MEOX2_RAT
ID MEOX2_RAT Reviewed; 303 AA.
AC P39020;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Homeobox protein MOX-2 {ECO:0000250|UniProtKB:P32443};
DE AltName: Full=Growth arrest-specific homeobox {ECO:0000303|PubMed:8098844};
DE AltName: Full=Mesenchyme homeobox 2 {ECO:0000250|UniProtKB:P32443};
GN Name=Meox2 {ECO:0000312|RGD:3079};
GN Synonyms=Gax {ECO:0000303|PubMed:8098844},
GN Mox-2 {ECO:0000250|UniProtKB:P32443}, Mox2 {ECO:0000250|UniProtKB:P32443};
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], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Aorta;
RX PubMed=8098844; DOI=10.1128/mcb.13.6.3722-3733.1993;
RA Gorski D.H., Lepage D.F., Patel C.V., Copeland N.G., Jenkins N.A.,
RA Walsh K.;
RT "Molecular cloning of a diverged homeobox gene that is rapidly down-
RT regulated during the G0/G1 transition in vascular smooth muscle cells.";
RL Mol. Cell. Biol. 13:3722-3733(1993).
RN [2]
RP SEQUENCE REVISION.
RA Walsh K.;
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mesodermal transcription factor that plays a key role in
CC somitogenesis and somitogenesis and limb muscle differentiation.
CC Required during limb development for normal appendicular muscle
CC formation and for the normal regulation of myogenic genes (By
CC similarity). May have a regulatory role when quiescent vascular smooth
CC muscle cells reenter the cell cycle (PubMed:8098844). Also acts as a
CC negative regulator of angiogenesis. Activates expression of CDKN1A and
CC CDKN2A in endothelial cells, acting as a regulator of vascular cell
CC proliferation. While it activates CDKN1A in a DNA-dependent manner, it
CC activates CDKN2A in a DNA-independent manner (By similarity). Together
CC with TCF15, regulates transcription in heart endothelial cells to
CC regulate fatty acid transport across heart endothelial cells (By
CC similarity). {ECO:0000250|UniProtKB:P32443,
CC ECO:0000250|UniProtKB:P50222, ECO:0000269|PubMed:8098844}.
CC -!- SUBUNIT: Interacts with RNF10 (By similarity). Interacts with TCF15 (By
CC similarity). {ECO:0000250|UniProtKB:P32443,
CC ECO:0000250|UniProtKB:P50222}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P50222}. Nucleus
CC speckle {ECO:0000250|UniProtKB:P50222}.
CC -!- TISSUE SPECIFICITY: Aorta and heart. Also detected in lung and kidney.
CC {ECO:0000269|PubMed:8098844}.
CC -!- INDUCTION: Rapidly and transiently down-regulated during the transition
CC from G0 to G1 induced by mitogen stimulation.
CC {ECO:0000269|PubMed:8098844}.
CC -!- DOMAIN: The polyhistidine repeat may act as a targeting signal to
CC nuclear speckles. {ECO:0000250|UniProtKB:P50222}.
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DR EMBL; Z17223; CAA78931.1; -; mRNA.
DR PIR; A48130; A48130.
DR RefSeq; NP_058845.1; NM_017149.1.
DR AlphaFoldDB; P39020; -.
DR SMR; P39020; -.
DR STRING; 10116.ENSRNOP00000008803; -.
DR iPTMnet; P39020; -.
DR PhosphoSitePlus; P39020; -.
DR PaxDb; P39020; -.
DR GeneID; 29279; -.
DR KEGG; rno:29279; -.
DR UCSC; RGD:3079; rat.
DR CTD; 4223; -.
DR RGD; 3079; Meox2.
DR eggNOG; KOG0489; Eukaryota.
DR InParanoid; P39020; -.
DR OrthoDB; 1522857at2759; -.
DR PhylomeDB; P39020; -.
DR PRO; PR:P39020; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0060173; P:limb development; ISO:RGD.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0061053; P:somite development; IBA:GO_Central.
DR GO; GO:0001757; P:somite specification; 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; IPR020479; Homeobox_metazoa.
DR InterPro; IPR042634; MOX-1/MOX-2.
DR PANTHER; PTHR24328; PTHR24328; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00024; HOMEOBOX.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 2: Evidence at transcript level;
KW Activator; Developmental protein; DNA-binding; Homeobox; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..303
FT /note="Homeobox protein MOX-2"
FT /id="PRO_0000049199"
FT DNA_BIND 186..245
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 63..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..82
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 303 AA; 33605 MW; 7776642AEFA3A2E8 CRC64;
MEHPLFGCLR SPHATAQGLH PFSQSSLALH GRSDHMSYPE LSTSSSSCII AGYPNEEGMF
ASQHHRGHHH HHHHHHHHHQ QQQHQALQSN WHLPQMSSPP SAARHSLCLQ PDSGGPPELG
SSPPVLCSNS SSLGSSTPTG AACAPRDYGR QALSPAEVEK RSGSKRKSDS SDSQEGNYKS
EVNSKPRKER TAFTKEQIRE LEAEFAHHNY LTRLRRYEIA VNLDLTERQV KVWFQNRRMK
WKRVKGGQQG AAAREKELVN VKKGTLLPSE LSGIGAATLQ QTGDSLANDD SRDSDHSSEH
AHL
