LPXN_RABIT
ID LPXN_RABIT Reviewed; 386 AA.
AC Q9N261; G1TMN6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Leupaxin;
GN Name=LPXN;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12674328; DOI=10.1359/jbmr.2003.18.4.669;
RA Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y.,
RA Goldknopf J., Hruska K.A.;
RT "Leupaxin is a critical adaptor protein in the adhesion zone of the
RT osteoclast.";
RL J. Bone Miner. Res. 18:669-685(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke;
RG The Genome Sequencing Platform;
RA Di Palma F., Heiman D., Young S., Gnerre S., Johnson J., Lander E.S.,
RA Lindblad-Toh K.;
RT "Genome Sequence of Oryctolagus cuniculus (European rabbit).";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional coactivator for androgen receptor (AR) and
CC serum response factor (SRF). Contributes to the regulation of cell
CC adhesion, spreading and cell migration and acts as a negative regulator
CC in integrin-mediated cell adhesion events. Suppresses the integrin-
CC induced tyrosine phosphorylation of paxillin (PXN). May play a critical
CC role as an adapter protein in the formation of the adhesion zone in
CC osteoclasts. Negatively regulates B-cell antigen receptor (BCR)
CC signaling (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with unphosphorylated ITGA4. Interacts with AR and
CC SRF (By similarity). Interacts with PTK2B/PYK2, PTPN22 and PTPN12.
CC Interacts (via LD motif 3) with LYN and the interaction is induced upon
CC B-cell antigen receptor (BCR) activation. Interacts (via LD motif 3)
CC with PTK2/FAK (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, focal
CC adhesion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Cell projection, podosome {ECO:0000250}. Cell
CC membrane {ECO:0000250}. Note=Shuttles between the cytoplasm and
CC nucleus. Recruited to the cell membrane following B-cell antigen
CC receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase
CC activity (PTK2/FAK) attenuates its nuclear accumulation and limits its
CC ability to enhance serum response factor (SRF)-dependent gene
CC transcription. Targeting to focal adhesions is essential for its
CC tyrosine phosphorylation in response to bombesin (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The LIM domain 3 is critical for focal adhesion targeting and
CC the suppression of paxillin (PXN) tyrosine phosphorylation. The LIM
CC domain 3 alone or both LIM domains 3 and 4 can mediate interaction with
CC AR (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues. Phosphorylation on Tyr-72 is
CC important for its inhibitory function. Bombesin stimulates
CC phosphorylation on Tyr-22, Tyr-62 and Tyr-72 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paxillin family. {ECO:0000305}.
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DR EMBL; AF118146; AAF37382.1; -; mRNA.
DR EMBL; AAGW02038189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02038193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001075517.1; NM_001082048.1.
DR AlphaFoldDB; Q9N261; -.
DR SMR; Q9N261; -.
DR STRING; 9986.ENSOCUP00000021842; -.
DR PRIDE; Q9N261; -.
DR GeneID; 100008712; -.
DR KEGG; ocu:100008712; -.
DR CTD; 9404; -.
DR eggNOG; KOG1703; Eukaryota.
DR InParanoid; Q9N261; -.
DR OrthoDB; 1593918at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR017305; Tgfb1i1/Leupaxin/TGFB1I1.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 4.
DR PIRSF; PIRSF037881; Leupaxin; 1.
DR SMART; SM00132; LIM; 4.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Cytoplasm; LIM domain; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..386
FT /note="Leupaxin"
FT /id="PRO_0000416038"
FT DOMAIN 150..209
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 210..267
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 268..327
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 328..386
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 12..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..15
FT /note="LD motif 1"
FT MOTIF 70..82
FT /note="LD motif 2"
FT MOTIF 92..103
FT /note="LD motif 3"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60711"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60711"
FT MOD_RES 22
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60711"
FT MOD_RES 62
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60711"
FT MOD_RES 72
FT /note="Phosphotyrosine; by LYN"
FT /evidence="ECO:0000250|UniProtKB:O60711"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60711"
SQ SEQUENCE 386 AA; 43318 MW; 417C7E41FEEFCB08 CRC64;
MEELDALLEE LERSTLQDSD EYSNSAPLPL DQSSRKESNL DETSKMLSVQ DSTNPFPVQL
VYTTNIQDRN VYSEVQEPKK SPPPAKTSAA AQLDELMAHL SEMQAKVSVK ADAGKKPVSE
NLDHKASLDS MLGGLEQELQ NLGIPTVPKG HCASCQKPIV GKVIHALGQS WHPEHFICTH
CKEEIGSSPF FERSGLAYCP KDYHHLFSPR CAYCAAPILD KVLTAMNQTW HPEHFFCSHC
GEVFGTEGFH EKDKKPYCRK DFLAMFSPKC GGCNRPVLEN YLSAMNTVWH PECFVCGDCF
SSFSTGSFFE LEGRPFCELH YHQRRGTLCH GCGQPITGRC ISAMGHKFHP EHFVCAFCLT
QLSKGVFREQ NDKTYCQPCF NKLFSL
