HXD3_MOUSE
ID HXD3_MOUSE Reviewed; 433 AA.
AC P09027; Q3UUD3;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Homeobox protein Hox-D3;
DE AltName: Full=Homeobox protein Hox-4.1;
DE AltName: Full=Homeobox protein MH-19;
GN Name=Hoxd3; Synonyms=Hox-4.1, Hoxd-3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7916214; DOI=10.1016/0167-4781(94)90276-3;
RA Brown W.M., Zhou L., Taylor G.R.;
RT "The nucleotide sequence of the murine Hox-D3 (Hox-4.1) gene reveals
RT extensive identity with the human protein.";
RL Biochim. Biophys. Acta 1219:219-222(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7710686; DOI=10.1089/dna.1995.14.295;
RA Bedford M., Orr-Urtreger A., Arman E., Lonai P.;
RT "Analysis of the Hoxd-3 gene: structure and localization of its sense and
RT natural antisense transcripts.";
RL DNA Cell Biol. 14:295-304(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=ICR X Swiss Webster; TISSUE=Liver;
RX PubMed=8710855; DOI=10.1073/pnas.93.16.8247;
RA Tan D.-P., Shao X., Pu L., Guo V., Nirenberg M.;
RT "Sequence and expression of the murine Hoxd-3 homeobox gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8247-8252(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-303.
RX PubMed=2890503; DOI=10.1089/dna.1987.6.409;
RA Lonai P., Arman E., Czosnek H., Ruddle F.H., Blatt C.;
RT "New murine homeoboxes: structure, chromosomal assignment, and differential
RT expression in adult erythropoiesis.";
RL DNA 6:409-418(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-335.
RA Lonai P.;
RL Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sequence-specific transcription factor which is part of a
CC developmental regulatory system that provides cells with specific
CC positional identities on the anterior-posterior axis.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Detected in adult kidney, but not in other adult
CC tissues tested. {ECO:0000269|PubMed:8710855}.
CC -!- DEVELOPMENTAL STAGE: Detected in 12-, 14-, and 17-day-old mouse embryos
CC in the posterior half of the myelencephalon, spinal cord, dorsal root
CC ganglia, first cervical vertebra, thyroid gland, kidney tubules,
CC esophagus, stomach, and intestines. {ECO:0000269|PubMed:8710855}.
CC -!- SIMILARITY: Belongs to the Antp homeobox family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60683.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAC52779.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAC52780.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE23694.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA51975.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U03485; AAB60683.1; ALT_INIT; Genomic_DNA.
DR EMBL; U03496; AAB60683.1; JOINED; Genomic_DNA.
DR EMBL; X73573; CAA51975.1; ALT_SEQ; mRNA.
DR EMBL; L24363; AAA37855.1; -; Genomic_DNA.
DR EMBL; U56400; AAC52779.1; ALT_INIT; mRNA.
DR EMBL; U56401; AAC52780.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK138525; BAE23694.1; ALT_INIT; mRNA.
DR EMBL; M18169; AAA37846.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS38149.1; -.
DR PIR; D29585; D29585.
DR PIR; S34164; S34164.
DR PIR; S47539; S47539.
DR RefSeq; NP_034598.2; NM_010468.2.
DR AlphaFoldDB; P09027; -.
DR SMR; P09027; -.
DR BioGRID; 200396; 4.
DR IntAct; P09027; 4.
DR STRING; 10090.ENSMUSP00000107614; -.
DR PhosphoSitePlus; P09027; -.
DR PaxDb; P09027; -.
DR PRIDE; P09027; -.
DR ProteomicsDB; 266935; -.
DR Antibodypedia; 19525; 211 antibodies from 24 providers.
DR DNASU; 15434; -.
DR Ensembl; ENSMUST00000047830; ENSMUSP00000044809; ENSMUSG00000079277.
DR Ensembl; ENSMUST00000111982; ENSMUSP00000107613; ENSMUSG00000079277.
DR Ensembl; ENSMUST00000111983; ENSMUSP00000107614; ENSMUSG00000079277.
DR GeneID; 15434; -.
DR KEGG; mmu:15434; -.
DR UCSC; uc008kee.1; mouse.
DR CTD; 3232; -.
DR MGI; MGI:96207; Hoxd3.
DR VEuPathDB; HostDB:ENSMUSG00000079277; -.
DR eggNOG; KOG0489; Eukaryota.
DR GeneTree; ENSGT00940000160027; -.
DR HOGENOM; CLU_051508_1_0_1; -.
DR InParanoid; P09027; -.
DR OMA; KTAYYDN; -.
DR OrthoDB; 934469at2759; -.
DR PhylomeDB; P09027; -.
DR TreeFam; TF315938; -.
DR BioGRID-ORCS; 15434; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Hoxd3; mouse.
DR PRO; PR:P09027; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P09027; protein.
DR Bgee; ENSMUSG00000079277; Expressed in ureteric bud and 98 other tissues.
DR ExpressionAtlas; P09027; baseline and differential.
DR Genevisible; P09027; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0051216; P:cartilage development; IGI:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0021615; P:glossopharyngeal nerve morphogenesis; IGI:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0030878; P:thyroid gland development; IGI:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; ISO:MGI.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR025281; DUF4074.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001827; Homeobox_Antennapedia_CS.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR020479; Homeobox_metazoa.
DR Pfam; PF13293; DUF4074; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00024; HOMEOBOX.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00032; ANTENNAPEDIA; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Homeobox; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..433
FT /note="Homeobox protein Hox-D3"
FT /id="PRO_0000200205"
FT DNA_BIND 195..254
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 44..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 161..166
FT /note="Antp-type hexapeptide"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 187
FT /note="D -> N (in Ref. 5 and 6; AAA37846)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="G -> D (in Ref. 5 and 6; AAA37846)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="A -> T (in Ref. 5 and 6; AAA37846)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="Missing (in Ref. 2; CAA51975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 45976 MW; 0BA0409A7F32F9E6 CRC64;
MLFEQGQLTL ELPECTMQKA AYYENPGLFG GYGYSKATDT YGYSTPHQPY PPPAAANSLD
SDYPSSACSI QSSAPLRAPA HKGAELNGSC MRPGTGNSQG GGGGNQPPGL NSEQQPPQPP
PPPPPTLPPS SPTNPGSGVP AKKTKGGLSA SSSSSTISKQ IFPWMKESRQ NSKQKNSCAT
SGENCEDKSP PGPASKRVRT AYTSAQLVEL EKEFHFNRYL CRPRRVEMAN LLNLTERQIK
IWFQNRRMKY KKDQKAKGIL HSPAGQSPER SPPLGGAAGH VAYSGQLPPV PGLAYDAPSP
PAFAKSQPNM YGLAAYTAPL SSCLPQQKRY PAPEFEPHPM ASNGGGFASA NLQGSPVYVG
GNFVDSMAPT SGPVFNLGHL SHPSSASVDY SCAAQIPGNH HHGPCDPHPT YTDLSAHHSS
QGRLPEAPKL THL
