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Database: UniProt
Entry: A0A091FMJ2_9AVES
LinkDB: A0A091FMJ2_9AVES
Original site: A0A091FMJ2_9AVES 
ID   A0A091FMJ2_9AVES        Unreviewed;       598 AA.
AC   A0A091FMJ2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Paxillin {ECO:0000256|ARBA:ARBA00023808};
DE   Flags: Fragment;
GN   ORFNames=N303_09727 {ECO:0000313|EMBL:KFO70359.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO70359.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO70359.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO70359.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC       {ECO:0000256|ARBA:ARBA00004246}. 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, ECO:0000256|PIRNR:PIRNR037881}.
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DR   EMBL; KL447166; KFO70359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091FMJ2; -.
DR   STRING; 55661.A0A091FMJ2; -.
DR   Proteomes; UP000053760; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR   GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR   GO; GO:0001725; C:stress fiber; ISS:AgBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017166; F:vinculin binding; ISS:AgBase.
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; IPR017305; Tgfb1i1/Leupaxin/TGFB1I1.
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   PIRSF; PIRSF037881; Leupaxin; 2.
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   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PIRNR:PIRNR037881};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          363..422
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          423..480
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          481..540
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          541..598
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   REGION          1..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..257
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..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO70359.1"
FT   NON_TER         598
FT                   /evidence="ECO:0000313|EMBL:KFO70359.1"
SQ   SEQUENCE   598 AA;  65650 MW;  06D36DB523F34824 CRC64;
     DALLADLEST TSHISKRPVF LTEETPYSYP TGNHTYQEIA VPPPVPPPPS NEALNGTVID
     PLDQWQPSVS RYTHQQPQSQ SPIYSSSAKS SSASIPRDGL SSPSPRASEE EHVYSFPNKQ
     KSAEPSPTMT SSSLGSNLSE LDRLLLELNA VQHNPAGGFP ADEASRSPSL PSLTGPHYVV
     PEGSSSVGGK AAPPTKEKPK RNGARGIEDV RPSVESLLDE LESSVPSPVP AITVSQGEVS
     SPQRVTASQQ QTRISASSAT RELDELMASL SDFKVPYHHN LMLCLFPPHS CPWFFLLNPH
     SPQGGRTCLT VFVFSSLQFM AQGKAGSSSP PSTASKPGSQ LDTMLGSLQS DLNKLGVATV
     AKGVCGACKK PIAGQVVTAM GKTWHPEHFV CTHCQEEIGS RNFFERDGQP YCEKDYHNLF
     SPRCYYCNGP ILDKVVTALD RTWHPEHFFC AQCGAFFGPE GFHEKDGKAY CRKDYFDMFA
     PKCGGCARAI LENYISALNT LWHPECFVCR ECFTPFVNGS FFEHDGQPYC EVHYHERRGS
     LCSGCQKPIT GRCITAMGKK FHPEHFVCAF CLKQLNKGTF KEQNDKPYCQ NCFLKLFC
//
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