ID   LZTS3_HUMAN             Reviewed;         673 AA.
AC   O60299; A2A2Q7; D3DVX6; Q8IXX8;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 167.
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|HGNC:HGNC:30139};
GN   Synonyms=KIAA0552 {ECO:0000312|EMBL:BAA25478.2}, PROSAPIP1
GN   {ECO:0000250|UniProtKB:Q8K1Q4};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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).
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=2;
CC       Name=1;
CC         IsoId=O60299-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60299-2; Sequence=VSP_039202;
CC   -!- SIMILARITY: Belongs to the LZTS3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA25478.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB011124; BAA25478.2; ALT_INIT; mRNA.
DR   EMBL; AL121891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471133; EAX10545.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10546.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10547.1; -; Genomic_DNA.
DR   EMBL; BC038860; AAH38860.1; -; mRNA.
DR   CCDS; CCDS13049.1; -. [O60299-1]
DR   CCDS; CCDS63218.1; -. [O60299-2]
DR   PIR; T00328; T00328.
DR   RefSeq; NP_001269462.1; NM_001282533.1. [O60299-2]
DR   RefSeq; XP_005260949.1; XM_005260892.1.
DR   RefSeq; XP_005260950.1; XM_005260893.2.
DR   AlphaFoldDB; O60299; -.
DR   SMR; O60299; -.
DR   BioGRID; 115109; 28.
DR   IntAct; O60299; 10.
DR   MINT; O60299; -.
DR   STRING; 9606.ENSP00000353496; -.
DR   GlyGen; O60299; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O60299; -.
DR   PhosphoSitePlus; O60299; -.
DR   BioMuta; LZTS3; -.
DR   EPD; O60299; -.
DR   jPOST; O60299; -.
DR   MassIVE; O60299; -.
DR   MaxQB; O60299; -.
DR   PaxDb; 9606-ENSP00000353496; -.
DR   PeptideAtlas; O60299; -.
DR   ProteomicsDB; 49329; -. [O60299-1]
DR   ProteomicsDB; 49330; -. [O60299-2]
DR   Pumba; O60299; -.
DR   Antibodypedia; 23459; 126 antibodies from 25 providers.
DR   DNASU; 9762; -.
DR   Ensembl; ENST00000329152.7; ENSP00000332123.3; ENSG00000088899.16. [O60299-1]
DR   Ensembl; ENST00000337576.7; ENSP00000338166.6; ENSG00000088899.16. [O60299-1]
DR   Ensembl; ENST00000360342.7; ENSP00000353496.3; ENSG00000088899.16. [O60299-2]
DR   Ensembl; ENST00000645462.1; ENSP00000495241.1; ENSG00000088899.16. [O60299-2]
DR   GeneID; 9762; -.
DR   KEGG; hsa:9762; -.
DR   MANE-Select; ENST00000337576.7; ENSP00000338166.6; NM_001365618.1; NP_001352547.1.
DR   UCSC; uc002wia.3; human. [O60299-1]
DR   AGR; HGNC:30139; -.
DR   CTD; 9762; -.
DR   DisGeNET; 9762; -.
DR   GeneCards; LZTS3; -.
DR   HGNC; HGNC:30139; LZTS3.
DR   HPA; ENSG00000088899; Tissue enhanced (brain).
DR   MIM; 610484; gene.
DR   neXtProt; NX_O60299; -.
DR   OpenTargets; ENSG00000088899; -.
DR   VEuPathDB; HostDB:ENSG00000088899; -.
DR   eggNOG; ENOG502QWFS; Eukaryota.
DR   GeneTree; ENSGT00940000154078; -.
DR   HOGENOM; CLU_026379_1_0_1; -.
DR   InParanoid; O60299; -.
DR   OMA; HMQQDIQ; -.
DR   OrthoDB; 5394101at2759; -.
DR   PhylomeDB; O60299; -.
DR   PathwayCommons; O60299; -.
DR   SignaLink; O60299; -.
DR   BioGRID-ORCS; 9762; 8 hits in 975 CRISPR screens.
DR   ChiTaRS; LZTS3; human.
DR   GenomeRNAi; 9762; -.
DR   Pharos; O60299; Tbio.
DR   PRO; PR:O60299; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; O60299; Protein.
DR   Bgee; ENSG00000088899; Expressed in Brodmann (1909) area 10 and 182 other cell types or tissues.
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; IBA:GO_Central.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR   InterPro; IPR045329; LZTS.
DR   PANTHER; PTHR19354; ZIPPER PUTATIVE TUMOR SUPPRESSOR 2 HOMOLOG-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR19354:SF6; ZIPPER PUTATIVE TUMOR SUPPRESSOR 3-RELATED; 1.
DR   Pfam; PF06818; Fez1; 1.
DR   Genevisible; O60299; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein; Reference proteome; Synapse.
FT   CHAIN           1..673
FT                   /note="Leucine zipper putative tumor suppressor 3"
FT                   /id="PRO_0000050760"
FT   REGION          1..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          317..496
FT                   /evidence="ECO:0000255"
FT   COILED          571..639
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        58..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..673
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2AHG0"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2AHG0"
FT   VAR_SEQ         351..396
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_039202"
FT   CONFLICT        557
FT                   /note="S -> Y (in Ref. 4; AAH38860)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   673 AA;  71791 MW;  3E548EC03A01F770 CRC64;
     MAKLETLPVR ADPGRDPLLA FAPRPSELGP PDPRLAMGSV GSGVAHAQEF AMKSVGTRTG
     GGGSQGSFPG PRGSGSGASR ERPGRYPSED KGLANSLYLN GELRGSDHTD VCGNVVGSSG
     GSSSSGGSDK APPQYREPSH PPKLLATSGK LDQCSEPLVR PSAFKPVVPK NFHSMQNLCP
     PQTNGTPEGR QGPGGLKGGL DKSRTMTPAG GSGSGLSDSG RNSLTSLPTY SSSYSQHLAP
     LSASTSHINR IGTASYGSGS GGSSGGGSGY QDLGTSDSGR ASSKSGSSSS MGRPGHLGSG
     EGGGGGLPFA ACSPPSPSAL IQELEERLWE KEQEVAALRR SLEQSEAAVA QVLEERQKAW
     ERELAELRQG CSGKLQQVAR RAQRAQQGLQ LQVLRLQQDK KQLQEEAARL MRQREELEDK
     VAACQKEQAD FLPRIEETKW EVCQKAGEIS LLKQQLKDSQ ADVSQKLSEI VGLRSQLREG
     RASLREKEEQ LLSLRDSFSS KQASLELGEG ELPAACLKPA LTPVDPAEPQ DALATCESDE
     AKMRRQAGVA AAASLVSVDG EAEAGGESGT RALRREVGRL QAELAAERRA RERQGASFAE
     ERRVWLEEKE KVIEYQKQLQ LSYVEMYQRN QQLERRLRER GAAGGASTPT PQHGEEKKAW
     TPSRLERIES TEI
//