ISL2_RAT
ID ISL2_RAT Reviewed; 360 AA.
AC P50480;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Insulin gene enhancer protein ISL-2;
DE Short=Islet-2;
GN Name=Isl2; Synonyms=Isl-2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spinal cord;
RX PubMed=7528105; DOI=10.1016/0092-8674(94)90027-2;
RA Tsuchida T., Ensini M., Morton S.B., Baldassare M., Edlund T.,
RA Jessell T.M., Pfaff S.L.;
RT "Topographic organization of embryonic motor neurons defined by expression
RT of LIM homeobox genes.";
RL Cell 79:957-970(1994).
RN [2]
RP STRUCTURE BY NMR OF 180-244.
RX PubMed=10329173; DOI=10.1006/jmbi.1999.2718;
RA Ippel H., Larsson G., Behravan G., Zdunek J., Lundqvist M., Schleucher J.,
RA Lycksell P.-O., Wijmenga S.;
RT "The solution structure of the homeodomain of the rat insulin-gene enhancer
RT protein Isl-1. Comparison with other homeodomains.";
RL J. Mol. Biol. 288:689-703(1999).
CC -!- FUNCTION: Transcriptional factor that defines subclasses of motoneurons
CC that segregate into columns in the spinal cord and select distinct axon
CC pathways. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LHX4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; L35571; AAA62161.1; -; mRNA.
DR PIR; A55198; A55198.
DR RefSeq; NP_065204.1; NM_020471.1.
DR PDB; 1BW5; NMR; -; A=191-255.
DR PDBsum; 1BW5; -.
DR AlphaFoldDB; P50480; -.
DR BMRB; P50480; -.
DR SMR; P50480; -.
DR STRING; 10116.ENSRNOP00000021074; -.
DR PaxDb; P50480; -.
DR GeneID; 57233; -.
DR KEGG; rno:57233; -.
DR UCSC; RGD:621849; rat.
DR CTD; 64843; -.
DR RGD; 621849; Isl2.
DR eggNOG; KOG0490; Eukaryota.
DR InParanoid; P50480; -.
DR OrthoDB; 948890at2759; -.
DR PhylomeDB; P50480; -.
DR EvolutionaryTrace; P50480; -.
DR PRO; PR:P50480; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0048663; P:neuron fate commitment; ISO:RGD.
DR GO; GO:0048665; P:neuron fate specification; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISO:RGD.
DR GO; GO:0021520; P:spinal cord motor neuron cell fate specification; ISO:RGD.
DR GO; GO:0021524; P:visceral motor neuron differentiation; ISO:RGD.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00132; LIM; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; DNA-binding; Homeobox; LIM domain;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..360
FT /note="Insulin gene enhancer protein ISL-2"
FT /id="PRO_0000075754"
FT DOMAIN 25..86
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 87..149
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DNA_BIND 192..251
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 151..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..302
FT /note="LIM-binding domain (LID)"
FT /evidence="ECO:0000250"
FT REGION 328..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96A47"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96A47"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96A47"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:1BW5"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:1BW5"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:1BW5"
SQ SEQUENCE 360 AA; 39675 MW; BE45E5AE7B6AA686 CRC64;
MVDIIFHYPF LGAMGDHSKK KPGTAMCVGC GSQIHDQFIL RVSPDLEWHA ACLKCAECSQ
YLDETCTCFV RDGKTYCKRD YVRLFGIKCA QCQVGFSSSD LVMRARDSVY HIECFRCSVC
SRQLLPGDEF SLREHELLCR ADHGLLLERA AAGSPRSPGP LPGTPPGLHL PDAGSGQQVS
LRTHVHKQAE KTTRVRTVLN EKQLHTLRTC YAANPRPDAL MKEQLVEMTG LSPRVIRVWF
QNKRCKDKKK SILMKQLQQQ QHSDKASLQG LTGTLLVAGS PSAHENAVQG SAVEVQTYQP
PWKALSEFAL QSDLDQPAFQ QLVSFSESGS LGNSSGSDVT SLSSQLPDTP NSMVPSPVET
