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Database: UniProt
Entry: A0A1U7QTV2_MESAU
LinkDB: A0A1U7QTV2_MESAU
Original site: A0A1U7QTV2_MESAU 
ID   A0A1U7QTV2_MESAU        Unreviewed;       589 AA.
AC   A0A1U7QTV2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Paxillin {ECO:0000256|ARBA:ARBA00023808};
GN   Name=Pxn {ECO:0000313|RefSeq:XP_005079036.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005079036.1};
RN   [1] {ECO:0000313|RefSeq:XP_005079036.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28071753;
RA   McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT   "De novo assembly, annotation, and characterization of the whole brain
RT   transcriptome of male and female Syrian hamsters.";
RL   Sci. Rep. 7:40472-40472(2017).
RN   [2] {ECO:0000313|RefSeq:XP_005079036.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the paxillin family.
CC       {ECO:0000256|ARBA:ARBA00005813}.
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DR   RefSeq; XP_005079036.1; XM_005078979.3.
DR   AlphaFoldDB; A0A1U7QTV2; -.
DR   STRING; 10036.ENSMAUP00000013577; -.
DR   eggNOG; KOG1703; Eukaryota.
DR   OrthoDB; 370973at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd09336; LIM1_Paxillin_like; 1.
DR   CDD; cd09407; LIM2_Paxillin; 1.
DR   CDD; cd09338; LIM3_Paxillin_like; 1.
DR   CDD; cd09411; LIM4_Paxillin; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR   InterPro; IPR047072; Paxillin_Lim_dom2.
DR   InterPro; IPR001904; Paxillin_Lim_dom4.
DR   InterPro; IPR047075; Paxillin_TGFB1I1_LIM_dom1.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24216:SF11; PAXILLIN; 1.
DR   PANTHER; PTHR24216; PAXILLIN-RELATED; 1.
DR   Pfam; PF00412; LIM; 4.
DR   Pfam; PF03535; Paxillin; 1.
DR   PRINTS; PR00832; PAXILLIN.
DR   SMART; SM00132; LIM; 4.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 5.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE   3: Inferred from homology;
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          354..413
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          414..471
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          472..531
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          532..589
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   REGION          13..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   589 AA;  64402 MW;  AF3B1D2886FACAEC CRC64;
     MDDLDALLAD LESTTSHISK RPVFLSEEPP YSYPTGNHTY QETVVPPPVP PPPSSEALNG
     TILDPLEEWQ PTGSRYTHQQ PPSPSPVYGA SAKTSSASNP LDGALCSRAG EEEHVYSFPN
     KQKSAEPSPT VMSSSLGSNL SELDRLLLEL NAVQHNPSGF PADEADTSPP LPGALTPLYG
     VPENNSSLGG KPGPLVKEKP KRNGSRGLED VRPSVESLLD ELESSVPSPV PAITVNQGEM
     SSPQRVTSSQ QQTRISASSA TRELDELMAS LSDFKMHGLE QRVDGERQWA AGWPPSSRQS
     SPEGQDEGGF MAQGKTGSSP PPGGLSKPGS QLDSMLGSLQ SDLNKLGVAT VAKGVCGACK
     KPIAGQVVTA MGKTWHPEHF VCTHCQEEIG SRNFFERDGQ PYCEKDYHSL FSPRCYYCNG
     PILDKVVTAL DRTWHPEHFF CAQCGAFFGP EGFHEKDGKA YCRKDYFDMF APKCGGCARA
     ILENYISALN TLWHPECFVC RECFTPFVNG SFFEHDGQPY CEVHYHERRG SLCSGCQKPI
     TGRCITAMAK KFHPEHFVCA FCLKQLNKGT FKEQNDKPYC QSCFLKLFC
//
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