ID A0A3Q1M1X1_BOVIN Unreviewed; 556 AA.
AC A0A3Q1M1X1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Paxillin {ECO:0000256|ARBA:ARBA00023808};
GN Name=PXN {ECO:0000313|Ensembl:ENSBTAP00000067366.1,
GN ECO:0000313|VGNC:VGNC:107261};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000067366.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000067366.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000067366.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000067366.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000067366.1};
RG Ensembl;
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 AlphaFoldDB; A0A3Q1M1X1; -.
DR SMR; A0A3Q1M1X1; -.
DR Ensembl; ENSBTAT00000072658.1; ENSBTAP00000067366.1; ENSBTAG00000018108.6.
DR VEuPathDB; HostDB:ENSBTAG00000018108; -.
DR VGNC; VGNC:107261; PXN.
DR GeneTree; ENSGT00940000158897; -.
DR OMA; FKFMSQG; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000018108; Expressed in neutrophil and 104 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1M1X1; baseline and differential.
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:UniProt.
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; cd09409; LIM3_Paxillin; 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 1: Evidence at protein level;
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};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A3Q1M1X1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 321..380
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 381..438
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 439..498
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 499..556
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..101
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 196..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 60768 MW; FDF3DCC1EF2D9AB2 CRC64;
MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPVPP PPSSEALNGS
VLDPLDPWPP STSRFTHQQP QSSSPVYGSS AKTSSASNPQ DGGGPPCPRA GEEDHVYSFP
NKQKSAEPSP TVMSSSLGSN LSELDRLLLE LNAVQHNPPG FPADEANSSP PLPGPLSTHY
GVPENNSLLG GKAGALTKEK PKRNGGRGLE DLRPSVENLL DELESSVPSP VPTITVNQGE
MSSPQRVTSS QQQTRISASS ATRELDELMA SLSDFKFMAQ GKTGSSSPPG GPPKPGSQLD
SMLGSLQSDL NKLGVATVAK GVCGACKKPI AGQVVTAMGK TWHPEHFVCT HCQEEIGSRN
FFERDGQPYC EKDYHNLFSP RCYYCNGPIL DKVVTALDRT WHPEHFFCAQ CGAFFGPEGF
HEKDGKAYCR KDYFDMFAPK CGGCARAILE NYISALNTLW HPECFVCREC FTPFVHGSFF
EHEGQPYCEA HYHERRGSLC SGCQKPITGR CITAMAKKFH PEHFVCAFCL KQLNKGTFKE
QNDKPYCQNC FLKLFC
//