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HXA13_MOUSE
ID   HXA13_MOUSE             Reviewed;         386 AA.
AC   Q62424;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Homeobox protein Hox-A13;
DE   AltName: Full=Homeobox protein Hox-1.10;
GN   Name=Hoxa13; Synonyms=Hox-1.10;
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=8673126; DOI=10.1038/ng0796-284;
RA   Mortlock D.P., Post L.C., Innis J.W.;
RT   "The molecular basis of hypodactyly (Hd): a deletion in Hoxa 13 leads to
RT   arrest of digital arch formation.";
RL   Nat. Genet. 13:284-289(1996).
RN   [2]
RP   INTERACTION WITH MEIS1; MEIS2 AND MEIS3.
RX   PubMed=15617687; DOI=10.1016/j.ydbio.2004.10.004;
RA   Williams T.M., Williams M.E., Innis J.W.;
RT   "Range of HOX/TALE superclass associations and protein domain requirements
RT   for HOXA13:MEIS interaction.";
RL   Dev. Biol. 277:457-471(2005).
RN   [3]
RP   STRUCTURE BY NMR OF 320-386 IN COMPLEX WITH DNA, SUBUNIT, AND MUTAGENESIS
RP   OF ILE-366; ASN-370 AND VAL-373.
RX   PubMed=21829694; DOI=10.1371/journal.pone.0023069;
RA   Zhang Y., Larsen C.A., Stadler H.S., Ames J.B.;
RT   "Structural basis for sequence specific DNA binding and protein
RT   dimerization of HOXA13.";
RL   PLoS ONE 6:E23069-E23069(2011).
CC   -!- FUNCTION: Sequence-specific, AT-rich binding transcription factor which
CC       is part of a developmental regulatory system that provides cells with
CC       specific positional identities on the anterior-posterior axis.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a homodimer. Interacts with MEIS1, MEIS2 and
CC       MEIS3. {ECO:0000269|PubMed:15617687, ECO:0000269|PubMed:21829694}.
CC   -!- INTERACTION:
CC       Q62424; Q60954-2: Meis1; NbExp=3; IntAct=EBI-925160, EBI-445723;
CC       Q62424; P97454: Smad5; NbExp=3; IntAct=EBI-925160, EBI-7066475;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DISEASE: Note=Defects in Hoxa13 are the cause of hypodactyly (Hd), a
CC       condition characterized by profound deficiency of digital arch
CC       structures.
CC   -!- SIMILARITY: Belongs to the Abd-B homeobox family. {ECO:0000305}.
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DR   EMBL; U59322; AAB03322.1; -; Genomic_DNA.
DR   RefSeq; NP_032290.1; NM_008264.1.
DR   PDB; 2LD5; NMR; -; A=320-386.
DR   PDBsum; 2LD5; -.
DR   AlphaFoldDB; Q62424; -.
DR   BMRB; Q62424; -.
DR   SMR; Q62424; -.
DR   BioGRID; 200366; 4.
DR   IntAct; Q62424; 6.
DR   STRING; 10090.ENSMUSP00000039170; -.
DR   PhosphoSitePlus; Q62424; -.
DR   PaxDb; Q62424; -.
DR   PRIDE; Q62424; -.
DR   ProteomicsDB; 273359; -.
DR   Antibodypedia; 12410; 150 antibodies from 25 providers.
DR   DNASU; 15398; -.
DR   Ensembl; ENSMUST00000147595; ENSMUSP00000125221; ENSMUSG00000038203.
DR   GeneID; 15398; -.
DR   KEGG; mmu:15398; -.
DR   UCSC; uc029vvl.1; mouse.
DR   CTD; 3209; -.
DR   MGI; MGI:96173; Hoxa13.
DR   eggNOG; KOG0487; Eukaryota.
DR   GeneTree; ENSGT00940000162322; -.
DR   InParanoid; Q62424; -.
DR   OMA; YMDTAAS; -.
DR   OrthoDB; 1190384at2759; -.
DR   PhylomeDB; Q62424; -.
DR   BioGRID-ORCS; 15398; 3 hits in 67 CRISPR screens.
DR   EvolutionaryTrace; Q62424; -.
DR   PRO; PR:Q62424; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q62424; protein.
DR   Bgee; ENSMUSG00000038203; Expressed in phalanx and 96 other tissues.
DR   ExpressionAtlas; Q62424; baseline and differential.
DR   GO; GO:0005694; C:chromosome; ISO:MGI.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA: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; IMP:NTNU_SB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IMP:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR   GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
DR   GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IMP:MGI.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
DR   GO; GO:0048619; P:embryonic hindgut morphogenesis; ISO:MGI.
DR   GO; GO:0060847; P:endothelial cell fate specification; IMP:MGI.
DR   GO; GO:0001886; P:endothelial cell morphogenesis; IMP:MGI.
DR   GO; GO:0048839; P:inner ear development; IMP:MGI.
DR   GO; GO:0030539; P:male genitalia development; IMP:MGI.
DR   GO; GO:0097152; P:mesenchymal cell apoptotic process; IMP:MGI.
DR   GO; GO:0140014; P:mitotic nuclear division; IMP:MGI.
DR   GO; GO:2001055; P:positive regulation of mesenchymal cell apoptotic process; IMP:MGI.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0030510; P:regulation of BMP signaling pathway; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR   GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR022067; HoxA13_N.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF12284; HoxA13_N; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Developmental protein; DNA-binding; Homeobox; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..386
FT                   /note="Homeobox protein Hox-A13"
FT                   /id="PRO_0000200102"
FT   DNA_BIND        320..379
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   MUTAGEN         366
FT                   /note="I->A: Decreased DNA binding and transcriptional
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:21829694"
FT   MUTAGEN         370
FT                   /note="N->A: Decreased DNA binding and transcriptional
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:21829694"
FT   MUTAGEN         373
FT                   /note="V->A: Decreased DNA binding and transcriptional
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:21829694"
FT   HELIX           329..341
FT                   /evidence="ECO:0007829|PDB:2LD5"
FT   HELIX           347..357
FT                   /evidence="ECO:0007829|PDB:2LD5"
FT   HELIX           362..381
FT                   /evidence="ECO:0007829|PDB:2LD5"
SQ   SEQUENCE   386 AA;  39567 MW;  2B01DCC9B1951324 CRC64;
     MTASVLLHPR WIEPTVMFLY DNGGGLVADE LNKNMEGAAA AAAAAAAAAA AGAGGGGFPH
     PAAAAAGGNF SVAAAAAAAA AAAANQCRNL MAHPAPLAPG AAAAYSSAPG EAPPSAAAAA
     AAAAAAAAAA AAASSSGGPG PAGPAGAEAA KQCSPCSAAA QSSSGPAALP YGYFGSGYYP
     CARMGPHPNA IKSCAQPASA AAAFADKYMD TAGPAAEEFS SRAKEFAFYH QGYAAGPYHH
     HQPVPGYLDM PVVPGLGGPG ESRHEPLGLP MESYQPWALP NGWNGQMYCP KEQTQPPHLW
     KSTLPDVVSH PSDASSYRRG RKKRVPYTKV QLKELEREYA TNKFITKDKR RRISATTNLS
     ERQVTIWFQN RRVKEKKVIN KLKTTS
 
 
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