ID   HXA9_MOUSE              Reviewed;         271 AA.
AC   P09631; O70154; O70155;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   24-JAN-2024, entry version 201.
DE   RecName: Full=Homeobox protein Hox-A9;
DE   AltName: Full=Homeobox protein Hox-1.7;
GN   Name=Hoxa9; Synonyms=Hox-1.7, Hoxa-9;
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 [MRNA] (ISOFORMS HOXA-9 AND HOXA-9T).
RC   STRAIN=C57BL/6J, and ICR;
RX   PubMed=9524228; DOI=10.1016/s0378-1119(98)00014-6;
RA   Fujimoto S., Araki K., Chisaka O., Araki M., Takagi K., Yamamura K.;
RT   "Analysis of the murine Hoxa-9 cDNA: an alternatively spliced transcript
RT   encodes a truncated protein lacking the homeodomain.";
RL   Gene 209:77-85(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HOXA-9).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 180-271 (HOXA-9).
RX   PubMed=2891029; DOI=10.1128/mcb.7.10.3836-3841.1987;
RA   Rubin M.R., King W., Toth L.E., Sawczuk I.S., Levine M.S., D'Eustachio P.,
RA   Nguyen-Huu M.C.;
RT   "Murine Hox-1.7 homeo-box gene: cloning, chromosomal location, and
RT   expression.";
RL   Mol. Cell. Biol. 7:3836-3841(1987).
RN   [4]
RP   ERRATUM OF PUBMED:2891029, AND SEQUENCE REVISION.
RA   Rubin M.R., King W., Toth L.E., Sawczuk I.S., Levine M.S., D'Eustachio P.,
RA   Nguyen-Huu M.C.;
RL   Mol. Cell. Biol. 8:5593-5593(1988).
RN   [5]
RP   FUNCTION, INTERACTION WITH EIF4E, AND MUTAGENESIS OF TYR-11.
RX   PubMed=15657436; DOI=10.1128/mcb.25.3.1100-1112.2005;
RA   Topisirovic I., Kentsis A., Perez J.M., Guzman M.L., Jordan C.T.,
RA   Borden K.L.;
RT   "Eukaryotic translation initiation factor 4E activity is modulated by HOXA9
RT   at multiple levels.";
RL   Mol. Cell. Biol. 25:1100-1112(2005).
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. Required for
CC       induction of SELE/E-selectin and VCAM1 on the endothelial cell surface
CC       at sites of inflammation (By similarity). Positively regulates EIF4E-
CC       mediated mRNA nuclear export and also increases the translation
CC       efficiency of ODC mRNA in the cytoplasm by competing with factors which
CC       repress EIF4E activity such as PRH (PubMed:15657436).
CC       {ECO:0000250|UniProtKB:P31269, ECO:0000269|PubMed:15657436}.
CC   -!- SUBUNIT: Transiently interacts with PRMT5 in TNF-alpha stimulated
CC       endothelial cells (By similarity). Interacts with EIF4E
CC       (PubMed:15657436). {ECO:0000250|UniProtKB:P31269,
CC       ECO:0000269|PubMed:15657436}.
CC   -!- INTERACTION:
CC       P09631; Q9Z148: Ehmt2; NbExp=2; IntAct=EBI-925334, EBI-444966;
CC       P09631; P41778: Pbx1; NbExp=2; IntAct=EBI-925334, EBI-6996259;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P31269}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P31269}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=HoxA-9;
CC         IsoId=P09631-1; Sequence=Displayed;
CC       Name=HoxA-9T;
CC         IsoId=P09631-2; Sequence=VSP_002382, VSP_002383;
CC   -!- TISSUE SPECIFICITY: Expressed in high level in the embryonic and adult
CC       spinal cord with a preference in the posterior region.
CC   -!- PTM: Methylated on Arg-140 by PRMT5; methylation is critical for E-
CC       selectin induction. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Abd-B homeobox family. {ECO:0000305}.
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DR   EMBL; AB005457; BAA25800.1; -; mRNA.
DR   EMBL; AB005458; BAA25801.1; -; mRNA.
DR   EMBL; AB008914; BAA25802.1; -; Genomic_DNA.
DR   EMBL; BC055059; AAH55059.1; -; mRNA.
DR   EMBL; M28449; AAA78790.1; -; mRNA.
DR   CCDS; CCDS20146.1; -. [P09631-1]
DR   PIR; A31400; A31400.
DR   PIR; JC6553; JC6553.
DR   RefSeq; NP_034586.1; NM_010456.3. [P09631-1]
DR   PDB; 1PUF; X-ray; 1.90 A; A=193-269.
DR   PDBsum; 1PUF; -.
DR   AlphaFoldDB; P09631; -.
DR   SMR; P09631; -.
DR   BioGRID; 200373; 13.
DR   CORUM; P09631; -.
DR   DIP; DIP-35619N; -.
DR   IntAct; P09631; 10.
DR   MINT; P09631; -.
DR   STRING; 10090.ENSMUSP00000046939; -.
