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 27-MAR-2024, entry version 179. 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}. 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; 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 GlyCosmos; P09022; 1 site, No reported glycans. DR GlyGen; P09022; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P09022; -. DR PhosphoSitePlus; P09022; -. DR PaxDb; 10090-ENSMUSP00000000964; -. DR AGR; MGI:96170; -. 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 Gene3D; 1.10.10.60; Homeodomain-like; 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:SF3; HOMEOBOX PROTEIN HOX-A1; 1. DR PANTHER; PTHR45946; HOMEOBOX PROTEIN ROUGH-RELATED; 1. DR Pfam; PF00046; Homeodomain; 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. 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 //