ID Q7TN74_MOUSE Unreviewed; 1095 AA.
AC Q7TN74;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 157.
DE SubName: Full=Neurabin I {ECO:0000313|EMBL:AAQ77229.1};
DE SubName: Full=Neural tissue-specific F-actin binding protein {ECO:0000313|EMBL:BAC77245.1};
DE SubName: Full=Protein phosphatase 1, regulatory subunit 9A {ECO:0000313|Ensembl:ENSMUSP00000046906.3};
GN Name=Ppp1r9a {ECO:0000313|Ensembl:ENSMUSP00000046906.3,
GN ECO:0000313|MGI:MGI:2442401};
GN Synonyms=Neurabin {ECO:0000313|EMBL:BAC77245.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAC77245.1};
RN [1] {ECO:0000313|EMBL:BAC77245.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL6 {ECO:0000313|EMBL:BAC77245.1};
RX PubMed=12840045; DOI=10.1101/gr.906803;
RA Ono R., Shiura H., Aburatani H., Kohda T., Kaneko-Ishino T., Ishino F.;
RT "Identification of a large novel imprinted gene cluster on mouse proximal
RT chromosome 6.";
RL Genome Res. 13:1696-1705(2003).
RN [2] {ECO:0000313|EMBL:AAQ77229.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CD-1 {ECO:0000313|EMBL:AAQ77229.1};
RA Nakabayashi K., Makino S., Minagawa S., Smith A.C., Bamforth J.S.,
RA Stanier P., Preece M., Oshimura M., Yoshikawa Y., Hui C.C., Moore G.E.,
RA Scherer S.W.;
RT "Genomic imprinting of PPP1R9A encoding neurabin I in skeletal muscle
RT tissues and extra-embryonic tissues.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007829|PubMed:16452087}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000046906.3, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000046906.3,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6] {ECO:0000313|Ensembl:ENSMUSP00000046906.3}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000046906.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; AY308065; AAQ77229.1; -; mRNA.
DR EMBL; AB091828; BAC77245.1; -; mRNA.
DR RefSeq; NP_853626.1; NM_181595.3.
DR RefSeq; XP_006505142.1; XM_006505079.3.
DR IntAct; Q7TN74; 4.
DR STRING; 10090.ENSMUSP00000046906; -.
DR PaxDb; 10090-ENSMUSP00000046906; -.
DR ProteomicsDB; 338778; -.
DR Antibodypedia; 4361; 169 antibodies from 27 providers.
DR DNASU; 243725; -.
DR Ensembl; ENSMUST00000035813.9; ENSMUSP00000046906.3; ENSMUSG00000032827.16.
DR GeneID; 243725; -.
DR UCSC; uc009avx.1; mouse.
DR AGR; MGI:2442401; -.
DR CTD; 55607; -.
DR MGI; MGI:2442401; Ppp1r9a.
DR VEuPathDB; HostDB:ENSMUSG00000032827; -.
DR eggNOG; KOG1945; Eukaryota.
DR GeneTree; ENSGT00940000155538; -.
DR OrthoDB; 2911512at2759; -.
DR TreeFam; TF105540; -.
DR BioGRID-ORCS; 243725; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Ppp1r9a; mouse.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000032827; Expressed in caudate-putamen and 226 other cell types or tissues.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR GO; GO:0044326; C:dendritic spine neck; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:1990761; C:growth cone lamellipodium; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IPI:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:MGI.
DR GO; GO:0097237; P:cellular response to toxic substance; ISO:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; ISO:MGI.
DR GO; GO:1904049; P:negative regulation of spontaneous neurotransmitter secretion; ISO:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISO:MGI.
DR GO; GO:0051963; P:regulation of synapse assembly; ISO:MGI.
DR GO; GO:0051823; P:regulation of synapse structural plasticity; ISO:MGI.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd09512; SAM_Neurabin-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR040645; Neurabin-1/2_PDZ.
DR InterPro; IPR043446; Neurabin-like.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR16154; NEURABIN; 1.
DR PANTHER; PTHR16154:SF22; NEURABIN-1; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17817; PDZ_5; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|MaxQB:Q7TN74,
KW ECO:0007829|PeptideAtlas:Q7TN74};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 505..593
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 989..1052
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 681..824
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..646
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 122955 MW; 3F207AADEC2E5010 CRC64;
MLKAESSGER TTLRSASPHR NAYRTEFQAL KSTFDKPKSD GEQKTKEGEG SQQSRGRKYG
SNVNRIKNLF MQMGMEPSEN AAIIAKTRGK GRPSSPQRRM KPKEFVEKTD GSVVKLESSV
SERISRFDTM HDGPSYAKFT ETRKMFERSV HESGQNHRYS PKKEKGGGTE PQDEWGGSKS
NRGSSDSLDS LSPRTEAVSP TVSQLSAVFE NSEPPGALTS GKAESADYSV TGHYPLNLPS
VTVTNLDTFG RLKDSNSKPP SNKQDTDTED AQKSDAVPVP EVAQKGTSLA SLPSEESQLS
TEAEDVTTAQ PEALDSTDKD SPEEPSAENQ AMPKSHILSP RNEPLEDAEA NVVGSERAQH
QKKDLTGGDL TSPDASASSC GREVPEDSNS FESSHVYMHS DYNVYRVRSR YNSDWGETGT
EQDEEEDSDE NNYYQPDMEY SEIVGLPEEE EIPANRKIKF SCAPIKVFNT YSNEDYDRRN
DDVDPVAASA EYELEKRVEK LELFPVELEK DEDGLGISII GMGVGADAGL EKLGIFVKTV
TDGGAAQRDG RIQVNDQIVE VDGISLVGVT QNFAATVLRN TKGNVRFVIG REKPGQVSEV
AQLISQTLEQ ERRQRELLER HYAQYDADDD ETGEYATDEE EDEGGPILPS GDVAIEVFEL
PENEDMFSPS DLDTSKLSHK FKELQIKHAV TEAEIQKLKT KLQAAENEKV RWELEKNQLQ
QNIEENKERM LKLESYWIEA QTLCHTVNEH LKETQSQYQA LEKKYNKAKK LIKDFQQKEL
DFIKRQEVER KKREEVEKAH LLEVQGLQVR IRDLEAEVFR LLKQNGTQVN NNNNIFERRP
SPGEVSKGDT MENVEVKQTS CQDGLSQDLN EAVPETERLD SKALKTRAQL SVKNRRQRPT
RTRLYDSVSS TDGEDSLERK NFTFNDDFSP SSTSSADLSG LGAEPKTPGL SQSLALSSDE
SLDMIDDEIL DDGQSPKHTQ SQNRAVHEWS VQQVSHWLMS LSLDQYVPEF SAQSISGEQL
LQLDGNKLKA LGMTSSQDRA LVKKKLKEMK MSLEKARKAQ EKMEKQREKL RRKEQEQMQR
KSKKSEKMTS TADQP
//
