NEB1_RAT
ID NEB1_RAT Reviewed; 1095 AA.
AC O35867;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Neurabin-1;
DE AltName: Full=Neurabin-I;
DE AltName: Full=Neural tissue-specific F-actin-binding protein I;
DE AltName: Full=PP1bp175;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 9A;
DE AltName: Full=p180;
GN Name=Ppp1r9a;
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 PROTEIN SEQUENCE OF 4-21; 180-211; 286-311; 467-482; 501-532; 710-715 AND
RP 779-790.
RC TISSUE=Brain;
RX PubMed=9362513; DOI=10.1083/jcb.139.4.951;
RA Nakanishi H., Obaishi H., Satoh A., Wada M., Mandai K., Satoh K.,
RA Nishioka H., Matsuura Y., Mizoguchi A., Takai Y.;
RT "Neurabin: a novel neural tissue-specific actin filament-binding protein
RT involved in neurite formation.";
RL J. Cell Biol. 139:951-961(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=9653190; DOI=10.1073/pnas.95.14.8351;
RA Burnett P.E., Blackshaw S., Lai M.M., Qureshi I.A., Burnett A.F.,
RA Sabatini D.M., Snyder S.H.;
RT "Neurabin is a synaptic protein linking p70 S6 kinase and the neuronal
RT cytoskeleton.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8351-8356(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=10585469; DOI=10.1074/jbc.274.50.35845;
RA MacMillan L.B., Bass M.A., Cheng N., Howard E.F., Tamura M., Strack S.,
RA Wadzinski B.E., Colbran R.J.;
RT "Brain actin-associated protein phosphatase 1 holoenzymes containing
RT spinophilin, neurabin, and selected catalytic subunit isoforms.";
RL J. Biol. Chem. 274:35845-35854(1999).
RN [4]
RP INTERACTION WITH TGN38.
RX PubMed=10514494; DOI=10.1074/jbc.274.42.30080;
RA Stephens D.J., Banting G.;
RT "Direct interaction of the trans-Golgi network membrane protein, TGN38,
RT with the F-actin binding protein, neurabin.";
RL J. Biol. Chem. 274:30080-30086(1999).
RN [5]
RP INTERACTION WITH PP1, PHOSPHORYLATION AT SER-461, AND MUTAGENESIS.
RC STRAIN=Sprague-Dawley;
RX PubMed=10504266; DOI=10.1021/bi991227d;
RA McAvoy T., Allen P.B., Obaishi H., Nakanishi H., Takai Y., Greengard P.,
RA Nairn A.C., Hemmings H.C. Jr.;
RT "Regulation of neurabin I interaction with protein phosphatase 1 by
RT phosphorylation.";
RL Biochemistry 38:12943-12949(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; THR-312; SER-372;
RP SER-916; SER-929; SER-957; SER-958; SER-961 AND SER-975, AND IDENTIFICATION
RP 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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 426-592 IN COMPLEX WITH HUMAN
RP PP1CA.
RX PubMed=20305656; DOI=10.1038/nsmb.1786;
RA Ragusa M.J., Dancheck B., Critton D.A., Nairn A.C., Page R., Peti W.;
RT "Spinophilin directs protein phosphatase 1 specificity by blocking
RT substrate binding sites.";
RL Nat. Struct. Mol. Biol. 17:459-464(2010).
CC -!- FUNCTION: Binds to actin filaments (F-actin) and shows cross-linking
CC activity. Binds along the sides of the F-actin. May be involved in
CC neurite formation. Inhibits protein phosphatase 1-alpha activity. May
CC play an important role in linking the actin cytoskeleton to the plasma
CC membrane at the synaptic junction.
CC -!- SUBUNIT: Possibly exists as a homodimer, homotrimer or a homotetramer.
CC Interacts with F-actin, protein phosphatase 1 (PP1), neurabin-2, TGN38
CC and p70-S6K. {ECO:0000269|PubMed:10504266, ECO:0000269|PubMed:10514494,
CC ECO:0000269|PubMed:20305656}.
CC -!- INTERACTION:
CC O35867; P62142: Ppp1cb; NbExp=2; IntAct=EBI-7092421, EBI-352326;
CC O35867; P63088: Ppp1cc; NbExp=2; IntAct=EBI-7092421, EBI-80049;
CC O35867; P67999: Rps6kb1; NbExp=4; IntAct=EBI-7092421, EBI-2639458;
CC O35867; P62136: PPP1CA; Xeno; NbExp=3; IntAct=EBI-7092421, EBI-357253;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Synapse, synaptosome.