DR   ChEMBL; CHEMBL4879429; -.
DR   iPTMnet; P09631; -.
DR   PhosphoSitePlus; P09631; -.
DR   jPOST; P09631; -.
DR   MaxQB; P09631; -.
DR   PaxDb; 10090-ENSMUSP00000046939; -.
DR   ProteomicsDB; 266926; -. [P09631-1]
DR   ProteomicsDB; 266927; -. [P09631-2]
DR   Antibodypedia; 12395; 384 antibodies from 40 providers.
DR   DNASU; 15405; -.
DR   Ensembl; ENSMUST00000048680.8; ENSMUSP00000046939.6; ENSMUSG00000038227.16. [P09631-1]
DR   Ensembl; ENSMUST00000114425.3; ENSMUSP00000110068.2; ENSMUSG00000038227.16. [P09631-2]
DR   GeneID; 15405; -.
DR   KEGG; mmu:15405; -.
DR   UCSC; uc009byl.2; mouse. [P09631-1]
DR   AGR; MGI:96180; -.
DR   CTD; 3205; -.
DR   MGI; MGI:96180; Hoxa9.
DR   VEuPathDB; HostDB:ENSMUSG00000038227; -.
DR   eggNOG; KOG0487; Eukaryota.
DR   GeneTree; ENSGT00940000161864; -.
DR   HOGENOM; CLU_071854_0_0_1; -.
DR   InParanoid; P09631; -.
DR   OMA; VGTCTFP; -.
DR   OrthoDB; 728401at2759; -.
DR   PhylomeDB; P09631; -.
DR   TreeFam; TF317819; -.
DR   BioGRID-ORCS; 15405; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Hoxa9; mouse.
DR   EvolutionaryTrace; P09631; -.
DR   PRO; PR:P09631; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P09631; Protein.
DR   Bgee; ENSMUSG00000038227; Expressed in presomitic mesoderm and 148 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
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:0060216; P:definitive hemopoiesis; IGI:MGI.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IGI:MGI.
DR   GO; GO:0048706; P:embryonic skeletal system development; IMP:MGI.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IBA:GO_Central.
DR   GO; GO:0042118; P:endothelial cell activation; ISO:MGI.
DR   GO; GO:0008584; P:male gonad development; IGI:MGI.
DR   GO; GO:0030879; P:mammary gland development; IGI:MGI.
DR   GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IGI:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IGI: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:0007338; P:single fertilization; IGI:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR   GO; GO:0060065; P:uterus development; IGI:MGI.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   IDEAL; IID50023; -.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR020479; Homeobox_metazoa.
DR   InterPro; IPR006711; Hox9_activation_N.
DR   InterPro; IPR017112; HXA9/HXB9/HXC9.
DR   PANTHER; PTHR45970; AGAP004664-PA; 1.
DR   PANTHER; PTHR45970:SF3; HOMEOBOX PROTEIN HOX-A9; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF04617; Hox9_act; 1.
DR   PIRSF; PIRSF037109; Homeobox_Hox9; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   Genevisible; P09631; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW   DNA-binding; Homeobox; Methylation; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..271
FT                   /note="Homeobox protein Hox-A9"
FT                   /id="PRO_0000200082"
FT   DNA_BIND        205..264
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          154..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         139
FT                   /note="Symmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P31269"
FT   VAR_SEQ         105
FT                   /note="R -> S (in isoform HoxA-9T)"
FT                   /evidence="ECO:0000303|PubMed:9524228"
FT                   /id="VSP_002382"
FT   VAR_SEQ         106..271
FT                   /note="Missing (in isoform HoxA-9T)"
FT                   /evidence="ECO:0000303|PubMed:9524228"
FT                   /id="VSP_002383"
FT   MUTAGEN         11
FT                   /note="Y->A: Significant reduction in interaction with
FT                   EIF4E."
FT                   /evidence="ECO:0000269|PubMed:15657436"
FT   TURN            195..198
FT                   /evidence="ECO:0007829|PDB:1PUF"
FT   HELIX           214..226
FT                   /evidence="ECO:0007829|PDB:1PUF"
FT   HELIX           232..242
FT                   /evidence="ECO:0007829|PDB:1PUF"
FT   HELIX           246..267
FT                   /evidence="ECO:0007829|PDB:1PUF"
SQ   SEQUENCE   271 AA;  29917 MW;  C1E679D9CBF677B0 CRC64;
     MATTGALGNY YVDSFLLGAD AADELGAGRY APGTLGQPPR QAAALAEHPD FSPCSFQSKA
     AVFGASWNPV HAAGANAVPA AVYHHHHHPY VHPQAPVAAA APDGRYMRSW LEPTPGALSF
     AGLPSSRPYG IKPEPLSARR GDCPTLDTHT LSLTDYACGS PPVDREKQPS EGAFSENNAE
     NESGGDKPPI DPNNPAANWL HARSTRKKRC PYTKHQTLEL EKEFLFNMYL TRDRRYEVAR
     LLNLTERQVK IWFQNRRMKM KKINKDRAKD E
//