LIPA4_RAT
ID LIPA4_RAT Reviewed; 1043 AA.
AC Q91Z80;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Liprin-alpha-4;
DE AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-4;
DE Short=PTPRF-interacting protein alpha-4;
DE Flags: Fragment;
GN Name=Ppfia4;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Mukherjee K., Wang Y., Suedhof T.C.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH RIMS1 AND RIMS2.
RC TISSUE=Brain;
RX PubMed=11797009; DOI=10.1038/415321a;
RA Schoch S., Castillo P.E., Jo T., Mukherjee K., Geppert M., Wang Y.,
RA Schmitz F., Malenka R.C., Suedhof T.C.;
RT "RIM1alpha forms a protein scaffold for regulating neurotransmitter release
RT at the active zone.";
RL Nature 415:321-326(2002).
RN [3]
RP INTERACTION WITH GRIP1.
RX PubMed=11931740; DOI=10.1016/s0896-6273(02)00640-2;
RA Wyszynski M., Kim E., Dunah A.W., Passafaro M., Valtschanoff J.G.,
RA Serra-Pages C., Streuli M., Weinberg R.J., Sheng M.;
RT "Interaction between GRIP and liprin-alpha/SYD2 is required for AMPA
RT receptor targeting.";
RL Neuron 34:39-52(2002).
RN [4]
RP INTERACTION WITH GIT1 AND GIT2.
RX PubMed=12629171; DOI=10.1523/jneurosci.23-05-01667.2003;
RA Ko J., Kim S., Valtschanoff J.G., Shin H., Lee J.R., Sheng M.,
RA Premont R.T., Weinberg R.J., Kim E.;
RT "Interaction between liprin-alpha and GIT1 is required for AMPA receptor
RT targeting.";
RL J. Neurosci. 23:1667-1677(2003).
RN [5]
RP INTERACTION WITH KIF1A.
RX PubMed=12522103; DOI=10.1074/jbc.m211874200;
RA Shin H., Wyszynski M., Huh K.H., Valtschanoff J.G., Lee J.R., Ko J.,
RA Streuli M., Weinberg R.J., Sheng M., Kim E.;
RT "Association of the kinesin motor KIF1A with the multimodular protein
RT liprin-alpha.";
RL J. Biol. Chem. 278:11393-11401(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500 AND SER-541, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By
CC similarity). {ECO:0000250}.
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 RIMS1 and RIMS2 (PubMed:11797009). Interacts
CC with GIT1 and GIT2 (PubMed:12629171). Interacts with GRIP1
CC (PubMed:11931740). Interacts with KIF1A (PubMed:12522103).
CC {ECO:0000269|PubMed:11797009, ECO:0000269|PubMed:11931740,
CC ECO:0000269|PubMed:12522103, ECO:0000269|PubMed:12629171}.
CC -!- INTERACTION:
CC Q91Z80; P19491: Gria2; NbExp=3; IntAct=EBI-8276907, EBI-77718;
CC Q91Z80; P97879: Grip1; NbExp=7; IntAct=EBI-8276907, EBI-936113;
CC Q91Z80; Q9WUL3: RPTPK; NbExp=2; IntAct=EBI-8276907, EBI-8277319;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell surface
CC {ECO:0000250}. Note=Colocalizes with PTPRF at the cell surface.
CC {ECO:0000250}.
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). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC {ECO:0000305}.
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DR EMBL; AY057064; AAL23695.1; -; mRNA.
DR RefSeq; NP_536334.1; NM_080409.1.
DR AlphaFoldDB; Q91Z80; -.
DR SMR; Q91Z80; -.
DR CORUM; Q91Z80; -.
DR IntAct; Q91Z80; 4.
DR MINT; Q91Z80; -.
DR STRING; 10116.ENSRNOP00000033209; -.
DR iPTMnet; Q91Z80; -.
DR PhosphoSitePlus; Q91Z80; -.
