HXA1_MOUSE
ID HXA1_MOUSE Reviewed; 331 AA.
AC P09022; P15463;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 25-MAY-2022, entry version 173.
DE RecName: Full=Homeobox protein Hox-A1;
DE AltName: Full=Early retinoic acid 1;
DE AltName: Full=Homeobox protein Hox-1.6;
DE AltName: Full=Homeoboxless protein ERA-1-399;
DE AltName: Full=Homeotic protein ERA-1-993;
GN Name=Hoxa1; Synonyms=Era-1, Hox-1.6, Hoxa-1;
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].
RX PubMed=2906112; DOI=10.1128/mcb.8.9.3906-3917.1988;
RA Larosa G.J., Gudas L.J.;
RT "Early retinoic acid-induced F9 teratocarcinoma stem cell gene ERA-1:
RT alternate splicing creates transcripts for a homeobox-containing protein
RT and one lacking the homeobox.";
RL Mol. Cell. Biol. 8:3906-3917(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-331.
RX PubMed=2891503; DOI=10.1002/j.1460-2075.1987.tb02603.x;
RA Baron A., Featherstone M.S., Hill R.E., Hall A., Galliott B., Duboule D.;
RT "Hox-1.6: a mouse homeo-box-containing gene member of the Hox-1 complex.";
RL EMBO J. 6:2977-2986(1987).
RN [3]
RP PROTEIN SEQUENCE OF 146-160, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP INTERACTION WITH OGT, SUBCELLULAR LOCATION, GLYCOSYLATION AT THR-149, AND
RP MUTAGENESIS OF 1-MET--ASN-40; 1-MET--GLN-224; 60-HIS--HIS-70;
RP 60-HIS--HIS-142; 71-PRO--GLN-199; 203-TRP-MET-204; 225-PRO--GLU-284 AND
RP 272-TRP--ASN-275.
RX PubMed=29465778; DOI=10.1002/1873-3468.13015;
RA Draime A., Bridoux L., Belpaire M., Pringels T., Degand H., Morsomme P.,
RA Rezsohazy R.;
RT "The O-GlcNAc transferase OGT interacts with and post-translationally
RT modifies the transcription factor HOXA1.";
RL FEBS Lett. 592:1185-1201(2018).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=2569969; DOI=10.1002/j.1460-2075.1989.tb03534.x;
RA Duboule D., Dolle P.;
RT "The structural and functional organization of the murine HOX gene family
RT resembles that of Drosophila homeotic genes.";
RL EMBO J. 8:1497-1505(1989).
CC -!- FUNCTION: Sequence-specific transcription factor (PubMed:29465778).
CC Regulates multiple developmental processes including brainstem, inner
CC and outer ear, abducens nerve and cardiovascular development and
CC morphogenesis as well as cognition and behavior (By similarity). Also
CC part of a developmental regulatory system that provides cells with
CC specific positional identities on the anterior-posterior axis. Acts on
CC the anterior body structures. Seems to act in the maintenance and/or
CC generation of hindbrain segments (By similarity). Activates
CC transcription in the presence of PBX1A and PKNOX1 (PubMed:29465778).
CC {ECO:0000250|UniProtKB:P49639, ECO:0000250|UniProtKB:Q90423,
CC ECO:0000269|PubMed:29465778}.
CC -!- FUNCTION: The homeobox domain presumably directs sequence-specific DNA
CC binding. The N-terminal portion of ERA-1-993 may be involved in
CC interactions with one or more other regulatory proteins. Such an
CC interaction could regulate either the DNA-binding activity or the
CC transcriptional regulatory activity of ERA-1-993.
CC -!- FUNCTION: The homeoboxless ERA-1-399 protein could act as a competitive
CC inhibitor of the ERA-1-993 protein by competing for interaction with
CC regulatory protein(s) while being unable to bind to DNA.
CC -!- SUBUNIT: Interacts with OGT (via TPR repeats domain); the interaction
CC takes place mainly in the nucleus (PubMed:29465778). Forms a DNA-
CC binding heterodimer with transcription factor PBX1 (By similarity).
CC {ECO:0000250|UniProtKB:P49639, ECO:0000269|PubMed:29465778}.
