ID A0A455AJ82_PHYMC Unreviewed; 909 AA.
AC A0A455AJ82;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Paxillin {ECO:0000256|ARBA:ARBA00023808};
GN Name=PXN {ECO:0000313|RefSeq:XP_028335783.1,
GN ECO:0000313|RefSeq:XP_028335791.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028335783.1};
RN [1] {ECO:0000313|RefSeq:XP_028335783.1, ECO:0000313|RefSeq:XP_028335791.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028335783.1,
RC ECO:0000313|RefSeq:XP_028335791.1};
RG RefSeq;
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 RefSeq; XP_028335783.1; XM_028479982.2.
DR RefSeq; XP_028335791.1; XM_028479990.2.
DR KEGG; pcad:102975066; -.
DR Proteomes; UP000248484; Chromosome 19.
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:UP000248484};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 674..733
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 734..791
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 792..851
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 852..909
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 23..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 97977 MW; 4649520D89F0D759 CRC64;
MSSSLGSNLS ELDRLLLELN AVQHNPPGFP ADEANSSPPL PGALSPHYGI PENNSPLGGK
AGPLTKEKPK RNGGRSLEDV RPSVESLLDE LESSVPSPVP AITVNQGEMS SPQRVTSSQQ
QTRISASSAT RELDELMASL SDFKTSSSAV ALSSPRLLPN SAPSPHHILS PPLPPPGPSV
FLPPPRKPSP RGHGHTLEVL CPDDNVARSW LDLAGLGEMP DTPNSRSPST ESSLGPPGAE
SQARVWRDPP NASLVSELSR VPPGHTLPHA GCTGPQEAGE PQVLSANPLC PGEAVAATWE
WPWALEALRP ESPRGAMPSF QEVIEPAAMA VDRQAIFPDT WSLTKARGQQ KERARPEPGE
PESRCPAPVE EEQLGGETAT GGSLVRPAQG PKTPRRPEGT TEAAAEARRE RPELPQAVVV
DTPNTTERIS TSGQAGIRSM IRRSRETGHA HPMSWEPSPR RRLDPATLSR TPSQERLIAE
LQGRLGIQPE VVFPSGSPIP LRRTFSVLPS PPPPSPLLQH RKDVSASSSS PRPSPPTSST
LGPSALPRGP PGVQSAGAGP REDGVQGPTP PTPAPHSVRS MGCQTDEDPL FPPMQIQGLE
QRVDGELCWV AGWPPNGSQS SPEGQDEGGF MAQGKTGSSS PPGGPPKPGS 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
QNCFVKLFC
//
