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Neurabin-1 (Neurabin-I) (Neural tissue-specific F-actin-binding protein I) (PP1bp175) (Protein phosphatase 1 regulatory subunit 9A) (p180)

 NEB1_RAT                Reviewed;        1095 AA.
O35867;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
23-MAY-2018, entry version 149.
RecName: Full=Neurabin-1;
AltName: Full=Neurabin-I;
AltName: Full=Neural tissue-specific F-actin-binding protein I;
AltName: Full=PP1bp175;
AltName: Full=Protein phosphatase 1 regulatory subunit 9A;
AltName: Full=p180;
Name=Ppp1r9a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
PROTEIN SEQUENCE OF 4-21; 180-211; 286-311; 467-482; 501-532; 710-715
AND 779-790.
TISSUE=Brain;
PubMed=9362513; DOI=10.1083/jcb.139.4.951;
Nakanishi H., Obaishi H., Satoh A., Wada M., Mandai K., Satoh K.,
Nishioka H., Matsuura Y., Mizoguchi A., Takai Y.;
"Neurabin: a novel neural tissue-specific actin filament-binding
protein involved in neurite formation.";
J. Cell Biol. 139:951-961(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Brain;
PubMed=9653190; DOI=10.1073/pnas.95.14.8351;
Burnett P.E., Blackshaw S., Lai M.M., Qureshi I.A., Burnett A.F.,
Sabatini D.M., Snyder S.H.;
"Neurabin is a synaptic protein linking p70 S6 kinase and the neuronal
cytoskeleton.";
Proc. Natl. Acad. Sci. U.S.A. 95:8351-8356(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Brain;
PubMed=10585469; DOI=10.1074/jbc.274.50.35845;
MacMillan L.B., Bass M.A., Cheng N., Howard E.F., Tamura M.,
Strack S., Wadzinski B.E., Colbran R.J.;
"Brain actin-associated protein phosphatase 1 holoenzymes containing
spinophilin, neurabin, and selected catalytic subunit isoforms.";
J. Biol. Chem. 274:35845-35854(1999).
[4]
INTERACTION WITH TGN38.
PubMed=10514494; DOI=10.1074/jbc.274.42.30080;
Stephens D.J., Banting G.;
"Direct interaction of the trans-Golgi network membrane protein,
TGN38, with the F-actin binding protein, neurabin.";
J. Biol. Chem. 274:30080-30086(1999).
[5]
INTERACTION WITH PP1, PHOSPHORYLATION AT SER-461, AND MUTAGENESIS.
STRAIN=Sprague-Dawley;
PubMed=10504266; DOI=10.1021/bi991227d;
McAvoy T., Allen P.B., Obaishi H., Nakanishi H., Takai Y.,
Greengard P., Nairn A.C., Hemmings H.C. Jr.;
"Regulation of neurabin I interaction with protein phosphatase 1 by
phosphorylation.";
Biochemistry 38:12943-12949(1999).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; THR-312; SER-372;
SER-916; SER-929; SER-957; SER-958; SER-961 AND SER-975, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[7]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 426-592 IN COMPLEX WITH HUMAN
PP1CA.
PubMed=20305656; DOI=10.1038/nsmb.1786;
Ragusa M.J., Dancheck B., Critton D.A., Nairn A.C., Page R., Peti W.;
"Spinophilin directs protein phosphatase 1 specificity by blocking
substrate binding sites.";
Nat. Struct. Mol. Biol. 17:459-464(2010).
-!- FUNCTION: Binds to actin filaments (F-actin) and shows cross-
linking activity. Binds along the sides of the F-actin. May be
involved in neurite formation. Inhibits protein phosphatase 1-
alpha activity. May play an important role in linking the actin
cytoskeleton to the plasma membrane at the synaptic junction.
