SYNPO_RAT
ID SYNPO_RAT Reviewed; 931 AA.
AC Q9Z327;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Synaptopodin;
GN Name=Synpo;
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 (ISOFORM 3), TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RC TISSUE=Hippocampus;
RX PubMed=9314539; DOI=10.1083/jcb.139.1.193;
RA Mundel P., Heid H.W., Mundel T.M., Krueger M., Reiser J., Kriz W.;
RT "Synaptopodin: an actin-associated protein in telencephalic dendrites and
RT renal podocytes.";
RL J. Cell Biol. 139:193-204(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11595771; DOI=10.1046/j.1471-4159.2001.00552.x;
RA Yamazaki M., Matsuo R., Fukazawa Y., Ozawa F., Inokuchi K.;
RT "Regulated expression of an actin-associated protein, synaptopodin, during
RT long-term potentiation.";
RL J. Neurochem. 79:192-199(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-490; SER-514;
RP THR-549; SER-767 AND SER-835, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Actin-associated protein that may play a role in modulating
CC actin-based shape and motility of dendritic spines and renal podocyte
CC foot processes. Seems to be essential for the formation of spine
CC apparatuses in spines of telencephalic neurons, which is involved in
CC synaptic plasticity. {ECO:0000269|PubMed:11595771}.
CC -!- SUBUNIT: Interacts with BAIAP1. Interacts with actin. Interacts (via
CC PPxY motifs) with WWC1 (via WW domains) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11595771, ECO:0000269|PubMed:9314539}. Cell
CC junction, tight junction {ECO:0000269|PubMed:9314539}. Perikaryon. Cell
CC projection, dendritic spine {ECO:0000269|PubMed:9314539}. Postsynaptic
CC density {ECO:0000269|PubMed:9314539}. Synapse
CC {ECO:0000269|PubMed:9314539}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8N3V7}. Note=Localized at the tight junction of
CC cells. In brain, localized to the postsynaptic densities and in the
CC perikarya. Associated with dendritic spines of a subset of synapses
CC (PubMed:9314539). {ECO:0000269|PubMed:9314539}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Z327-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z327-2; Sequence=VSP_010480, VSP_010481;
CC Name=3;
CC IsoId=Q9Z327-3; Sequence=VSP_010480;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain and at moderate,
CC but still significant levels in the heart, skeletal muscle, lung and
CC kidney. In brain, expressed in the cerebral cortex, hippocampus,
CC olfactory bulb and striatum. {ECO:0000269|PubMed:11595771,
CC ECO:0000269|PubMed:9314539}.
CC -!- DEVELOPMENTAL STAGE: First expressed around day 15, increased
CC thereafter, and reached the maximum level of expression in the adult
CC brain. In vitro, in neurons, expression started at E12, increased
CC thereafter in parallel with process of spine formation, and reached its
CC maximum level after 25 days. {ECO:0000269|PubMed:9314539}.
CC -!- INDUCTION: Depends on the long term potentiation (LTP) and the
CC activation of NMDA receptor signaling. {ECO:0000269|PubMed:11595771}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the synaptopodin family. {ECO:0000305}.
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DR EMBL; AB013130; BAA34925.1; -; mRNA.
DR EMBL; AABR03110007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_067727.2; NM_021695.2. [Q9Z327-3]
DR RefSeq; XP_017456508.1; XM_017601019.1. [Q9Z327-1]
DR AlphaFoldDB; Q9Z327; -.
DR BioGRID; 248774; 5.
DR IntAct; Q9Z327; 2.
DR MINT; Q9Z327; -.
DR iPTMnet; Q9Z327; -.
DR PhosphoSitePlus; Q9Z327; -.
DR PaxDb; Q9Z327; -.
DR PRIDE; Q9Z327; -.
DR Ensembl; ENSRNOT00000064686; ENSRNOP00000061109; ENSRNOG00000019181. [Q9Z327-3]
DR Ensembl; ENSRNOT00000102376; ENSRNOP00000077576; ENSRNOG00000019181. [Q9Z327-1]
DR Ensembl; ENSRNOT00000103982; ENSRNOP00000087286; ENSRNOG00000019181. [Q9Z327-2]
DR GeneID; 60324; -.
DR KEGG; rno:60324; -.
DR UCSC; RGD:620668; rat. [Q9Z327-1]
DR CTD; 11346; -.
DR RGD; 620668; Synpo.
DR eggNOG; ENOG502R7RM; Eukaryota.
DR GeneTree; ENSGT00950000183054; -.
DR HOGENOM; CLU_071316_1_0_1; -.
DR InParanoid; Q9Z327; -.
DR OrthoDB; 691538at2759; -.
DR PhylomeDB; Q9Z327; -.
DR TreeFam; TF330867; -.