CC -!- INTERACTION:
CC P09022; Q96GS6: ABHD17A; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-2870273;
CC P09022; Q6UY14: ADAMTSL4; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-742002;
CC P09022; Q6P1W5: C1orf94; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-946029;
CC P09022; Q9BSW2: CRACR2A; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-739773;
CC P09022; O95967: EFEMP2; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-743414;
CC P09022; Q5TD97: FHL5; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-750641;
CC P09022; P28799: GRN; Xeno; NbExp=2; IntAct=EBI-3957603, EBI-747754;
CC P09022; P49639: HOXA1; Xeno; NbExp=4; IntAct=EBI-3957603, EBI-740785;
CC P09022; P31249: HOXD3; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-3957655;
CC P09022; Q9UKS7: IKZF2; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-3893057;
CC P09022; Q14533: KRT81; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-739648;
CC P09022; Q6PEX3: KRTAP26-1; Xeno; NbExp=4; IntAct=EBI-3957603, EBI-3957672;
CC P09022; Q9BYR7: KRTAP3-2; Xeno; NbExp=4; IntAct=EBI-3957603, EBI-751260;
CC P09022; Q9BQ66: KRTAP4-12; Xeno; NbExp=4; IntAct=EBI-3957603, EBI-739863;
CC P09022; P26371: KRTAP5-9; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-3958099;
CC P09022; Q9UHV8: LGALS13; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-3957707;
CC P09022; P48059: LIMS1; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-306928;
CC P09022; Q8N448: LNX2; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-2340947;
CC P09022; O60711: LPXN; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-744222;
CC P09022; Q99750: MDFI; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-724076;
CC P09022; Q3V5L5: MGAT5B; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-3957727;
CC P09022; Q92802: N4BP2L2; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-2514973;
CC P09022; O15294: OGT; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-539828;
CC P09022; Q8WUM4: PDCD6IP; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-310624;
CC P09022; Q9NR12: PDLIM7; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-350517;
CC P09022; Q99697: PITX2; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-1175211;
CC P09022; O15162: PLSCR1; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-740019;
CC P09022; Q9NRQ2: PLSCR4; Xeno; NbExp=4; IntAct=EBI-3957603, EBI-769257;
CC P09022; Q9GZV8: PRDM14; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-3957793;
CC P09022; Q5JSZ5: PRRC2B; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-744891;
CC P09022; Q14088: RAB33A; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-744685;
CC P09022; Q9BYM8: RBCK1; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-2340624;
CC P09022; Q93062: RBPMS; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-740322;
CC P09022; O76081: RGS20; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-1052678;
CC P09022; Q8IYX7: SAXO1; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-3957636;
CC P09022; Q9H4F8: SMOC1; Xeno; NbExp=2; IntAct=EBI-3957603, EBI-2801103;
CC P09022; O43609: SPRY1; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-3866665;
CC P09022; Q13077: TRAF1; Xeno; NbExp=4; IntAct=EBI-3957603, EBI-359224;
CC P09022; Q12933: TRAF2; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-355744;
CC P09022; O75865: TRAPPC6A; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-743573;
CC P09022; P36406: TRIM23; Xeno; NbExp=2; IntAct=EBI-3957603, EBI-740098;
CC P09022; Q15654: TRIP6; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-742327;
CC P09022; Q05516: ZBTB16; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-711925;
CC P09022; Q9Y2Y4: ZBTB32; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-954098;
CC P09022; Q8IYH5: ZZZ3; Xeno; NbExp=3; IntAct=EBI-3957603, EBI-2795524;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29465778}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=ERA-1-993;
CC IsoId=P09022-1; Sequence=Displayed;
CC Name=ERA-1-399;
CC IsoId=P09022-2; Sequence=VSP_002380, VSP_002381;
CC -!- DEVELOPMENTAL STAGE: Expressed along the entire length of the primitive
CC streak. In early neurogenesis it is expressed in lateral and paraxial
CC mesoderm, endoderm and superficial ectoderm or in the neural tube. From
CC late neurogenesis to mid-embryogenesis, it presents similar spatial
CC domains in the lateral mesoderm, endoderm and superficial ectoderm but
CC is not detectable in any part of the hindbrain. At day 8-8.5 post-
CC coitum found in the embryonic mesoderm, anterior to the first somite,
CC up to the cephalic region at the level of the foregut and developing
CC heart. At day 9 post-coitum found in an anterior part of the developing
CC foregut and is restricted to an epithelial cell type. Expression in the
CC gut is found at the level of the second to third branchial bars.
CC {ECO:0000269|PubMed:2569969}.
CC -!- INDUCTION: By retinoic acid.
CC -!- PTM: Glycosylated by OGT. {ECO:0000269|PubMed:29465778}.
CC -!- SIMILARITY: Belongs to the Antp homeobox family. Labial subfamily.
CC {ECO:0000305}.
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DR EMBL; M22115; AAA37559.1; -; mRNA.
DR EMBL; M22115; AAA37558.1; -; mRNA.
DR EMBL; X06023; CAA29426.1; -; Genomic_DNA.
DR EMBL; X06024; CAA29427.1; -; Genomic_DNA.
DR EMBL; M20214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M20216; AAA37839.1; -; Genomic_DNA.
DR EMBL; M20215; AAA37839.1; JOINED; Genomic_DNA.
DR PIR; A27155; A27155.
DR PIR; A30242; A30242.
DR PIR; B30242; B30242.
DR AlphaFoldDB; P09022; -.
DR SMR; P09022; -.
DR DIP; DIP-59869N; -.
DR IntAct; P09022; 62.
DR STRING; 10090.ENSMUSP00000000964; -.
