LZTS3_RAT
ID LZTS3_RAT Reviewed; 703 AA.
AC Q8K1Q4;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Leucine zipper putative tumor suppressor 3 {ECO:0000305};
DE AltName: Full=ProSAP-interacting protein 1 {ECO:0000303|PubMed:16522626};
DE Short=ProSAPiP1 {ECO:0000303|PubMed:16522626};
GN Name=Lzts3 {ECO:0000312|RGD:631327};
GN Synonyms=Prosapip1 {ECO:0000303|PubMed:16522626};
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], INTERACTION WITH SHANK3 AND SIPA1L1, SUBUNIT,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF SER-700; THR-701
RP AND ILE-703, AND TISSUE SPECIFICITY.
RX PubMed=16522626; DOI=10.1074/jbc.m601101200;
RA Wendholt D., Spilker C., Schmitt A., Dolnik A., Smalla K.H., Proepper C.,
RA Bockmann J., Sobue K., Gundelfinger E.D., Kreutz M.R., Boeckers T.M.;
RT "ProSAP-interacting protein 1 (ProSAPiP1), a novel protein of the
RT postsynaptic density that links the spine-associated Rap-Gap (SPAR) to the
RT scaffolding protein ProSAP2/Shank3.";
RL J. Biol. Chem. 281:13805-13816(2006).
RN [2]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=27252646; DOI=10.3389/fnsyn.2016.00013;
RA Reim D., Weis T.M., Halbedl S., Delling J.P., Grabrucker A.M.,
RA Boeckers T.M., Schmeisser M.J.;
RT "The Shank3 interaction partner ProSAPiP1 regulates postsynaptic SPAR
RT levels and the maturation of dendritic spines in hippocampal neurons.";
RL Front. Synaptic Neurosci. 8:13-13(2016).
CC -!- FUNCTION: May be involved in promoting the maturation of dendritic
CC spines, probably via regulating SIPA1L1 levels at the postsynaptic
CC density of synapses(PubMed:27252646). {ECO:0000269|PubMed:27252646}.
CC -!- SUBUNIT: Interacts (via C-terminus) with SHANK3 (via PDZ domain)
CC (PubMed:16522626). Interacts (via coiled coil) with SIPA1L1
CC (PubMed:16522626). Can form homooligomers (PubMed:16522626).
CC {ECO:0000269|PubMed:16522626}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:27252646}.
CC Postsynaptic density {ECO:0000269|PubMed:16522626,
CC ECO:0000269|PubMed:27252646}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:16522626}. Cell projection, dendrite
CC {ECO:0000269|PubMed:16522626}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16522626}. Note=Rather found at excitatory than
CC inhibitory synapses (PubMed:27252646). {ECO:0000269|PubMed:16522626,
CC ECO:0000269|PubMed:27252646}.
CC -!- TISSUE SPECIFICITY: Detected in brain, with highest expression in brain
CC cortex, caudate putamen, cerebellum and hippocampus. Detected in
CC neuropil (at protein level). Detected in brain and kidney.
CC {ECO:0000269|PubMed:16522626}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels in newborn brain. Levels
CC increase steadily during postnatal development up to adulthood.
CC {ECO:0000269|PubMed:16522626}.
CC -!- SIMILARITY: Belongs to the LZTS3 family. {ECO:0000305}.
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DR EMBL; AJ278801; CAC82182.2; -; mRNA.
DR RefSeq; NP_742019.2; NM_172022.2.
DR PDB; 5OVV; X-ray; 1.40 A; B=698-703.
DR PDBsum; 5OVV; -.
DR AlphaFoldDB; Q8K1Q4; -.
DR SMR; Q8K1Q4; -.
DR STRING; 10116.ENSRNOP00000028835; -.
DR iPTMnet; Q8K1Q4; -.
DR PhosphoSitePlus; Q8K1Q4; -.
DR PaxDb; Q8K1Q4; -.
DR PRIDE; Q8K1Q4; -.
DR GeneID; 280670; -.
DR KEGG; rno:280670; -.
DR UCSC; RGD:631327; rat.
DR CTD; 9762; -.
DR RGD; 631327; Lzts3.
DR eggNOG; ENOG502QWFS; Eukaryota.
DR InParanoid; Q8K1Q4; -.
DR OrthoDB; 363339at2759; -.
DR PhylomeDB; Q8K1Q4; -.
DR PRO; PR:Q8K1Q4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IPI:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:UniProtKB.
DR InterPro; IPR045329; LZTS.
DR InterPro; IPR033295; LZTS3.
DR PANTHER; PTHR19354; PTHR19354; 1.
DR PANTHER; PTHR19354:SF6; PTHR19354:SF6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..703
FT /note="Leucine zipper putative tumor suppressor 3"
FT /id="PRO_0000394200"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 348..526
FT /evidence="ECO:0000255"
FT COILED 600..669
FT /evidence="ECO:0000255"
FT COMPBIAS 88..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AHG0"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AHG0"
FT MUTAGEN 700
FT /note="S->G,S: Abolishes interaction with SHANK3."
FT /evidence="ECO:0000269|PubMed:16522626"
FT MUTAGEN 701
FT /note="T->A,S: Abolishes interaction with SHANK3."
FT /evidence="ECO:0000269|PubMed:16522626"
FT MUTAGEN 703
FT /note="I->A,G,V: Abolishes interaction with SHANK3."
FT /evidence="ECO:0000269|PubMed:16522626"
FT STRAND 699..702
FT /evidence="ECO:0007829|PDB:5OVV"
SQ SEQUENCE 703 AA; 75179 MW; 3B6F33FE933B60D1 CRC64;
MAPADLASEG PKLEDPPAPH LFGKCPSGLI MANVETLPVR ADPGRDPLLA FAPRPAELGP
PDPRLTMGSV GGGVTHAQEF PMKSVGTRTG GGGSQGSFPG PRSSGSGTNR ERPGPGRYPS
EDKVLANSLY LNGELRGSDH TDVCGNVVGS SGGSSSSGGS DKAPPQYREP NHPPKLLTTS
GKLDQCSEPL VRPSAFKPVV PKNFHSMQNL CPPQTNGTPE GRQGPAGLKG GLEKSRTMTP
AGGSGGGGLS DSGRNSLTSL PTYSSSYSQH LAPLSASTSH INRIGTPGYS SGGGGGGSGY
QDLGTSDSGR ASSKSGSSSS MGRSGHLGSG EGGNGGLPFA ACSPPSPSAL IQELEERLWE
KEQEVAALRR SQEQSEAAVA QVLEERQKAW ERELAELRQG CSGKLQQVAR RAQRAQQGLQ
LQVLRLQQDK KQLQEEAAQL IRQREELEDK VAACQKEQAD FLPRMEETKW EVCQKAGEIS
LLKQQLKDSQ ADVSQKLSEI VGLRSQLREG RASLREKEEQ LLSLRDSFGS KQASLELSEG
ELPPACLKPA LTPVDLVEPQ EALASCESDE AKMRRQAGVA AAASLVSVDG EVDAGGEGGT
RALRREVGRL QAELAAERRA RERQGASFAE ERRVWLEEKE KVIEYQKQLQ LSYVEMYQRN
QQLERRLRER GAAGGSRTPT PQHGEEEKAW TPSRLERIES TEI
