PAXI_RAT
ID PAXI_RAT Reviewed; 586 AA.
AC Q66H76;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Paxillin;
GN Name=Pxn;
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 TISSUE=Kidney;
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 INTERACTION WITH PARVA.
RX PubMed=11134073; DOI=10.1083/jcb.151.7.1435;
RA Nikolopoulos S.N., Turner C.E.;
RT "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and
RT actin and regulates cell adhesion.";
RL J. Cell Biol. 151:1435-1448(2000).
RN [3]
RP INTERACTION WITH TGFB1I1.
RX PubMed=16546139; DOI=10.1016/j.bbrc.2006.02.162;
RA Guignandon A., Boutahar N., Rattner A., Vico L., Lafage-Proust M.-H.;
RT "Cyclic strain promotes shuttling of PYK2/Hic-5 complex from focal contacts
RT in osteoblast-like cells.";
RL Biochem. Biophys. Res. Commun. 343:407-414(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-126; SER-130;
RP SER-143; SER-259; SER-287; SER-290; SER-327 AND SER-335, AND IDENTIFICATION
RP 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: Cytoskeletal protein involved in actin-membrane attachment at
CC sites of cell adhesion to the extracellular matrix (focal adhesion).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts in vitro with VCL/vinculin as well as to the SH3
CC domain of SRC and, when tyrosine phosphorylated, to the SH2 domain of
CC CRK (By similarity). Interacts with GIT1 (By similarity). Interacts
CC with NUDT16L1/SDOS (By similarity). Interacts with PTK2/FAK1 (By
CC similarity). Interacts with PTK2B/PYK2 (By similarity). Interacts with
CC ASAP2 (By similarity). Interacts with unphosphorylated ITGA4 (By
CC similarity). Interacts with RNF5 (By similarity). Interacts with PDCD10
CC (By similarity). Interacts with NEK3, the interaction is prolactin-
CC dependent (By similarity). Interacts with PTK6 (By similarity).
CC Interacts with TGFB1I1 (PubMed:16546139). Interacts with SORBS1 (By
CC similarity). Interacts with PARVB (By similarity). Interacts (via LD
CC motif 4) with PARVA/PARVIN (PubMed:11134073). Interacts (via LD motif
CC 4) with ILK (By similarity). Interacts (via cytoplasmic domain) with
CC CEACAM1; the interaction is phosphotyrosyl-dependent (By similarity).
CC Interacts with LIMA1; this complex stabilizes actin dynamics (By
CC similarity). Interacts with CD36 (via C-terminus) (By similarity).
CC {ECO:0000250|UniProtKB:P49023, ECO:0000250|UniProtKB:Q8VI36,
CC ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:16546139}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P49023}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:P49023}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q8VI36}. Note=Colocalizes with integrins at the
CC cell periphery. Colocalizes with PXN to membrane ruffles and the
CC leading edge of migrating cells (By similarity).
CC {ECO:0000250|UniProtKB:P49023}.
CC -!- PTM: Phosphorylated by MAPK1/ERK2 (By similarity). Phosphorylated on
CC tyrosine residues during integrin-mediated cell adhesion, embryonic
CC development, fibroblast transformation and following stimulation of
CC cells by mitogens. Phosphorylation at Ser-273 by CDK5 reduces its
CC interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during
CC oligodendrocytes (OLs) differentiation (By similarity). Phosphorylation
CC at Tyr-31 and Tyr-118 by PTK6 promote the activation of RAC1 via
CC CRK/CrKII, thereby promoting migration and invasion (By similarity).
CC Phosphorylation at Ser-279 by SLK is required for PXN redistribution
CC and cell motility (By similarity). {ECO:0000250|UniProtKB:P49023}.
CC -!- SIMILARITY: Belongs to the paxillin family. {ECO:0000305}.
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DR EMBL; BC081984; AAH81984.1; -; mRNA.
DR RefSeq; NP_001012147.1; NM_001012147.1.
DR AlphaFoldDB; Q66H76; -.
DR SMR; Q66H76; -.
DR BioGRID; 262228; 4.
