ID A0A2I3HWJ0_NOMLE Unreviewed; 1078 AA.
AC A0A2I3HWJ0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Paxillin {ECO:0000256|ARBA:ARBA00023808};
GN Name=PXN {ECO:0000313|Ensembl:ENSNLEP00000047920.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000047920.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000047920.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000047920.1}
RP IDENTIFICATION.
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; A0A2I3HWJ0; -.
DR STRING; 61853.ENSNLEP00000047920; -.
DR Ensembl; ENSNLET00000051941.1; ENSNLEP00000047920.1; ENSNLEG00000007512.3.
DR GeneTree; ENSGT00940000158897; -.
DR InParanoid; A0A2I3HWJ0; -.
DR OMA; SRAPPCH; -.
DR Proteomes; UP000001073; 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:UP000001073};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 843..902
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 903..960
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 961..1020
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1021..1078
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1078 AA; 115471 MW; 671EC93147D3168E CRC64;
DALLADLEST TSHISKRPVF LSEETPYSYP TGNHTYQEIA VPPPVPPPPS SEALNGTILD
PLDQWQPSGS RFIHQQPQSS SPVYGSSAKT SSVSNPQDGV GSPCSRVGEE EHVYSFPNKQ
KSAEPSPTVM STSLGSNLSE LDRLLLELNA VQHNPPGFPA DEANSSPPLP GALSPHYGVP
ETNSPLGGKA GPLTKEKPKR NGGRGLEDVR PSVESLLDEL ESSVPSPVPA ITVNQGEMSS
PQRVTSTQQQ TRISASSATR ELDELMASLS DFKTSSSTVA LSAPGLLSSS APSSYCSLPP
SPPPMPSVFL PLTTTPSPRG QGHTPEFPCT EQSGRGLLPP VAPSWLDLAG LGVMPDTLNS
RSPSVEGSLW AVGTESQGRD WRHLPTITSE LSGAPRCHTV PCAGSIALQE PGEPQGPPAS
PSCPEEALAA TWERPWASEV FRPERMPPSG AARSFQEVAE PAVVAVDQQA IFPDTWTLTE
EHGLQQERPR PEPGRLGSSS PASVTMEQLG AKMTERGSVA RPTQGPETPR SPEGTTEAAT
QAGKEQPELP CAMAMGTPST TERISTSGQI RSVIRRSQET GHAHPMSREP SPRRRLDPAT
LSRTPSQEQL IAELQGRLGI QPEAEEPAEA AGPSAQDWLT EGIIITVQPR GKRAGGQLIE
KVVFPPGSPI PLRRTISVLA SPSVPLLQHR TDAAASSSSP LPSLLASSPL GLSAYTCGSS
GVQSAGEEPH DEGVQGPALP TPAPHTMRSV GCQTDEDPLL PPMQIQGLEQ RADGERCWAA
GWPRDGGQSS PGGQDEGGFM AQGKTGSSSP PGGPPKPGSQ LDSMLGSLQS DLNKLGVATV
AKGVCGACKK PIAGQVVTAM GKTWHPEHFV CTHCQEEIGS RNFFERDGQP YCEKDYHNLF
SPRCYYCNGP ILDKVVTALD RTWHPEHFFC AQCGAFFGPE GFHEKDGKAY CRKDYFDMFA
PKCGGCARAI LENYISALNT LWHPECFVCR ECFTPFVNGS FFEHDGQPYC EVHYHERRGS
LCSGCQKPIT GRCITAMAKK FHPEHFVCAF CLKQLNKGTF KEQNDKPYCQ NCFLKLFC
//