-!- SUBUNIT: Possibly exists as a homodimer, homotrimer or a
homotetramer. Interacts with F-actin, protein phosphatase 1 (PP1),
neurabin-2, TGN38 and p70-S6K. {ECO:0000269|PubMed:10504266,
ECO:0000269|PubMed:10514494, ECO:0000269|PubMed:20305656}.
-!- INTERACTION:
P62136:PPP1CA (xeno); NbExp=3; IntAct=EBI-7092421, EBI-357253;
P62142:Ppp1cb; NbExp=2; IntAct=EBI-7092421, EBI-352326;
P63088:Ppp1cc; NbExp=2; IntAct=EBI-7092421, EBI-80049;
P67999:Rps6kb1; NbExp=4; IntAct=EBI-7092421, EBI-2639458;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction,
synapse, synaptosome.
-!- TISSUE SPECIFICITY: Brain, and widely expressed in neural tissue.
Highly concentrated in synapses of developed neurons. In
developing neurons, concentrated in the lamellipodia of the growth
cone.
-!- DOMAIN: Interacts with p70-S6K via its PDZ domain.
-!- DOMAIN: The PP1 binding region is natively unstructured, upon PP1
binding, it acquires structure, blocks a substrate-binding site,
and restricts PP1 phosphatase specificity to a subset of
substrates.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U72994; AAC53454.1; -; mRNA.
PIR; T43275; T43275.
RefSeq; NP_445925.1; NM_053473.2.
UniGene; Rn.10849; -.
PDB; 2FN5; NMR; -; A=502-592.
PDB; 2GLE; NMR; -; A=986-1056.
PDB; 3HVQ; X-ray; 2.20 A; C/D=426-592.
PDBsum; 2FN5; -.
PDBsum; 2GLE; -.
PDBsum; 3HVQ; -.
ProteinModelPortal; O35867; -.
SMR; O35867; -.
BioGrid; 250039; 2.
DIP; DIP-40850N; -.
IntAct; O35867; 5.
MINT; O35867; -.
STRING; 10116.ENSRNOP00000011756; -.
iPTMnet; O35867; -.
PhosphoSitePlus; O35867; -.
PaxDb; O35867; -.
PRIDE; O35867; -.
Ensembl; ENSRNOT00000011756; ENSRNOP00000011756; ENSRNOG00000008869.
GeneID; 84685; -.
KEGG; rno:84685; -.
UCSC; RGD:632280; rat.
CTD; 55607; -.
RGD; 632280; Ppp1r9a.
eggNOG; KOG1945; Eukaryota.
eggNOG; ENOG410Y7F2; LUCA.
GeneTree; ENSGT00390000010033; -.
HOGENOM; HOG000252962; -.
HOVERGEN; HBG005213; -.
InParanoid; O35867; -.
KO; K17551; -.
OMA; HYAQYDA; -.
OrthoDB; EOG091G0NSU; -.
PhylomeDB; O35867; -.
EvolutionaryTrace; O35867; -.
PRO; PR:O35867; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000008869; -.
Genevisible; O35867; RN.
GO; GO:0015629; C:actin cytoskeleton; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
GO; GO:0005856; C:cytoskeleton; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0044326; C:dendritic spine neck; IDA:RGD.
GO; GO:0030175; C:filopodium; IDA:RGD.
GO; GO:0030426; C:growth cone; IDA:MGI.
GO; GO:1990761; C:growth cone lamellipodium; IDA:RGD.
GO; GO:0030027; C:lamellipodium; IDA:RGD.
GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0051015; F:actin filament binding; IDA:WormBase.
GO; GO:0051020; F:GTPase binding; IDA:RGD.
GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0008157; F:protein phosphatase 1 binding; IDA:RGD.
GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
GO; GO:0097237; P:cellular response to toxic substance; IDA:RGD.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:RGD.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IMP:RGD.
GO; GO:1904049; P:negative regulation of spontaneous neurotransmitter secretion; IMP:RGD.
GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:RGD.