DR SwissPalm; Q91Z80; -.
DR PaxDb; Q91Z80; -.
DR PRIDE; Q91Z80; -.
DR GeneID; 140592; -.
DR KEGG; rno:140592; -.
DR UCSC; RGD:620055; rat.
DR CTD; 8497; -.
DR RGD; 620055; Ppfia4.
DR eggNOG; KOG0249; Eukaryota.
DR InParanoid; Q91Z80; -.
DR OrthoDB; 440941at2759; -.
DR PhylomeDB; Q91Z80; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-388844; Receptor-type tyrosine-protein phosphatases.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; ISS:ParkinsonsUK-UCL.
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; IPR030439; PPFIA4.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; PTHR12587; 1.
DR PANTHER; PTHR12587:SF5; PTHR12587:SF5; 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 Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN <1..1043
FT /note="Liprin-alpha-4"
FT /id="PRO_0000191033"
FT DOMAIN 688..754
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 803..867
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 891..960
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 498..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 24..332
FT /evidence="ECO:0000255"
FT COILED 426..470
FT /evidence="ECO:0000255"
FT COILED 864..890
FT /evidence="ECO:0000255"
FT COMPBIAS 498..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT NON_TER 1
SQ SEQUENCE 1043 AA; 118004 MW; C7C119B83EDA5C88 CRC64;
DVSSEVEVLK ALKSLFEHHK ALDEKVRERL RAALERVTTL EEQLAGAHQQ VSALQQGAGI
RDGVAEEEET VDLGPKRLWK DDTGRVEELQ GLLEKQNYEL SQARERLVTL SATVTELEED
LGTARRDLIK SEELSGKHQR DLREALAQKE DMEERITTLE KRYLAAQREA TSIHDLNDKL
ENELANKESL HRQCEEKARH LQELLEVAEQ KLQQTMRKAE TLPEVEAELS QRIAALTKAE
ERHGNIEEHL RQLEGQLEEK NQELARVRQR EKMNEDHNKR LSDTVDRLLS ESNERLQLHL
KERMAALEEK GRLSEEIEKL RQEVDQLKGR GGPFVDGIHS RSHVGSTTDV RFSLSTAAHV
PPGLHRRYTA LREESAKDWK PAPLPGVLAA TTTPALTVTL RSPMWTRMSL GAWWALRLMS
SHLVAILDAQ TLAMMLQEQL DAINQEIRMI QEEKESTELR AEEIETRVTS GSMEALNLTQ
LRKRGSIPTS LTALSLASAS PPLSGRSTPK LTSRSAAQDL DRMGVMTLPS DLRKHRRKLL
SPVSREENRE DKATIKCETS PPSSPRTLRL EKLGHPTLSQ EEGKSALEGQ DSNPSSSNSS
QDSLHKGAKR KGIKSSIGRL FGKKEKGRLI HLSRDATGHV LLTDSELSLQ EPMVPAKLGT
QAEKDRRLKK KHQLLEDARR KGMPFAQWDG PTVVSWLELW VGMPAWYVAA CRANVKSGAI
MSALSDTEIQ REIGISNALH RLKLRLAIQE MVSLTSPSAP PTSRTSSGNV WVTHEEMETL
ATSTKTDSEE GSWAQTLAYG DMNHEWIGNE WLPSLGLPQY RSYFMECLVD ARMLDHLTKK
DLRVHLKMVD SFHRTSLQYG IMCLKRLNYD RKELEKRREE SQHEIKDVLV WTNDQVVHWV
QSIGLRDYAG NLHESGVHGA LLALDENFDH NTLALVLQIP TQNTQARQVM EREFNNLLAL
GTDRKLDDGE EKVFRRAPSW RKRFRPRDHH SGGMLGTSAE TLPAGFRVST LGPLQPPPAP
PNKIMPEAHS HYLYGHMLSA FRD
