LIPA3_MOUSE
ID LIPA3_MOUSE Reviewed; 1194 AA.
AC P60469; B8QI35;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Liprin-alpha-3;
DE AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-3;
DE Short=PTPRF-interacting protein alpha-3;
GN Name=Ppfia3;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:ACE63189.1};
RX PubMed=19013515; DOI=10.1016/j.ygeno.2008.10.007;
RA Zurner M., Schoch S.;
RT "The mouse and human Liprin-alpha family of scaffolding proteins: genomic
RT organization, expression profiling and regulation by alternative
RT splicing.";
RL Genomics 93:243-253(2009).
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; 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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-508; SER-645 AND
RP THR-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23124857; DOI=10.1007/s00418-012-1044-y;
RA Joshi C.S., Suryawanshi A.R., Khan S.A., Balasinor N.H., Khole V.V.;
RT "Liprin alpha3: a putative estrogen regulated acrosomal protein.";
RL Histochem. Cell Biol. 139:535-548(2013).
CC -!- FUNCTION: May regulate the disassembly of focal adhesions. May localize
CC receptor-like tyrosine phosphatases type 2A at specific sites on the
CC plasma membrane, possibly regulating their interaction with the
CC extracellular environment and their association with substrates.
CC {ECO:0000250|UniProtKB:O75145}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with liprins-alpha and
CC liprins-beta. Interacts with the second PTPase domain of PTPRD, PTPRF
CC and PTPRS. Binds RIMS1, RIMS2, RIMS3 and RIMS4.
CC {ECO:0000250|UniProtKB:O75145, ECO:0000250|UniProtKB:Q91Z79}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q91Z79}.
CC Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000269|PubMed:23124857}. Note=Also detected in epididymosome.
CC {ECO:0000250|UniProtKB:Q91Z79}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60469-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60469-2; Sequence=VSP_057923;
CC -!- TISSUE SPECIFICITY: Detected in sperm (at protein level).
CC {ECO:0000269|PubMed:23124857}.
CC -!- DOMAIN: The N-terminal coiled coil regions mediate homodimerization
CC preferentially and heterodimerization type alpha/alpha. The C-terminal,
CC non-coiled coil regions mediate heterodimerization type alpha/beta and
CC interaction with PTPRD, PTPRF and PTPRS.
CC {ECO:0000250|UniProtKB:O75145}.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC {ECO:0000305}.
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DR EMBL; EU568871; ACE63189.1; -; mRNA.
DR EMBL; AC150897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC151602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058404; AAH58404.1; -; mRNA.
DR CCDS; CCDS52246.1; -. [P60469-1]
DR RefSeq; NP_084017.2; NM_029741.2. [P60469-1]
DR RefSeq; XP_006541336.1; XM_006541273.1. [P60469-1]
DR RefSeq; XP_011249214.1; XM_011250912.2. [P60469-1]
DR PDB; 4UWX; X-ray; 1.65 A; C/D=718-738.
DR PDB; 6KIP; X-ray; 1.91 A; B=806-1127.
DR PDB; 6KR4; X-ray; 2.85 A; E/F/G/H=806-1126.
DR PDBsum; 4UWX; -.
DR PDBsum; 6KIP; -.
DR PDBsum; 6KR4; -.
DR AlphaFoldDB; P60469; -.
DR SMR; P60469; -.
DR BioGRID; 218314; 24.
DR IntAct; P60469; 5.
DR MINT; P60469; -.
DR STRING; 10090.ENSMUSP00000003961; -.
DR iPTMnet; P60469; -.
DR PhosphoSitePlus; P60469; -.
DR EPD; P60469; -.
DR MaxQB; P60469; -.
DR PaxDb; P60469; -.
DR PeptideAtlas; P60469; -.
DR PRIDE; P60469; -.
DR ProteomicsDB; 265076; -. [P60469-1]
DR ProteomicsDB; 265077; -. [P60469-2]
DR Antibodypedia; 31915; 72 antibodies from 23 providers.
DR DNASU; 76787; -.
DR Ensembl; ENSMUST00000003961; ENSMUSP00000003961; ENSMUSG00000003863. [P60469-1]
DR Ensembl; ENSMUST00000211067; ENSMUSP00000148200; ENSMUSG00000003863. [P60469-1]
DR GeneID; 76787; -.
DR KEGG; mmu:76787; -.
DR UCSC; uc012fkh.1; mouse.
DR CTD; 8541; -.
DR MGI; MGI:1924037; Ppfia3.
DR VEuPathDB; HostDB:ENSMUSG00000003863; -.
DR eggNOG; KOG0249; Eukaryota.
DR GeneTree; ENSGT01050000244900; -.
DR InParanoid; P60469; -.
DR OMA; LMMMCEV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P60469; -.
DR TreeFam; TF314207; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR BioGRID-ORCS; 76787; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Ppfia3; mouse.
DR PRO; PR:P60469; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P60469; protein.
DR Bgee; ENSMUSG00000003863; Expressed in primary visual cortex and 141 other tissues.
DR ExpressionAtlas; P60469; baseline and differential.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098875; C:epididymosome; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0007269; P:neurotransmitter secretion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR GO; GO:0016081; P:synaptic vesicle docking; IDA:SynGO.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:SynGO.
DR CDD; cd09562; SAM_liprin-alpha1_2_3_4_repeat1; 1.
