LIPA2_MOUSE
ID LIPA2_MOUSE Reviewed; 1257 AA.
AC Q8BSS9; Q6P1D2; Q8BN73;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Liprin-alpha-2;
DE AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-2;
DE Short=PTPRF-interacting protein alpha-2;
GN Name=Ppfia2;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-215 AND 1019-1257.
RC STRAIN=C57BL/6J; TISSUE=Eye, and Pituitary;
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 [4]
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; THR-237; SER-239;
RP SER-687; SER-689; SER-817 AND SER-820, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Alters PTPRF cellular localization and induces PTPRF
CC clustering. May regulate the disassembly of focal adhesions. May
CC localize receptor-like tyrosine phosphatases type 2A at specific sites
CC on the plasma membrane, possibly regulating their interaction with the
CC extracellular environment and their association with substrates. In
CC neuronal cells, is a scaffolding protein in the dendritic spines which
CC acts as immobile postsynaptic post able to recruit KIF1A-driven dense
CC core vesicles to dendritic spines. {ECO:0000250|UniProtKB:O75334}.
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. Interacts with KIF1A; the interaction decreases in presence
CC of calcium. {ECO:0000250|UniProtKB:O75334}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75334}. Cell
CC surface {ECO:0000250|UniProtKB:O75334}. Cell projection, dendritic
CC spine {ECO:0000250|UniProtKB:O75334}. Note=Colocalizes with PTPRF at
CC the cell surface. {ECO:0000250|UniProtKB:O75334}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:O75334}.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC {ECO:0000305}.
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DR EMBL; AC111014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065133; AAH65133.1; -; mRNA.
DR EMBL; AK030621; BAC27051.1; -; mRNA.
DR EMBL; AK087448; BAC39878.1; -; mRNA.
DR CCDS; CCDS56746.1; -.
DR RefSeq; NP_796347.2; NM_177373.4.
DR AlphaFoldDB; Q8BSS9; -.
DR SMR; Q8BSS9; -.
DR BioGRID; 236493; 11.
DR IntAct; Q8BSS9; 4.
DR MINT; Q8BSS9; -.
DR STRING; 10090.ENSMUSP00000029404; -.
DR iPTMnet; Q8BSS9; -.
DR PhosphoSitePlus; Q8BSS9; -.
DR EPD; Q8BSS9; -.
DR jPOST; Q8BSS9; -.
DR MaxQB; Q8BSS9; -.
DR PaxDb; Q8BSS9; -.
DR PeptideAtlas; Q8BSS9; -.
DR PRIDE; Q8BSS9; -.
DR ProteomicsDB; 291957; -.
DR DNASU; 327814; -.
DR GeneID; 327814; -.
DR KEGG; mmu:327814; -.
DR CTD; 8499; -.
DR MGI; MGI:2443834; Ppfia2.
DR eggNOG; KOG0249; Eukaryota.
DR InParanoid; Q8BSS9; -.
DR OrthoDB; 440941at2759; -.
DR PhylomeDB; Q8BSS9; -.
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; 327814; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Ppfia2; mouse.
DR PRO; PR:Q8BSS9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BSS9; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:GOC.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; 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:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0099181; F:structural constituent of presynapse; ISO:MGI.
DR GO; GO:0099519; P:dense core granule cytoskeletal transport; ISS:UniProtKB.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
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; IPR030441; PPFIA2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; PTHR12587; 1.
DR PANTHER; PTHR12587:SF6; PTHR12587:SF6; 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 Cell projection; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; Synapse.
FT CHAIN 1..1257
FT /note="Liprin-alpha-2"
FT /id="PRO_0000191028"
FT DOMAIN 898..964
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1020..1084
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1108..1177
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 29..154
FT /evidence="ECO:0000255"
FT COILED 185..235
FT /evidence="ECO:0000255"
FT COILED 264..541
FT /evidence="ECO:0000255"
FT COILED 643..695
FT /evidence="ECO:0000255"
FT COILED 1081..1107
FT /evidence="ECO:0000255"
FT COMPBIAS 10..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 516..517
FT /note="VS -> ER (in Ref. 2; AAH65133)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="Missing (in Ref. 2; AAH65133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1257 AA; 143234 MW; 2EC6B680B46EA4B2 CRC64;
MMCEVMPTIN EDTPMSQRGS QSSGSDSDSH FEQLMVNMLD ERDRLLDTLR ETQESLSLAQ
QRLQDVIYDR DSLQRQLNSA LPQDIESLTG GLTGSKGADP PEFAALTKEL NACREQLLEK
EEEISELKAE RNNTRLLLEH LECLVSRHER SLRMTVVKRQ AQSPSGVSSE VEVLKALKSL
FEHHKALDEK VRERLRVSLE RVSALEEELA AANQEIVALR EQNVHIQRKM VSSEGSTESE
HLEGMEAGQK VHEKRLSNGS IDSTDDTSQI VELQELLEKQ NYEMAQMKER LTALSSRVGE
VEQEAETARK DLIKTEEMNT KYQRDIREAM AQKEDMEERI TTLEKRYLSA QRESTSIHDM
NDKLENELAN KEAILRQMEE KNRQLQERLE LAEQKLQQTM RKAETLPEVE AELAQRIAAL
TKAEERHGNI EERMRHLEGQ LEEKNQELQR ARQREKMNEE HNKRLSDTVD RLLTESNERL
QLHLKERMAA LEEKNVLIQE SENFRKNLEE SLHDKVSLAE EIEKLRSELD QMKMRTGSLI
EPTISRTHID TSTELRYSVG SLVDSQSDYR TTKVIRRPRR GRMGVRRDEP KVKSLGDHEW
NRTQQIGVLG SHPFESDTEM SDIDDDDRET IFSSMDLLSP SGHSDAQTLA MMLQEQLDAI
NKEIRLIQEE KESTELRAEE IENRVASVSL EGLNLARVHP GTSITASVTA SSLASSSPPS
GHSTPKLTPR SPAREMDRMG VMTLPSDLRK HRRKIAVVEE DGREDKATIK CETSPPPTPR
AVRMTHTLPS SYHNDARSSL SASLEPDSLG LGSANSSQDS LHKAPKKKGI KSSIGRLFGK
KEKARLGQLR GFMETEAAAQ ESLGLGKLGT QAEKDRRLKK KHELLEEARR KGLPFAQWDG
PTVVAWLELW LGMPAWYVAA CRANVKSGAI MSALSDTEIQ REIGISNPLH RLKLRLAIQE
MVSLTSPSAP PTSRTPSGNV WVTHEEMENL TAPAKTKESE EGSWAQCPVF LQTLAYGDMN
HEWIGNEWLP SLGLPQYRSY FMECLVDARM LDHLTKKDLR VHLKMVDSFH RTSLQYGIMC
LKRLNYDRKE LERRREASQH EIKDVLVWSN DRVIRWIQAI GLREYANNIL ESGVHGSLIA
LDENFDYSSL ALLLQIPTQN TQARQILERE YNNLLALGTE RRLDESDDKN FRRGSTWRRQ
FPPREVHGIS MMPGSSETLP AGFRLTTTSG QSRKMTTDVA SSRLQRLDNS TVRTYSC