CC -!- TISSUE SPECIFICITY: Brain, and widely expressed in neural tissue.
CC Highly concentrated in synapses of developed neurons. In developing
CC neurons, concentrated in the lamellipodia of the growth cone.
CC -!- DOMAIN: Interacts with p70-S6K via its PDZ domain.
CC -!- DOMAIN: The PP1 binding region is natively unstructured, upon PP1
CC binding, it acquires structure, blocks a substrate-binding site, and
CC restricts PP1 phosphatase specificity to a subset of substrates.
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DR EMBL; U72994; AAC53454.1; -; mRNA.
DR PIR; T43275; T43275.
DR RefSeq; NP_445925.1; NM_053473.2.
DR PDB; 2FN5; NMR; -; A=502-592.
DR PDB; 2GLE; NMR; -; A=986-1056.
DR PDB; 3HVQ; X-ray; 2.20 A; C/D=426-592.
DR PDBsum; 2FN5; -.
DR PDBsum; 2GLE; -.
DR PDBsum; 3HVQ; -.
DR AlphaFoldDB; O35867; -.
DR BMRB; O35867; -.
DR SMR; O35867; -.
DR BioGRID; 250039; 6.
DR DIP; DIP-40850N; -.
DR IntAct; O35867; 6.
DR MINT; O35867; -.
DR STRING; 10116.ENSRNOP00000011756; -.
DR iPTMnet; O35867; -.
DR PhosphoSitePlus; O35867; -.
DR PaxDb; O35867; -.
DR PRIDE; O35867; -.
DR Ensembl; ENSRNOT00000011756; ENSRNOP00000011756; ENSRNOG00000008869.
DR GeneID; 84685; -.
DR KEGG; rno:84685; -.
DR UCSC; RGD:632280; rat.
DR CTD; 55607; -.
DR RGD; 632280; Ppp1r9a.
DR eggNOG; KOG1945; Eukaryota.
DR GeneTree; ENSGT00940000155538; -.
DR HOGENOM; CLU_007401_0_0_1; -.
DR InParanoid; O35867; -.
DR OMA; XLNEAVP; -.
DR OrthoDB; 128743at2759; -.
DR PhylomeDB; O35867; -.
DR EvolutionaryTrace; O35867; -.
DR PRO; PR:O35867; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000008869; Expressed in frontal cortex and 15 other tissues.
DR Genevisible; O35867; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0044326; C:dendritic spine neck; IDA:RGD.
DR GO; GO:0030175; C:filopodium; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:1990761; C:growth cone lamellipodium; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:WormBase.
DR GO; GO:0051020; F:GTPase binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:0097237; P:cellular response to toxic substance; IDA:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IMP:RGD.
DR GO; GO:1904049; P:negative regulation of spontaneous neurotransmitter secretion; IMP:RGD.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:RGD.
DR GO; GO:0048666; P:neuron development; IEP:RGD.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:RGD.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:RGD.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:RGD.
DR GO; GO:0051963; P:regulation of synapse assembly; IMP:RGD.
DR GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:RGD.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR IDEAL; IID50060; -.
DR InterPro; IPR029994; Neurabin-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; PTHR16154; 1.
DR PANTHER; PTHR16154:SF22; PTHR16154:SF22; 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; SSF47769; SSF47769; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Neurogenesis; Phosphoprotein; Reference proteome; Synapse; Synaptosome.
FT CHAIN 1..1095
FT /note="Neurabin-1"
FT /id="PRO_0000071508"
FT DOMAIN 505..593
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 989..1052
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..144
FT /note="Actin-binding"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..503
FT /note="Interaction with protein phosphatase 1"
FT REGION 598..1091
FT /note="Interaction with TGN38"
FT /evidence="ECO:0000269|PubMed:10514494"
FT REGION 874..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 598..628
FT /evidence="ECO:0000255"
FT COILED 674..825
FT /evidence="ECO:0000255"
FT COILED 1036..1091
FT /evidence="ECO:0000255"
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..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..264
FT /note="Polar 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..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULJ8"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 461
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:10504266"
FT MOD_RES 841
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULJ8"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 957
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 958
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 461
FT /note="S->E: 35-fold decrease in inhibition of PP1-alpha."
FT /evidence="ECO:0000269|PubMed:10504266"
FT MUTAGEN 516..517
FT /note="GI->AA: Abolishes P70-S6K binding."
