ID A0A2K6D2I4_MACNE Unreviewed; 1079 AA.
AC A0A2K6D2I4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Paxillin {ECO:0000256|ARBA:ARBA00023808};
GN Name=PXN {ECO:0000313|Ensembl:ENSMNEP00000030118.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000030118.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000030118.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A2K6D2I4; -.
DR Ensembl; ENSMNET00000054533.1; ENSMNEP00000030118.1; ENSMNEG00000038305.1.
DR GeneTree; ENSGT00940000158897; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000038305; Expressed in cerebellum and 11 other cell types or tissues.
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; 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:UP000233120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 844..903
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 904..961
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 962..1021
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1022..1079
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 26..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 115723 MW; 68384AB3A7E9D907 CRC64;
MNALLADLES TTSHISKRPV FLSEETPYSY PTGNHTYQEI AVPPPVPPPP SSEALNGTIL
DPLDQWQPSG SRFIHQQPQS SSPVCGSSAK TSSASNPQDS VGSPCSRVGE EEHVYSFPNK
QKSAEPSPTV MSTSLGSNLS ELDRLLLELN AVQHNPPGFP ADEANSSPPL PGALSPHYGV
PETNSPLGGK AGPLTKEKPK RNGGRGLEDV RPSVESLLDE LESSVPSPVP AITVNQGEMS
SPQRVTSTQQ QTRISASSAT RELDELMASL SDFKTSSSTV ALSAPGLLPG SAPSSYCSLP
PSPPPIPSVF LPPTTKPSPR GQGHTPEFPC TEQSGRDLLP PVAPSWLDLA GLGVMPDILN
SRSPSVEGSL WAVGTESQGR DWRHLPTLTH ELSGVPRGHT VPYAGSIGPQ EPGEPQGPPA
SPSCPEEALA ATREQPWASE VFRPERMPPS GAARSFQEVI EPAIVAVDRQ AVFPDTWTLT
EERGLQQERP RPEPGRLGSS SPASVTMEQL GAKMTERGSV ARPTQGPETP GSPEGTTEAA
TQAGKEQPEL PCAMATSTPS TTERISTSGQ IRSVIRRSRE TGHAHPMSRE PSPRRRLDPA
TLSRTPSQEQ LIAELQGRLG IQPEAEEPAE AAGPSAQDWL TEGIIITVQP RGKRAGGQLV
EKVVFPPGSP IPLRRTISVL ASPSVPLLQH RTDAVASSSS PLPSLPTSSP LGPSAYTCGS
SGVQSAGEEP HDEGVQGPTL STPAPHTMRS VGCQTDEDPL FPPMQIQGLE QRADGERCWA
AGWPRDSGRS SPGGQDEGGF MAQGKTGSSS PSGGPPKPGS QLDSMLGSLQ SDLNKLGVAT
VAKGVCGACK KPIAGQVVTA MGKTWHPEHF VCTHCQEEIG SRNFFERDGQ PYCEKDYHNL
FSPRCYYCNG PILDKVVTAL DRTWHPEHFF CAQCGAFFGP EGFHEKDGKA YCRKDYFDMF
APKCGGCARA ILENYISALN TLWHPECFVC RECFTPFVNG SFFEHDGQPY CEVHYHERRG
SLCSGCQKPI TGRCITAMAK KFHPEHFVCA FCLKQLNKGT FKEQNDKPYC QNCFLKLFC
//