DR PRO; PR:Q9Z327; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000019181; Expressed in frontal cortex and 18 other tissues.
DR ExpressionAtlas; Q9Z327; baseline and differential.
DR Genevisible; Q9Z327; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0097444; C:spine apparatus; IDA:SynGO.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0098886; P:modification of dendritic spine; ISO:RGD.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISO:RGD.
DR GO; GO:0099588; P:positive regulation of postsynaptic cytosolic calcium concentration; ISO:RGD.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:1905355; P:spine apparatus assembly; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR InterPro; IPR028753; Synpo.
DR PANTHER; PTHR24217:SF13; PTHR24217:SF13; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Cell projection;
KW Cytoplasm; Cytoskeleton; Glycoprotein; Methylation; Phosphoprotein;
KW Reference proteome; Synapse; Tight junction.
FT CHAIN 1..931
FT /note="Synaptopodin"
FT /id="PRO_0000187672"
FT REGION 56..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 551..554
FT /note="PPxY motif"
FT MOTIF 570..573
FT /note="PPxY motif"
FT COMPBIAS 149..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC35"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC35"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC35"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 549
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3V7"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3V7"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3V7"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC35"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 771
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC35"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 850
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC35"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3V7"
FT VAR_SEQ 1..239
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_010480"
FT VAR_SEQ 923..931
FT /note="VWKPSFCFK -> DRPESLPTSPPWTPGASRPPSSLDGWIITSVGTCPEYSQ
FT ELTACWMIPKEQKEPVMAVPGDLADPVPSLDLGKKLSVPQDLMIEELSLRNNRGSLLFQ
FT KRQRRVQKFTFELSESLQGILAGSARGKAAGRAAVATVPNGLEEQNHHSETHTHVFQGS
FT PGDSGIAHPGAAGTGSVRSPSVLAPGYAEPLKGVPPEKFNHTAIPKGYRCPWQEFISYR
FT DYYPSGSRSHTPIPRDYRNFNKTPVPFGGPHVGEAIFHAGTPFVPEPFSGLELLRLRPN
FT FNRVAQGWVRKLPESEEL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010481"
FT CONFLICT 561
FT /note="A -> V (in Ref. 1; BAA34925)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="Q -> R (in Ref. 1; BAA34925)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="H -> Y (in Ref. 1; BAA34925)"
FT /evidence="ECO:0000305"
FT CONFLICT 815
FT /note="I -> T (in Ref. 1; BAA34925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 931 AA; 99986 MW; 4D50DDBF129EC5E1 CRC64;
MLGTHFPPPP LGPSEGRAAP CTFQIPDGSY RCLALEAEES SSEDGLQGEV RLVDLEEEGT
SKSRVNHGTP PLSRAPAIIQ PSSCCREARG GFQHSDKPSR EWDVVQARKV MTASVSSSPV
PRVAQKPALG RSTSFTEKDL KEAKERSQRI AAQLTTPPSS NSRGVQLFNR RRQRVNEFTL
ESRGQRSPKL SQEALQTGHP SSPIGHAPGL SVNPTSPSKP GSPKHSSSQS PSRGVPGHIM
EGYSEEASLL RHLEKVASEE EEVPLVVYLK ENAALLTANG LHLSQNRETQ QSSPNPPETE
EVPSPAADIN QNPSSPNATL TTAASNSHHN QPTADVNQNP PATITPVQQN SSETQCSPNG
TLDSKPNTPS ADDGQRPVPA EEVRSSILLI DKVSAPPSAA SPFSREATPL SSSGPPAADL
MSSSLLIGMQ PSTLVASAEQ EVSGHAAVTT PTKVYSEVHL TLAKPASVVN RTARPFGMQS
PGTTSQIEQS PMMGRRHFGE KAWAPPASSM ADRSPQPQRH IMARSPMVER RLVGQRSPVV
ERRPLGNFTP PPTYAETLST APVASQVRSP PSYSTLYPSS DPKPPHLKGQ VVPANKTGIL
EESMARRGSR KSMFTFVEKP KVTPNPDLLD LVQTADEKRR QRDQGEVGME DEPFALGAEA
SNFQQEPIAR DRSGPAAAEE TVPEWASCLK SPRIQAKPKP KPNQNLSEAS GKGAELYARR
QSRMEKYVIE SSGHAELARC PSPTMSLPSS WKYTTNAPGG FRVASLSPAR TPPASLYHGY
LPENGVLRPE PTKQQPHQMR PSLYALSPVK EPAKISSRAT SSRASSRTVS PRAASPAKPS
SLDLVPNLPR AGLPPSPALP RPSRSSPGLY NAPVQDSLQP TAVSPTYSSD ISPVSPSRAW
SPRAKQAPRP SFSTRNAGIE AQVWKPSFCF K