FT /evidence="ECO:0000269|PubMed:10504266"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:3HVQ"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:3HVQ"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:3HVQ"
FT HELIX 485..498
FT /evidence="ECO:0007829|PDB:3HVQ"
FT STRAND 501..509
FT /evidence="ECO:0007829|PDB:3HVQ"
FT STRAND 516..522
FT /evidence="ECO:0007829|PDB:3HVQ"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:2FN5"
FT STRAND 530..540
FT /evidence="ECO:0007829|PDB:3HVQ"
FT HELIX 545..549
FT /evidence="ECO:0007829|PDB:3HVQ"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:2FN5"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:3HVQ"
FT HELIX 571..580
FT /evidence="ECO:0007829|PDB:3HVQ"
FT STRAND 583..591
FT /evidence="ECO:0007829|PDB:3HVQ"
FT HELIX 986..988
FT /evidence="ECO:0007829|PDB:2GLE"
FT HELIX 992..994
FT /evidence="ECO:0007829|PDB:2GLE"
FT HELIX 995..1000
FT /evidence="ECO:0007829|PDB:2GLE"
FT TURN 1001..1003
FT /evidence="ECO:0007829|PDB:2GLE"
FT HELIX 1004..1010
FT /evidence="ECO:0007829|PDB:2GLE"
FT TURN 1011..1014
FT /evidence="ECO:0007829|PDB:2GLE"
FT HELIX 1017..1021
FT /evidence="ECO:0007829|PDB:2GLE"
FT HELIX 1025..1029
FT /evidence="ECO:0007829|PDB:2GLE"
FT TURN 1030..1032
FT /evidence="ECO:0007829|PDB:2GLE"
FT HELIX 1036..1047
FT /evidence="ECO:0007829|PDB:2GLE"
FT HELIX 1049..1055
FT /evidence="ECO:0007829|PDB:2GLE"
SQ SEQUENCE 1095 AA; 122735 MW; 58E3650320B3BD61 CRC64;
MLKAESSGER TTLRSASPHR NAYRTEFQAL KSTFDKPKPD GEQKTKEGEG SQQSRGRKYG
SNVNRIKNLF MQMGMEPNEN AAIIAKTRGK GRPSSPQKRM KPKEFVEKTD GSVVKLESSV
SERISRFDTM HDGPSYAKFT ETRKMFERSG HESGQNNRHS PKKEKAGEAE PQDEWGGSKS
NRGSSDSLDS LSPRTEAVSP TVSQLSAVFE NSESPGAITP GKAENSNYSV TGHYPLNLPS
VTVTNLDTFG RLKDSNSRPS SNKQATDTEE PEKSEAVPVP EVAQKGTSLA SLPSEERQLS
TEAEDVTAQP DTPDSTDKDS PGEPSAESQA MPKSNTLSRP KEPLEDAEAN VVGSEAEQPQ
RRDLTGGGDL TSPDASASSC GKEVPEDSNS FEGSHVYMHS DYNVYRVRSR YNSDWGETGT
EQDEGDDSDE NNYYQPDMEY SEIVGLPQEE EIPANRKIKF SCAPIKVFNT YSNEDYDRRN
DDVDPVAASA EYELEKRVEK LELFPVELEK DEDGLGISII GMGVGADAGL EKLGIFVKTV
TEGGAAQRDG RIQVNDQIVE VDGISLVGVT QNFAATVLRN TKGNVRFVIG REKPGQVSEV
AQLISQTLEQ ERRQRELLER HYAQYDADDD ETGEYATDEE EDEVGPILPG GDMAIEVFEL
PENEDMFSPS DLDTSKLSHK FKELQIKHAV TEAEIQKLKT KLQAAENEKV RWELEKNQLQ
QNIEENKERM VKLESYWIEA QTLCHTVNEH LKETQSQYQA LEKKYNKAKK LIKDFQQKEL
DFIRRQEVER KKLEEVEKAH LVEVQGLQVR IRDLEAEVFR LLKQNGTQVN NNNNIFERRP
SPGEVSKGDT MENVEVKQTS CQDGLSQDLN EAVPETERLD SKALKTRAQL SVKNRRQRPT
RTRLYDSVSS TDGEDSLERK NFTFNDDFSP SSTSSADLSG LGAEPKTPGL SQSLALSSDE
SLDMIDDEIL DDGQSPKHTQ SQSRAVHEWS VQQVSHWLVG LSLDQYVSEF SAQNISGEQL
LQLDGNKLKA LGMTSSQDRA LVKKKLKEMK MSLEKARKAQ EKMEKQREKL RRKEQEQMQR
KSKKSEKMTS TTEQP
