PDLI2_BOVIN
ID PDLI2_BOVIN Reviewed; 348 AA.
AC Q3T0C8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=PDZ and LIM domain protein 2;
GN Name=PDLIM2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable adapter protein located at the actin cytoskeleton
CC that promotes cell attachment. Necessary for the migratory capacity of
CC epithelial cells. Overexpression enhances cell adhesion to collagen and
CC fibronectin and suppresses anchorage independent growth. May contribute
CC to tumor cell migratory capacity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with alpha-actinins ACTN1 and ACTN4, FLNA and MYH9
CC (By similarity). Interacts (via LIM zinc-binding domain) with MKRN2 (By
CC similarity). {ECO:0000250|UniProtKB:Q6AYD6,
CC ECO:0000250|UniProtKB:Q8R1G6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC Note=Localizes at the cytoskeleton. Colocalizes with beta-1 integrin
CC (ITGB1) and alpha-actinin but not with paxillin (PXN) (By similarity).
CC {ECO:0000250}.
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DR EMBL; BC102452; AAI02453.1; -; mRNA.
DR RefSeq; NP_001029602.1; NM_001034430.2.
DR AlphaFoldDB; Q3T0C8; -.
DR SMR; Q3T0C8; -.
DR STRING; 9913.ENSBTAP00000009697; -.
DR iPTMnet; Q3T0C8; -.
DR PaxDb; Q3T0C8; -.
DR PeptideAtlas; Q3T0C8; -.
DR PRIDE; Q3T0C8; -.
DR Ensembl; ENSBTAT00000009697; ENSBTAP00000009697; ENSBTAG00000007369.
DR Ensembl; ENSBTAT00000066358; ENSBTAP00000065726; ENSBTAG00000007369.
DR GeneID; 512907; -.
DR KEGG; bta:512907; -.
DR CTD; 64236; -.
DR VEuPathDB; HostDB:ENSBTAG00000007369; -.
DR VGNC; VGNC:32708; PDLIM2.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000160418; -.
DR HOGENOM; CLU_038114_1_1_1; -.
DR InParanoid; Q3T0C8; -.
DR OMA; HAVRIQE; -.
DR OrthoDB; 840552at2759; -.
DR TreeFam; TF106408; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000007369; Expressed in esophagus and 104 other tissues.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF15936; DUF4749; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..348
FT /note="PDZ and LIM domain protein 2"
FT /id="PRO_0000239837"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 280..340
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 67..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 132
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYD6"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYD6"
SQ SEQUENCE 348 AA; 37671 MW; 77BBA79DDA12D13C CRC64;
MALTVDVVGP APWGFRISGG RDFHTPIMVT KVTERGKAEA ADLRPGDIIV SINGESAKDM
LHAEAQSKIR QSPSPLRLQL DRPQAASPGQ ANGESSLEVL ATRFQSSRRT HTDSQASLSP
RPCSPFFTLP PTSPQAPTGE VVTSHSFQSL AYSLEPASAD HLYYGGRRGS RQASLSPAGD
SAVLVLPPPP SPGARSSSSR LSVVSEGESH LLREDSEVFK MLQENREARM APRQSSSFRL
LQEALEAEER GGTPAYLPSS LSPQSSLPTS RALASPPKLH TCEKCNTSIA NQAVRIQEGR
YRHPGCYTCA DCGLNLKMRG HFWVGDELYC EKHARQRYSA PPTLNSQA