DR GlyGen; P09022; 1 site.
DR iPTMnet; P09022; -.
DR PaxDb; P09022; -.
DR PRIDE; P09022; -.
DR ProteomicsDB; 273360; -. [P09022-1]
DR MGI; MGI:96170; Hoxa1.
DR eggNOG; KOG0489; Eukaryota.
DR InParanoid; P09022; -.
DR PRO; PR:P09022; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P09022; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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:0021599; P:abducens nerve formation; ISO:MGI.
DR GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IGI:MGI.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IGI:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0060840; P:artery development; ISO:MGI.
DR GO; GO:0048844; P:artery morphogenesis; ISO:MGI.
DR GO; GO:0071361; P:cellular response to ethanol; IEP:MGI.
DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:MGI.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IMP:MGI.
DR GO; GO:0090102; P:cochlea development; ISO:MGI.
DR GO; GO:0090103; P:cochlea morphogenesis; ISO:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; ISO:MGI.
DR GO; GO:0021612; P:facial nerve structural organization; IGI:MGI.
DR GO; GO:0021754; P:facial nucleus development; IMP:MGI.
DR GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; ISO:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0008045; P:motor neuron axon guidance; IGI:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0050905; P:neuromuscular process; ISO:MGI.
DR GO; GO:0007634; P:optokinetic behavior; ISO:MGI.
DR GO; GO:0042473; P:outer ear morphogenesis; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0050795; P:regulation of behavior; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0021569; P:rhombomere 3 development; IMP:MGI.
DR GO; GO:0021570; P:rhombomere 4 development; IMP:MGI.
DR GO; GO:0021571; P:rhombomere 5 development; IMP:MGI.
DR GO; GO:0060876; P:semicircular canal formation; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
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; IPR046327; HXA1/B1/D1.
DR PANTHER; PTHR45946; PTHR45946; 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 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Direct protein sequencing;
KW DNA-binding; Glycoprotein; Homeobox; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..331
FT /note="Homeobox protein Hox-A1"
FT /id="PRO_0000200031"
FT DNA_BIND 225..284
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 57..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..199
FT /note="Interaction with OGT"
FT /evidence="ECO:0000269|PubMed:29465778"
FT REGION 279..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 200..205
FT /note="Antp-type hexapeptide"
FT COMPBIAS 57..72
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 149
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:29465778"
FT VAR_SEQ 115..133
FT /note="VSGGYPPCAPAVYSGNLST -> PPRSLSFPCFRDVFSSADL (in
FT isoform ERA-1-399)"
FT /evidence="ECO:0000305"
FT /id="VSP_002380"
FT VAR_SEQ 134..331
FT /note="Missing (in isoform ERA-1-399)"
FT /evidence="ECO:0000305"
FT /id="VSP_002381"
FT MUTAGEN 1..224
FT /note="Missing: Loss of interaction with OGT."
FT /evidence="ECO:0000269|PubMed:29465778"
FT MUTAGEN 1..40
FT /note="Missing: Interacts with OGT."
FT /evidence="ECO:0000269|PubMed:29465778"
FT MUTAGEN 60..142
FT /note="Missing: Loss of interaction with OGT."
FT /evidence="ECO:0000269|PubMed:29465778"
FT MUTAGEN 60..70
FT /note="Missing: Loss of interaction with OGT."
FT /evidence="ECO:0000269|PubMed:29465778"
FT MUTAGEN 71..199
FT /note="Missing: Loss of interaction with OGT."
FT /evidence="ECO:0000269|PubMed:29465778"
FT MUTAGEN 203..204
FT /note="WM->AA: Interacts with OGT."
FT /evidence="ECO:0000269|PubMed:29465778"
FT MUTAGEN 225..284
FT /note="Missing: Interacts with OGT."
FT /evidence="ECO:0000269|PubMed:29465778"
FT MUTAGEN 272..275
FT /note="WFQN->SVAA: Interacts with OGT."
FT /evidence="ECO:0000269|PubMed:29465778"
SQ SEQUENCE 331 AA; 36037 MW; F73E4FFB1C6F15B2 CRC64;
MNSFLEYPIL GSGDSGTCSA RAYPSDHGIT TFQSCAVSAN SCGGDDRFLV GRGVQISSPH
HHHHHHHHHH PQTATYQTSG NLGISYSHSS CGPSYGAQNF SAPYGPYGLN QEADVSGGYP
PCAPAVYSGN LSTPMVQHHH HHQGYAGGTV GSPQYIHHSY GQEQQTLALA TYNNSLSPLH
ASHQEACRSP ASETSSPAQT FDWMKVKRNP PKTGKVGEYG YVGQPNAVRT NFTTKQLTEL
EKEFHFNKYL TRARRVEIAA SLQLNETQVK IWFQNRRMKQ KKREKEGLLP ISPATPPGSD
EKTEESSEKS SPSPSAPSPA SSTSDTLTTS H
