 is greatly increased upon
CC mitotic entry. It regulates cytokinesis downstream of calcineurin, and
CC does not affect clathrin-mediated endocytosis. Dephosphorylated by
CC calcineurin/PP2. Phosphorylated on tyrosine residues after activation
CC of SRC (PubMed:19995918). {ECO:0000269|PubMed:19995918,
CC ECO:0000269|PubMed:21195118}.
CC -!- MISCELLANEOUS: [Isoform 2]: Sequestered to clathrin-coated pits and
CC vesicles at the plasma membrane and the Golgi apparatus. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Localized to numerous punctate spots on the
CC plasma membrane. {ECO:0000305}.
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; L25605; AAA19736.1; -; mRNA.
DR EMBL; L24562; AAA16746.1; -; mRNA.
DR PIR; A36878; A36878.
DR PIR; A53165; A53165.
DR PIR; B53165; B53165.
DR RefSeq; NP_037331.1; NM_013199.1. [P39052-1]
DR RefSeq; XP_006242670.1; XM_006242608.3. [P39052-2]
DR RefSeq; XP_006242674.1; XM_006242612.3. [P39052-4]
DR RefSeq; XP_006242675.1; XM_006242613.3. [P39052-3]
DR AlphaFoldDB; P39052; -.
DR BMRB; P39052; -.
DR SMR; P39052; -.
DR BioGRID; 247779; 6.
DR CORUM; P39052; -.
DR DIP; DIP-33275N; -.
DR IntAct; P39052; 20.
DR MINT; P39052; -.
DR STRING; 10116.ENSRNOP00000060296; -.
DR BindingDB; P39052; -.
DR ChEMBL; CHEMBL2311233; -.
DR iPTMnet; P39052; -.
DR PhosphoSitePlus; P39052; -.
DR jPOST; P39052; -.
DR PaxDb; P39052; -.
DR PRIDE; P39052; -.
DR GeneID; 25751; -.
DR KEGG; rno:25751; -.
DR UCSC; RGD:2513; rat. [P39052-1]
DR CTD; 1785; -.
DR RGD; 2513; Dnm2.
DR VEuPathDB; HostDB:ENSRNOG00000007649; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; P39052; -.
DR OMA; XVIRRGW; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; P39052; -.
DR TreeFam; TF300362; -.
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-203641; NOSTRIN mediated eNOS trafficking.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-437239; Recycling pathway of L1.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P39052; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000007649; Expressed in jejunum and 19 other tissues.
DR ExpressionAtlas; P39052; baseline and differential.
DR Genevisible; P39052; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:RGD.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:RGD.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0001891; C:phagocytic cup; IDA:RGD.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0032587; C:ruffle membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR GO; GO:0031749; F:D2 dopamine receptor binding; IPI:RGD.
DR GO; GO:0005525; F:GTP binding; TAS:RGD.
DR GO; GO:0003924; F:GTPase activity; IDA:RGD.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IDA:RGD.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IPI:RGD.
DR GO; GO:0050699; F:WW domain binding; IPI:RGD.
DR GO; GO:0035904; P:aorta development; ISO:RGD.
DR GO; GO:0071245; P:cellular response to carbon monoxide; IEP:RGD.
DR GO; GO:1903351; P:cellular response to dopamine; IDA:RGD.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEP:RGD.
DR GO; GO:0071481; P:cellular response to X-ray; IEP:RGD.
DR GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IMP:RGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:RGD.
DR GO; GO:0044351; P:macropinocytosis; IMP:RGD.
DR GO; GO:1903526; P:negative regulation of membrane tubulation; ISO:RGD.
DR GO; GO:1902856; P:negative regulation of non-motile cilium assembly; IMP:RGD.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:RGD.
DR GO; GO:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; IMP:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:RGD.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:RGD.
DR GO; GO:0031623; P:receptor internalization; ISO:RGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:RGD.
DR GO; GO:0030516; P:regulation of axon extension; IMP:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; IMP:RGD.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IMP:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0009416; P:response to light stimulus; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:RGD.
DR GO; GO:0033572; P:transferrin transport; ISO:RGD.
DR GO; GO:0003281; P:ventricular septum development; ISO:RGD.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027188; DNM2.
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:SF23; PTHR11566:SF23; 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 Acetylation; Alternative splicing; Cell junction; Cell membrane;
KW Cell projection; Coated pit; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Endocytosis; GTP-binding; Hydrolase; Membrane; Microtubule; Motor protein;
KW Nucleotide-binding; Phagocytosis; Phosphoprotein; Reference proteome;
KW Synapse.
FT CHAIN 1..870
FT /note="Dynamin-2"
FT /id="PRO_0000206572"
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 653..744
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 741..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..851
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 205..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 236..239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT MOD_RES 231
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:19995918"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P39054"
FT MOD_RES 597
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:19995918"
FT MOD_RES 598
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50570"
FT MOD_RES 755
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P50570"
FT MOD_RES 764
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:21195118"
FT VAR_SEQ 407..444
FT /note="LAFEAIVKKQVVKLKEPCLKCVDLVIQELISTVRQCTS -> MAFEAIVKKQ
FT LVKLKEPSLKCVDLVVSELATVIKKCAE (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8308025"
FT /id="VSP_001327"
FT VAR_SEQ 516..519
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8290576,
FT ECO:0000303|PubMed:8308025"
FT /id="VSP_001328"
FT MUTAGEN 231
FT /note="Y->F: Strongly reduced phosphorylation. Decreases
FT receptor-mediated endocytosis."
FT /evidence="ECO:0000269|PubMed:19995918"
FT MUTAGEN 597
FT /note="Y->F: Strongly reduced phosphorylation. Decreases
FT receptor-mediated endocytosis."
FT /evidence="ECO:0000269|PubMed:19995918"
FT MUTAGEN 764
FT /note="S->A: Reduces proline-rich domain phosphorylation by
FT 80%."
FT /evidence="ECO:0000269|PubMed:21195118"
FT MUTAGEN 764
FT /note="S->E: Abolishes midbody localization and shows
FT increased multinucleation."
FT /evidence="ECO:0000269|PubMed:21195118"
FT CONFLICT 298
FT /note="S -> T (in Ref. 2; AAA16746)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="S -> T (in Ref. 2; AAA16746)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="N -> K (in Ref. 2; AAA16746)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="G -> E (in Ref. 2; AAA16746)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="Missing (in Ref. 2; AAA16746)"
FT /evidence="ECO:0000305"
FT CONFLICT 786..791
FT /note="GPTPGP -> PHTGA (in Ref. 2; AAA16746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 870 AA; 98230 MW; 3802DBAFA3ABBE98 CRC64;
MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLI LQLIFSKTEY AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI
NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
DIEGRKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPTLRSKL
QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA
RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL
KEPCLKCVDL VIQELISTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID
IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQGEILV IRRGWLTINN ISLMKGGSKE
YWFVLTAESL SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL
RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE RQVETIRNLV
DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY SSADQSSLME ESAEQAQRRD
DMLRMYHALK EALNIIGDIS TSTVSTPVPP PVDDTWLQNT SSHSPTPQRR PVSSVHPPGR
PPAVRGPTPG PPLIPMPVGA TSSFSAPPIP SRPGPQNVFA NNDPFSAPPQ IPSRPARIPP
GIPPGVPSRR APAAPSRPTI IRPAEPSLLD
