ID   PDLI2_MACFA             Reviewed;         352 AA.
AC   Q9GKU1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=PDZ and LIM domain protein 2;
GN   Name=PDLIM2; ORFNames=QccE-18810;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (DEC-2000) 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; AB052137; BAB18991.1; -; mRNA.
DR   AlphaFoldDB; Q9GKU1; -.
DR   SMR; Q9GKU1; -.
DR   STRING; 9541.XP_005562866.1; -.
DR   eggNOG; KOG1703; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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..352
FT                   /note="PDZ and LIM domain protein 2"
FT                   /id="PRO_0000075863"
FT   DOMAIN          1..84
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          284..344
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          69..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT   MOD_RES         126
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96JY6"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYD6"
FT   MOD_RES         266
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYD6"
SQ   SEQUENCE   352 AA;  37392 MW;  BA94339A068EB954 CRC64;
     MALTVDVAGP APWGFRITGG RDFHTPIMVT KVAERGKAKD ADLRPGDIIV AINGESAEGM
     LHAEAQSKIR QSPSPLRLQL DRSQAASPGQ TNGDSSLEVL ATRFQGSVRT HTESHSSLRS
     SYSSPTSLSP RAGSPFSPPP FSSPLAGEAA ISRSFQSLAC SPGLPAADRL SYSGRPGSQQ
     AGLGRAGDSA VLVLPPSPGP RSSRPSVDSE GGSLLLDEDS EVFKMLQENR EGRAAPRQSS
     SFRLLQEALE AEERGGTPAF LPSSLSPQSS LPASRALATP PKLHTCEKCS TSIANQAVRI
     QEGRYRHPGC YTCADCGLNL KMRGHFWVGD ELYCEKHARQ RYSAPATLSS RA