DR CDD; cd09565; SAM_liprin-alpha1_2_3_4_repeat2; 1.
DR CDD; cd09568; SAM_liprin-alpha1_2_3_4_repeat3; 1.
DR Gene3D; 1.10.150.50; -; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037620; Liprin-alpha_SAM_rpt_1.
DR InterPro; IPR037621; Liprin-alpha_SAM_rpt_2.
DR InterPro; IPR037622; Liprin-alpha_SAM_rpt_3.
DR InterPro; IPR030440; PPFIA3.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; PTHR12587; 1.
DR PANTHER; PTHR12587:SF4; PTHR12587:SF4; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF47769; SSF47769; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1194
FT /note="Liprin-alpha-3"
FT /id="PRO_0000191030"
FT DOMAIN 838..904
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 953..1017
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1041..1110
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..133
FT /evidence="ECO:0000255"
FT COILED 171..501
FT /evidence="ECO:0000255"
FT COILED 596..644
FT /evidence="ECO:0000255"
FT COILED 1014..1040
FT /evidence="ECO:0000255"
FT COMPBIAS 544..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75145"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75145"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75145"
FT MOD_RES 714
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 792
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q91Z79"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Z79"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13136"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75145"
FT VAR_SEQ 178..328
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057923"
FT HELIX 719..731
FT /evidence="ECO:0007829|PDB:4UWX"
FT HELIX 813..830
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 835..837
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 840..849
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 855..864
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 868..872
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 876..882
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 888..904
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 954..959
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 961..964
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 968..970
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 971..976
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 981..984
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 989..993
FT /evidence="ECO:0007829|PDB:6KIP"
FT TURN 994..996
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 1001..1016
FT /evidence="ECO:0007829|PDB:6KIP"
FT TURN 1017..1019
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 1021..1029
FT /evidence="ECO:0007829|PDB:6KIP"
FT STRAND 1032..1035
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 1038..1040
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 1043..1052
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 1056..1059
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 1060..1062
FT /evidence="ECO:0007829|PDB:6KIP"
FT TURN 1063..1066
FT /evidence="ECO:0007829|PDB:6KR4"
FT HELIX 1069..1074
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 1080..1086
FT /evidence="ECO:0007829|PDB:6KIP"
FT HELIX 1094..1111
FT /evidence="ECO:0007829|PDB:6KIP"
SQ SEQUENCE 1194 AA; 133426 MW; CA6386D6281470FA CRC64;
MMCEVMPTIS EDGRRGSALG PDEAGGELER LMVTMLTERE RLLETLREAQ DGLATAQLRL
RELGHEKDSL QRQLSIALPQ EFAALTKELN LCREQLLERE EEIAELKAER NNTRLLLEHL
ECLVSRHERS LRMTVVKRQA QSPGGVSSEV EVLKALKSLF EHHKALDEKV RERLRMALER
VAVLEEELEL SNQEALNLRD QLSRRRSGLE EPGKDGDGQT LANGLGPVGE SNRRTAELEE
ALERQRAEVC QLRERLAVLC RQMSQLEEEL GTAHRELGKA EEANSKLQRD LKEALAQRED
MEERITTLEK RYLSAQREAT SLHDANDKLE NELASKESLY RQSEEKSRQL AEWLDDAKQK
LQQTLQKAET LPEIEAQLAQ RVAALNKAEE RHGNFEERLR QLEAQLEEKN QELQRARQRE
KMNDDHNKRL SETVDKLLSE SNERLQLHLK ERMGALEEKN SLSEEIANMK KLQDELLLNK
EQLLAEMERM QMEIDQLRGR PPSSYSRSLP GSALELRYSQ APTLPSGAPL DPYGAGSGRA
GKRGRWSGAK DESSKDWDRS APAGSIPPPF PGELDGSDEE EAEGMFGAEL LSPSGQADVQ
TLAIMLQEQL EAINKEIKLI QEEKETTEQR AEELESRVSS SGLDSLGRYR SSCSLPPSLT
TSTLASPSPP SSGHSTPRLA PPSPAREGTD KTNHVSKEEA GVPRGEGPAV PGDTPPPTPR
SARLERMAQA LALQAGSPED GAPPRGSEST PDSLHKAPKR KSIKSSIGRL FGKKEKGRMG
PPGRESVSLA GTPSDETLAT DPLGLAKLTG PGDKDRRNKR KHELLEEACR QGLPFAAWDG
PTVVSWLELW VGMPAWYVAA CRANVKSGAI MANLSDTEIQ REIGISNPLH RLKLRLAIQE
MVSLTSPSAP ASSRTPTGNV WMTHEEMESL TAATKPETKE ISWEQILAYG DMNHEWVGND
WLPSLGLPQY RSYFMESLVD ARMLDHLNKK ELRGQLKMVD SFHRVSLHYG IMCLKRLNYD
RKDLERRREE SQTQIRDVMV WSNERVMGWV SGLGLKEFAT NLTESGVHGA LLALDETFDY
SDLALLLQIP TQNAQARQLL EKEFSNLISL GTDRRLDEDS AKSFSRSPSW RKMFREKDLR
GVTPDSAEML PPNFRSAAAG ALGSPGLPLR KLQPEGQTSG SSRADGVSVR TYSC
