ID A0A3P9AMR7_ESOLU Unreviewed; 1132 AA.
AC A0A3P9AMR7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Paxillin {ECO:0000256|ARBA:ARBA00023808};
GN Name=PXN {ECO:0000313|Ensembl:ENSELUP00000042373.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000042373.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000042373.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000042373.1}
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}.
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DR RefSeq; XP_010874612.1; XM_010876310.2.
DR AlphaFoldDB; A0A3P9AMR7; -.
DR STRING; 8010.ENSELUP00000042373; -.
DR Ensembl; ENSELUT00000036384.2; ENSELUP00000042373.1; ENSELUG00000023581.2.
DR GeneID; 105014199; -.
DR GeneTree; ENSGT00940000158897; -.
DR InParanoid; A0A3P9AMR7; -.
DR OMA; CENDWND; -.
DR OrthoDB; 370973at2759; -.
DR Proteomes; UP000265140; LG13.
DR Bgee; ENSELUG00000023581; Expressed in heart and 14 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; PAXILLIN-RELATED; 1.
DR PANTHER; PTHR24216:SF8; 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 4: Predicted;
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:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 897..956
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 957..1014
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1015..1074
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1075..1132
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1132 AA; 122306 MW; A1CF1E9987B9619C CRC64;
MDDLDALLAD LESTTSHISK RPVFLSEETP YSFPTGGNSY QDVSASPPVP PPPSAEALNG
TVLGSHNSSQ QSLGSAPKDS WSGDCSSPSG TEEDHVYSFP NKQKTDSSVA TMSSALGSNL
SELDRLLLEL NAVQQNSPSF PTTEETAPPL PSCSITHYVQ ENGGPPDITV SSPPQERLRR
DGPVDEGRPT VESLLDELEG SVPTPSPSMS VLHSELDSSS QQQARISASC ATRELDELMA
SLSDFKPVLG SLGSMNFDPS VDQAETSPSS TLAVHPPSRS PSSPAAAASP PLLPPQTSCD
SPLFALPAWE LHIEEEGGRA LSPPQPSVPS PPTVTGPAQD TLSFVEGDPE PKASMLTSGQ
KSPVLLNNYD PSPNAAKPSL NSATTDLDHN PSPALELGSS PAVTKSPSPL THINGSFSTP
MTTKSHVPVS KSHSAPPASV TKGPTPPLTS SKASSPSLIR SLKAPTPPAL TSPKISRRVQ
EPVAAAEPSL DEALDKLLAM SFTKVEDSST PPEAGQLKVE VVRQVYEQPI MPLDRRDLQP
DTTRSLQDGT STRDGSVMSG HTDGHRELMD WADVELNMCL QDGLDGSMTP YTERPYTDGS
LTPMTEASWM DESLDGLSCP GTPDGALDLP LLQPAAMDRV SASGHLKSVI RRTKETPNVH
PMYRDGHPRR GRVGPIIVNK SSSQDRLIEE LQGKLGIGRL TDRRRKQPDD WLTEGVIVMS
KPQRFRGDGA TKEVDKIIIP PESPVPQRRV ISPPPRHPPV AEEPRRLPCV MQTHAPLPPT
PPPCPPPQLP PHQKYIPPPP LPVQQPPAPK REPPPPAPPA PAPPPVQHKP TPPPPPKVLV
SVGCQTEYNP VFPPMQIMAQ GKGGPGGPPT QVNKLDNMLG SLQSDLHKLG VQTVAKGVCG
ACCKPIVGQV VTAMGRTWHP EHFVCTHCQE EIGSRNFFER DGAPYCEKDY HNLFSPRCHY
CNGPILDKVV TALDRTWHPE HFFCAQCGSF FGPEGFHEKD GKAYCRKDYF DMFAPKCGGC
ARAILENYIS ALNSLWHPEC FVCRECFTPF VNGSFFEHDG QPYCEVHYHE RRGSLCSGCQ
KPITGRCITA MAKKFHPEHF VCAFCLKQLN KGTFKEQNDK PYCQGCFVKL FS
//
