HXA9_MOUSE
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 03-AUG-2022, entry version 193.
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).
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 E-selectin and VCAM-1, on the endothelial cells surface at
CC sites of inflammation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Transiently interacts with PRMT5 in TNF-alpha stimulated
CC endothelial cells. {ECO:0000250}.
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.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 iPTMnet; P09631; -.
DR PhosphoSitePlus; P09631; -.
DR jPOST; P09631; -.
DR MaxQB; P09631; -.
DR PaxDb; P09631; -.
DR PRIDE; P09631; -.
DR ProteomicsDB; 266926; -. [P09631-1]
DR ProteomicsDB; 266927; -. [P09631-2]
DR Antibodypedia; 12395; 352 antibodies from 40 providers.
DR DNASU; 15405; -.
DR Ensembl; ENSMUST00000048680; ENSMUSP00000046939; ENSMUSG00000038227. [P09631-1]
DR Ensembl; ENSMUST00000114425; ENSMUSP00000110068; ENSMUSG00000038227. [P09631-2]
DR GeneID; 15405; -.
DR KEGG; mmu:15405; -.
DR UCSC; uc009byl.2; mouse. [P09631-1]
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; HHQAPMA; -.
DR OrthoDB; 976319at2759; -.
DR PhylomeDB; P09631; -.
DR TreeFam; TF317819; -.
DR BioGRID-ORCS; 15405; 1 hit in 74 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 146 other tissues.
DR Genevisible; P09631; MM.
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: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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0060065; P:uterus development; IGI:MGI.
DR CDD; cd00086; homeodomain; 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 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; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; DNA-binding;
KW Homeobox; Methylation; Nucleus; Reference proteome; Transcription;
KW 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 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
