LZTS3_MOUSE
ID LZTS3_MOUSE Reviewed; 700 AA.
AC A2AHG0; A2AHF9; Q3TSY0; Q6PE51;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Leucine zipper putative tumor suppressor 3 {ECO:0000305};
DE AltName: Full=ProSAP-interacting protein 1 {ECO:0000250|UniProtKB:Q8K1Q4};
DE Short=ProSAPiP1 {ECO:0000250|UniProtKB:Q8K1Q4};
GN Name=Lzts3 {ECO:0000312|MGI:MGI:2656976};
GN Synonyms=Prosapip1 {ECO:0000250|UniProtKB:Q8K1Q4};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-700 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-345, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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).
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. {ECO:0000250|UniProtKB:Q8K1Q4}.
CC -!- SUBUNIT: Interacts (via C-terminus) with SHANK3 (via PDZ domain).
CC Interacts (via coiled coil) with SIPA1L1. Can form homooligomers.
CC {ECO:0000250|UniProtKB:Q8K1Q4}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:Q8K1Q4}.
CC Postsynaptic density {ECO:0000250|UniProtKB:Q8K1Q4}. Cell projection,
CC dendritic spine {ECO:0000250|UniProtKB:Q8K1Q4}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:Q8K1Q4}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8K1Q4}. Note=Rather found at excitatory than
CC inhibitory synapses. {ECO:0000250|UniProtKB:Q8K1Q4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2AHG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AHG0-2; Sequence=VSP_039203;
CC Name=3;
CC IsoId=A2AHG0-3; Sequence=VSP_039204, VSP_039205;
CC -!- SIMILARITY: Belongs to the LZTS3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58280.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL731707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28282.1; -; Genomic_DNA.
DR EMBL; CH466519; EDL28283.1; -; Genomic_DNA.
DR EMBL; AK161711; BAE36545.1; -; mRNA.
DR EMBL; BC058280; AAH58280.1; ALT_INIT; mRNA.
DR CCDS; CCDS50714.1; -. [A2AHG0-1]
DR CCDS; CCDS71145.1; -. [A2AHG0-2]
DR RefSeq; NP_001277956.1; NM_001291027.1.
DR RefSeq; NP_001277957.1; NM_001291028.1. [A2AHG0-2]
DR RefSeq; NP_922936.3; NM_197945.4. [A2AHG0-1]
DR RefSeq; XP_017173693.1; XM_017318204.1. [A2AHG0-1]
DR AlphaFoldDB; A2AHG0; -.
DR SMR; A2AHG0; -.
DR BioGRID; 232338; 4.
DR IntAct; A2AHG0; 4.
DR MINT; A2AHG0; -.
DR STRING; 10090.ENSMUSP00000037109; -.
DR iPTMnet; A2AHG0; -.
DR PhosphoSitePlus; A2AHG0; -.
DR jPOST; A2AHG0; -.
DR MaxQB; A2AHG0; -.
DR PaxDb; A2AHG0; -.
DR PeptideAtlas; A2AHG0; -.
DR PRIDE; A2AHG0; -.
DR ProteomicsDB; 291983; -. [A2AHG0-1]
DR ProteomicsDB; 291984; -. [A2AHG0-2]
DR ProteomicsDB; 291985; -. [A2AHG0-3]
DR Antibodypedia; 23459; 93 antibodies from 25 providers.
DR Ensembl; ENSMUST00000045761; ENSMUSP00000037109; ENSMUSG00000037703. [A2AHG0-1]
DR Ensembl; ENSMUST00000089561; ENSMUSP00000086990; ENSMUSG00000037703. [A2AHG0-1]
DR Ensembl; ENSMUST00000110260; ENSMUSP00000105889; ENSMUSG00000037703. [A2AHG0-2]
DR GeneID; 241638; -.
DR KEGG; mmu:241638; -.
DR UCSC; uc008mjo.3; mouse. [A2AHG0-2]
DR UCSC; uc008mjq.3; mouse. [A2AHG0-1]
DR CTD; 9762; -.
DR MGI; MGI:2656976; Lzts3.
DR VEuPathDB; HostDB:ENSMUSG00000037703; -.
DR eggNOG; ENOG502QWFS; Eukaryota.
DR GeneTree; ENSGT00940000154078; -.
DR HOGENOM; CLU_026379_1_0_1; -.
DR InParanoid; A2AHG0; -.
DR OMA; PATCLKP; -.
DR OrthoDB; 363339at2759; -.
DR PhylomeDB; A2AHG0; -.
DR TreeFam; TF331420; -.
DR BioGRID-ORCS; 241638; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Lzts3; mouse.
DR PRO; PR:A2AHG0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AHG0; protein.
DR Bgee; ENSMUSG00000037703; Expressed in caudate-putamen and 189 other tissues.
DR Genevisible; A2AHG0; MM.
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; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS: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 Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..700
FT /note="Leucine zipper putative tumor suppressor 3"
FT /id="PRO_0000394199"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 345..523
FT /evidence="ECO:0000255"
FT COILED 597..666
FT /evidence="ECO:0000255"
FT COMPBIAS 88..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 70..183
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039203"
FT VAR_SEQ 589..591
FT /note="VEA -> IAG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039204"
FT VAR_SEQ 592..700
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039205"
FT CONFLICT 97
FT /note="S -> G (in Ref. 1; BAE36545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 700 AA; 74986 MW; 2DD613B6F77BB6A2 CRC64;
MAPADLASEG PKLEDPPAPH LFGKCPSGLI MAKLETLPVR ADPGRDPLLA FAPRPSELGP
PDPRLTMGSV GSGVTHAQEF PMKSVGTRTG GGGNQGSFPG PRSGGSGANR ERPGRYPSED
KVLANSLYLN GELRGSDHTD VCGNVVGSSG GSSSSGGSDK APPQYREPNH PPKLLTTSGK
LDQCSEPLVR PSAFKPVVPK NFHSMQNLCP PQTNGTPEGR QGPAGLKGGL DKSRTMTPAG
GSGGGLSDSG RNSLTSLPTY SSSYSQHLAP LSASTSHINR IGTAGYSSGS SGGGSGYQDL
GTSDSGRASS KSGSSSSMGR SGHLGSGEGG NGGLPFAACS PPSPSALIQE LEERLWEKEQ
EVAALRRSLE QSEAAVAQVL EERQKAWERE LAELRQGCSG KLQQVARRAQ RAQQGLQLQV
LRLQQDKKQL QEEAAQLIRQ REELEDKVAV CQKEQADFLP RMEETKWEVC QKAGEISLLK
QQLKDSQADV SQKLSEIVGL RSQLREGRAS LREKEEQLLS LRDSFGSKQA SLELSEGELP
PACLKPALTP VDLVEPQEAL ASCESDEAKM RRQAGVAAAA SLVSVDGEVE AGGEGGTRAL
RREVGRLQAE LAAERRARER QGASFAEERR VWLEEKEKVI EYQKQLQLSY VEMYQRNQQL
ERRLRERGAA GGSSTPTPQH GEEKKAWTPS RLERIESTEI
