ID A0A401T752_CHIPU Unreviewed; 368 AA.
AC A0A401T752;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=PDZ and LIM domain protein 2 {ECO:0000256|ARBA:ARBA00039370};
GN ORFNames=chiPu_0016983 {ECO:0000313|EMBL:GCC38469.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC38469.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC38469.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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. {ECO:0000256|ARBA:ARBA00037701}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC38469.1}.
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DR EMBL; BEZZ01001189; GCC38469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401T752; -.
DR STRING; 137246.A0A401T752; -.
DR OMA; MRGHFWF; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR InterPro; IPR031847; PDLI1-4/Zasp-like_mid.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24214:SF1; PDZ AND LIM DOMAIN PROTEIN 2; 1.
DR PANTHER; PTHR24214; PDZ AND LIM DOMAIN PROTEIN ZASP; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 11..84
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 303..363
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 120..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 40871 MW; AFFB2105560E772D CRC64;
MSRTVKLCGP GPWGFRITGG RDFHKKIAVS KVTSGSKADL VDLRLGDLIT NINGTETSDM
LNMEAQNRIR MCEGDLILDI ERPEAGSPGP LDGSPTNTFL AQRFESVLHT DKDENKNLVE
RRWSASNSPR SPNLTPVRSL SPAPDQKSIS PNTNRRSVSP AWSSEEKEET AFRGNMVPKG
IPAGIQVRRS TSPVSSSYSV PRVSHSTDSS PSEVRHQTEG SRSPSSAALS KRVPDRRSSN
HIDKDSEVYK MIQENRAAKE PPRQSNRFRQ LQEALDADQD GAVVLFPGRF SPSAPNTPVP
KYRVCEKCGS SITTEVVKIR DGCYRHQQCY ACTDCGLNLS MRGHFWFQDQ MYCEKHAQKR
FQEAEGSS
//