GO; GO:0048666; P:neuron development; IEP:RGD.
GO; GO:0031175; P:neuron projection development; IDA:MGI.
GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
GO; GO:1900454; P:positive regulation of long term synaptic depression; IMP:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:RGD.
GO; GO:0030833; P:regulation of actin filament polymerization; IMP:RGD.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:RGD.
GO; GO:0051489; P:regulation of filopodium assembly; IMP:RGD.
GO; GO:0051963; P:regulation of synapse assembly; IMP:RGD.
GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:RGD.
InterPro; IPR029994; Neurabin-1.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
PANTHER; PTHR16154:SF22; PTHR16154:SF22; 2.
Pfam; PF00595; PDZ; 1.
Pfam; PF07647; SAM_2; 1.
SMART; SM00228; PDZ; 1.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS50106; PDZ; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Cell junction; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
Differentiation; Direct protein sequencing; Neurogenesis;
Phosphoprotein; Reference proteome; Synapse; Synaptosome.
CHAIN 1 1095 Neurabin-1.
/FTId=PRO_0000071508.
DOMAIN 505 593 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 989 1052 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
REGION 1 144 Actin-binding.
REGION 426 503 Interaction with protein phosphatase 1.
REGION 598 1091 Interaction with TGN38.
{ECO:0000269|PubMed:10514494}.
COILED 598 628 {ECO:0000255}.
COILED 674 825 {ECO:0000255}.
COILED 1036 1091 {ECO:0000255}.
MOD_RES 192 192 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 312 312 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ULJ8}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 461 461 Phosphoserine; by PKA.
{ECO:0000269|PubMed:10504266}.
MOD_RES 841 841 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ULJ8}.
MOD_RES 916 916 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 929 929 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 957 957 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 958 958 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 961 961 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 975 975 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MUTAGEN 461 461 S->E: 35-fold decrease in inhibition of
PP1-alpha. {ECO:0000269|PubMed:10504266}.
MUTAGEN 516 517 GI->AA: Abolishes P70-S6K binding.
{ECO:0000269|PubMed:10504266}.
STRAND 440 443 {ECO:0000244|PDB:3HVQ}.
STRAND 465 470 {ECO:0000244|PDB:3HVQ}.
TURN 473 475 {ECO:0000244|PDB:3HVQ}.
HELIX 485 498 {ECO:0000244|PDB:3HVQ}.
STRAND 501 509 {ECO:0000244|PDB:3HVQ}.
STRAND 516 522 {ECO:0000244|PDB:3HVQ}.
STRAND 527 529 {ECO:0000244|PDB:2FN5}.
STRAND 530 540 {ECO:0000244|PDB:3HVQ}.
HELIX 545 549 {ECO:0000244|PDB:3HVQ}.
STRAND 550 552 {ECO:0000244|PDB:2FN5}.
STRAND 557 561 {ECO:0000244|PDB:3HVQ}.
HELIX 571 580 {ECO:0000244|PDB:3HVQ}.
STRAND 583 591 {ECO:0000244|PDB:3HVQ}.
HELIX 986 988 {ECO:0000244|PDB:2GLE}.
HELIX 992 994 {ECO:0000244|PDB:2GLE}.
HELIX 995 1000 {ECO:0000244|PDB:2GLE}.
TURN 1001 1003 {ECO:0000244|PDB:2GLE}.
HELIX 1004 1010 {ECO:0000244|PDB:2GLE}.
TURN 1011 1014 {ECO:0000244|PDB:2GLE}.
HELIX 1017 1021 {ECO:0000244|PDB:2GLE}.
HELIX 1025 1029 {ECO:0000244|PDB:2GLE}.
TURN 1030 1032 {ECO:0000244|PDB:2GLE}.
HELIX 1036 1047 {ECO:0000244|PDB:2GLE}.
HELIX 1049 1055 {ECO:0000244|PDB:2GLE}.
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


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