LPP_RAT
ID LPP_RAT Reviewed; 632 AA.
AC Q5XI07;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Lipoma-preferred partner homolog;
GN Name=Lpp;
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 [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-152, 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 play a structural role at sites of cell adhesion in
CC maintaining cell shape and motility. In addition to these structural
CC functions, it may also be implicated in signaling events and activation
CC of gene transcription. May be involved in signal transduction from cell
CC adhesion sites to the nucleus allowing successful integration of
CC signals arising from soluble factors and cell-cell adhesion. Also
CC suggested to serve as a scaffold protein upon which distinct protein
CC complexes are assembled in the cytoplasm and in the nucleus (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PDZ domains of SCRIB, with VASP and with
CC ACTN1/alpha-actinin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell junction {ECO:0000250}. Note=Found in the nucleus, in the
CC cytoplasm and at cell adhesion sites. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR EMBL; BC083627; AAH83627.1; -; mRNA.
DR EMBL; BC083890; AAH83890.1; -; mRNA.
DR RefSeq; NP_001013886.1; NM_001013864.1.
DR RefSeq; XP_006248567.1; XM_006248505.3.
DR RefSeq; XP_017453399.1; XM_017597910.1.
DR RefSeq; XP_017453400.1; XM_017597911.1.
DR RefSeq; XP_017453401.1; XM_017597912.1.
DR RefSeq; XP_017453402.1; XM_017597913.1.
DR RefSeq; XP_017453403.1; XM_017597914.1.
DR RefSeq; XP_017453404.1; XM_017597915.1.
DR RefSeq; XP_017453405.1; XM_017597916.1.
DR RefSeq; XP_017453406.1; XM_017597917.1.
DR RefSeq; XP_017453407.1; XM_017597918.1.
DR AlphaFoldDB; Q5XI07; -.
DR SMR; Q5XI07; -.
DR STRING; 10116.ENSRNOP00000042917; -.
DR iPTMnet; Q5XI07; -.
DR PhosphoSitePlus; Q5XI07; -.
DR jPOST; Q5XI07; -.
DR PaxDb; Q5XI07; -.
DR PeptideAtlas; Q5XI07; -.
DR PRIDE; Q5XI07; -.
DR Ensembl; ENSRNOT00000113595; ENSRNOP00000090019; ENSRNOG00000031669.
DR GeneID; 288010; -.
DR KEGG; rno:288010; -.
DR UCSC; RGD:1310535; rat.
DR CTD; 4026; -.
DR RGD; 1310535; Lpp.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000156022; -.
DR HOGENOM; CLU_001357_10_0_1; -.
DR InParanoid; Q5XI07; -.
DR OMA; FNPYKQM; -.
DR OrthoDB; 483341at2759; -.
DR PhylomeDB; Q5XI07; -.
DR PRO; PR:Q5XI07; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000031669; Expressed in testis and 18 other tissues.
DR Genevisible; Q5XI07; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR InterPro; IPR028771; LPP.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24207:SF0; PTHR24207:SF0; 1.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cell adhesion; Cell junction; Cytoplasm;
KW Isopeptide bond; LIM domain; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc.
FT CHAIN 1..632
FT /note="Lipoma-preferred partner homolog"
FT /id="PRO_0000075834"
FT DOMAIN 434..493
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 494..554
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 555..623
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..96
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFW7"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 241
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFW7"
FT MOD_RES 246
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFW7"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q93052"
SQ SEQUENCE 632 AA; 68260 MW; 8539C27B5D7D02BC CRC64;
MSHPSWLPPR STGEPLGHVP ARMETTHSFG TPSISVSTQQ PPKKFAPVVA PKPKYNPYKQ
PGGEGDFLPP PPPPLEDPGT IPSGSGHFPP PPPLDEGAFI VQRGNPGGKT LEERRSSLDA
EIDSLTSILA DLECSSPYKP RAPPGSSSSI ASPPVSTPVT GHKRMVIPQQ PPLTATKKSA
TKPQAIPIPV TPIGTLKPQP QPVPASYSTA STSSRPAFNV QVKSAQPSTH YMTGSSSGQM
YGPGSRSYNT QQVPLSAQCP PPTTCAGTDY AYIPPSGQQA ESGFGYTSNQ GRYFEPFFAA
CPSYGGRNEA DPAYGQQVQP NTWKREPGYA APGAGNQNQP GMYSVSGPKK TYITDPVSAP
CAPPVQPKER LVKNQKVLQN VVDDRVHGLR KSGFPAPMGP PSVPPSFRPE DELEHLTKKM
LYDMENPPAD DYFGRCARCG ENVVGEGTGC TAMDQVFHVD CFTCMVCDIK LRGQPFYAVE
KKAYCEPCYI NTLEQCSVCS KPIMERILRA TGKAYHPHCF TCVMCHRSLD GIPFTVDACG
LIHCIEDFHK KFAPRCSVCK EPIMPAPGQE ETVRIVALDR DFHVHCYRCE DCGGLLSEGD
NQGCYPLDGH ILCKSCNSAR IRVLTAKAST DL
