PAXI_CHICK
ID PAXI_CHICK Reviewed; 559 AA.
AC P49024;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Paxillin;
GN Name=PXN;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7534286; DOI=10.1074/jbc.270.10.5039;
RA Salgia R., Li J.-L., Lo S.H., Brunkhorst B., Kansas G.S., Sobhany E.S.,
RA Sun Y., Pisick E., Hallek M., Ernst T., Tantravahi R., Chen L.B.,
RA Griffin J.D.;
RT "Molecular cloning of human paxillin, a focal adhesion protein
RT phosphorylated by P210BCR/ABL.";
RL J. Biol. Chem. 270:5039-5047(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=7525621; DOI=10.1242/jcs.107.6.1583;
RA Turner C.E., Miller J.T.;
RT "Primary sequence of paxillin contains putative SH2 and SH3 domain binding
RT motifs and multiple LIM domains: identification of a vinculin and pp125Fak-
RT binding region.";
RL J. Cell Sci. 107:1583-1591(1994).
RN [3]
RP PHOSPHORYLATION AT TYR-118.
RX PubMed=7615549; DOI=10.1074/jbc.270.29.17437;
RA Bellis S.L., Miller J.T., Turner C.E.;
RT "Characterization of tyrosine phosphorylation of paxillin in vitro by focal
RT adhesion kinase.";
RL J. Biol. Chem. 270:17437-17441(1995).
RN [4]
RP INTERACTION WITH PARVA AND ILK.
RX PubMed=15817463; DOI=10.1074/jbc.m500752200;
RA LaLonde D.P., Brown M.C., Bouverat B.P., Turner C.E.;
RT "Actopaxin interacts with TESK1 to regulate cell spreading on
RT fibronectin.";
RL J. Biol. Chem. 280:21680-21688(2005).
CC -!- FUNCTION: Cytoskeletal protein involved in actin-membrane attachment at
CC sites of cell adhesion to the extracellular matrix (focal adhesion).
CC Binds in vitro to vinculin as well as to the SH3 domain of c-SRC and,
CC when tyrosine phosphorylated, to the SH2 domain of v-CRK.
CC -!- SUBUNIT: Interacts (via LD motif 4) with PARVA/PARVIN and ILK.
CC {ECO:0000269|PubMed:15817463}.
CC -!- INTERACTION:
CC P49024; Q00944: PTK2; NbExp=2; IntAct=EBI-2896280, EBI-2896409;
CC P49024; P12003: VCL; NbExp=5; IntAct=EBI-2896280, EBI-1039563;
CC P49024; P12003-1: VCL; NbExp=2; IntAct=EBI-2896280, EBI-6138078;
CC P49024; P12003-2: VCL; NbExp=2; IntAct=EBI-2896280, EBI-6138096;
CC P49024; P03126: E6; Xeno; NbExp=2; IntAct=EBI-2896280, EBI-1177242;
CC P49024; P06931: E6; Xeno; NbExp=5; IntAct=EBI-2896280, EBI-7281937;
CC P49024; Q9Y2X7: GIT1; Xeno; NbExp=3; IntAct=EBI-2896280, EBI-466061;
CC P49024; Q64727: Vcl; Xeno; NbExp=4; IntAct=EBI-2896280, EBI-432047;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:7525621}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:7525621}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q8VI36}.
CC -!- PTM: Phosphorylated on tyrosine residues during integrin-mediated cell
CC adhesion, embryonic development, fibroblast transformation and
CC following stimulation of cells by mitogens.
CC {ECO:0000269|PubMed:7615549}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U14589; AAC59665.1; -; mRNA.
DR EMBL; L30099; AAC38018.1; -; mRNA.
DR PIR; B55933; B55933.
DR RefSeq; NP_990315.1; NM_204984.1.
DR PDB; 2L6F; NMR; -; A=140-161, A=262-275.
DR PDB; 2L6G; NMR; -; A=140-161.
DR PDB; 2L6H; NMR; -; A=263-276.
DR PDB; 4R32; X-ray; 3.50 A; B/C=139-162.
DR PDBsum; 2L6F; -.
DR PDBsum; 2L6G; -.
DR PDBsum; 2L6H; -.
DR PDBsum; 4R32; -.
DR AlphaFoldDB; P49024; -.
DR SMR; P49024; -.
DR BioGRID; 676106; 4.
DR ELM; P49024; -.
DR IntAct; P49024; 13.
DR MINT; P49024; -.
DR STRING; 9031.ENSGALP00000011713; -.
DR iPTMnet; P49024; -.
DR PaxDb; P49024; -.
DR GeneID; 395832; -.
DR KEGG; gga:395832; -.
DR CTD; 5829; -.
DR VEuPathDB; HostDB:geneid_395832; -.
DR eggNOG; KOG1703; Eukaryota.
DR InParanoid; P49024; -.
DR OrthoDB; 1593918at2759; -.
DR PhylomeDB; P49024; -.
DR PRO; PR:P49024; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR GO; GO:0001725; C:stress fiber; IDA:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0017166; F:vinculin binding; IPI:AgBase.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0043542; P:endothelial cell migration; IBA:GO_Central.
DR GO; GO:0035994; P:response to muscle stretch; IDA:AgBase.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR InterPro; IPR001904; Paxillin.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24216:SF11; PTHR24216:SF11; 4.
DR Pfam; PF00412; LIM; 4.
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 3D-structure; Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton;
KW LIM domain; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..559
FT /note="Paxillin"
FT /id="PRO_0000075857"
FT DOMAIN 326..376
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 385..435
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 444..494
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 503..553
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 17..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..282
FT /note="Required for binding to PARVA and ILK"
FT /evidence="ECO:0000269|PubMed:15817463"
FT REGION 281..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..15
FT /note="LD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOTIF 144..156
FT /note="LD motif 2"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOTIF 217..229
FT /note="LD motif 3"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOTIF 266..277
FT /note="LD motif 4"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOTIF 301..313
FT /note="LD motif 5"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT COMPBIAS 65..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 118
FT /note="Phosphotyrosine; by FAK1"
FT /evidence="ECO:0000269|PubMed:7615549"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:2L6F"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:2L6H"
SQ SEQUENCE 559 AA; 61243 MW; 6450270D90B2DE84 CRC64;
MDDLDALLAD LESTTSHISK RPVFLTEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG
TVIDPLDQWQ PSVSRYGHQQ PQSQSPIYSS SAKSSSASVP RDGLSSPSPR ASEEEHVYSF
PNKQKSAEPS PTMTSTSLGS NLSELDRLLL ELNAVQHNPP SGFSADEVSR SPSLPNVTGP
HYVIPESSSS AGGKAAPPTK EKPKRNGGRG IEDVRPSVES LLDELESSVP SPVPAITVSQ
GEVSSPQRVN ASQQQTRISA SSATRELDEL MASLSDFKFM AQGKAGGSSS PPSTTPKPGS
QLDTMLGSLQ SDLNKLGVAT VAKGVCGACK KPIAGQVVTA MGKTWHPEHF VCTHCQEEIG
SRNFFERDGQ PYCEKDYHNL FSPRCYYCNG PILDKVVTAL DRTWHPEHFF CAQCGVFFGP
EGFHEKDGKA YCRKDYFDMF APKCGGCARA ILENYISALN TLWHPECFVC RECFTPFING
SFFEHDGQPY CEVHYHERRG SLCSGCQKPI TGRCITAMGK KFHPEHFVCA FCLKQLNKGT
FKEQNDKPYC QNCFLKLFC