DR DIP; DIP-48423N; -.
DR IntAct; Q66H76; 1.
DR STRING; 10116.ENSRNOP00000043928; -.
DR ChEMBL; CHEMBL5613; -.
DR iPTMnet; Q66H76; -.
DR PhosphoSitePlus; Q66H76; -.
DR jPOST; Q66H76; -.
DR PaxDb; Q66H76; -.
DR PRIDE; Q66H76; -.
DR GeneID; 360820; -.
DR KEGG; rno:360820; -.
DR CTD; 5829; -.
DR RGD; 1305759; Pxn.
DR VEuPathDB; HostDB:ENSRNOG00000001149; -.
DR eggNOG; KOG1703; Eukaryota.
DR InParanoid; Q66H76; -.
DR OrthoDB; 1593918at2759; -.
DR PhylomeDB; Q66H76; -.
DR Reactome; R-RNO-180292; GAB1 signalosome.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR Reactome; R-RNO-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-RNO-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR Reactome; R-RNO-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR PRO; PR:Q66H76; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001149; Expressed in lung and 19 other tissues.
DR ExpressionAtlas; Q66H76; baseline and differential.
DR Genevisible; Q66H76; RN.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0051435; F:BH4 domain binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; IPI:RGD.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038191; F:neuropilin binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0017166; F:vinculin binding; ISO:RGD.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISO:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:RGD.
DR GO; GO:0043542; P:endothelial cell migration; ISO:RGD.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:RGD.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:RGD.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:1901652; P:response to peptide; IPI:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR InterPro; IPR001904; Paxillin.
DR InterPro; IPR017305; Tgfb1i1/Leupaxin/TGFB1I1.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24216:SF11; PTHR24216:SF11; 4.
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 1: Evidence at protein level;
KW Acetylation; Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton;
KW LIM domain; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..586
FT /note="Paxillin"
FT /id="PRO_0000075856"
FT DOMAIN 353..403
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 412..462
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 471..521
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 530..580
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 13..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..310
FT /note="Required for binding to PARVA and ILK"
FT /evidence="ECO:0000250|UniProtKB:P49024"
FT REGION 309..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..15
FT /note="LD motif 1"
FT MOTIF 144..156
FT /note="LD motif 2"
FT MOTIF 245..257
FT /note="LD motif 3"
FT MOTIF 294..305
FT /note="LD motif 4"
FT MOTIF 328..340
FT /note="LD motif 5"
FT COMPBIAS 65..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 31
FT /note="Phosphotyrosine; by PTK6"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 88
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 118
FT /note="Phosphotyrosine; by PTK6"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 132
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 210
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 273
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
SQ SEQUENCE 586 AA; 64019 MW; D4B9477CC0B7BB7E CRC64;
MDDLDALLAD LESTTSHISK RPVFLSEEPP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG
TVLDPLDQWQ PSGSRYAHQQ PPSPSPIYSS STKNSSASNP QDSVGSLCSR AGEEEHVYSF
PNKQKSAEPS PTVMSSSLGS NLSELDRLLL ELNAVQRSPS GFSAGMVSVQ ASREPLGSWG
TEGRAIILSP FFQDEAESSP PLPGALSPLY GVPESNNLLG GKAGPLMKEK PKRNGGRGLE
DVRPSVESLL DELENSVPSP VPAITVNQGE MSSPQRVTSS QQQTRISASS ATRELDELMA
SLSDFKFMAQ GKTGSSSPPG GLSKPGSQLD SMLGSLQSDL NKLGVATVAK GVCGACKKPI
AGQVVTAMGK TWHPEHFVCT HCQEEIGSRN FFERDGQPYC EKDYHSLFSP RCYYCNGPIL
DKVVTALDRT WHPEHFFCAQ CGAFFGPEGF HEKDGKAYCR KDYFDMFAPK CGGCARAILE
NYISALNTLW HPECFVCREC FTPFVNGSFF EHDGQPYCEV HYHERRGSLC SGCQKPITGR
CITAMAKKFH PEHFVCAFCL KQLNKGTFKE QNDKPYCQSC FLKLFC
