PAXI_PONAB
ID PAXI_PONAB Reviewed; 591 AA.
AC Q5R7I1;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Paxillin;
GN Name=PXN;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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: Binds to vinculin and to the SH3 domain of SRC. Interacts with
CC GIT1, NUDT16L1/SDOS, PARVA, PARVB, SORBS1 and TGFB1I1. Component of
CC cytoplasmic complexes, which also contain GIT1, ARHGEF6 and PAK1. Binds
CC ASAP2. Interacts with RNF5 and PDCD10 (By similarity). Interacts with
CC NEK3 and this interaction is prolactin-dependent (By similarity).
CC Interacts with PTK2/FAK1 and PTK2B/PYK2 (By similarity). Interacts with
CC PTK6 (By similarity). Interacts with CD36. Interacts (via cytoplasmic
CC domain) with CEACAM1; the interaction is phosphotyrosyl-dependent (By
CC similarity). Interacts with PXN; this complex stabilizes actin dynamics
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P49023}.
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-244 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-250 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; CR860135; CAH92279.1; -; mRNA.
DR RefSeq; NP_001126332.1; NM_001132860.1.
DR AlphaFoldDB; Q5R7I1; -.
DR SMR; Q5R7I1; -.
DR GeneID; 100173313; -.
DR KEGG; pon:100173313; -.
DR CTD; 5829; -.
DR eggNOG; KOG1703; Eukaryota.
DR InParanoid; Q5R7I1; -.
DR OrthoDB; 1593918at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton;
KW LIM domain; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..591
FT /note="Paxillin"
FT /id="PRO_0000075855"
FT DOMAIN 356..415
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 416..473
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 474..533
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 534..591
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 17..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..335
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 216..228
FT /note="LD motif 3"
FT MOTIF 265..276
FT /note="LD motif 4"
FT MOTIF 333..345
FT /note="LD motif 5"
FT COMPBIAS 65..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
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:0000250|UniProtKB:Q8VI36"
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:0000250|UniProtKB:P49023"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
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:0000250|UniProtKB:P49023"
FT MOD_RES 181
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H76"
FT MOD_RES 244
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H76"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H76"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H76"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI36"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49023"
SQ SEQUENCE 591 AA; 64515 MW; C96D79C454092054 CRC64;
MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG
TILDPLDQWQ PSGSRFIHQQ PQSSSPVYGS SAKTSSVSNP QDGVGSPCSR VGEEEHVYSF
PNKQKSAESS PTVMSTSLGS NLSELDRLLL ELNAVQHNPP GFPADEANSG PPLPGALSPH
YGVPETNSPL GGKAGPLTKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG
EMSSPQRVTS TQQQTRISAS SATRELDELM ASLSDFRIQG LEQRADGERC WAADWPRDGG
RSSPGGQDEG GFMAQGKTGS SSPPGGPPKP GSQLDSMLGS LQSDLNKLGV ATVAKGVCGA
CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD GQPYCEKDYH NLFSPRCYYC
NGPILDKVVT ALDRTWHPEH FFCAQCGAFF GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA
RAILENYISA LNTLWHPECF VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK
PITGRCITAM AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQNCFLKLF C
