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ALX1_RAT
ID   ALX1_RAT                Reviewed;         326 AA.
AC   Q63087;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=ALX homeobox protein 1 {ECO:0000305};
DE   AltName: Full=Cartilage homeoprotein 1 {ECO:0000303|PubMed:7690966};
DE            Short=CART-1 {ECO:0000303|PubMed:7690966};
GN   Name=Alx1 {ECO:0000312|RGD:2273};
GN   Synonyms=Cart1 {ECO:0000250|UniProtKB:Q8C8B0};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Chondrosarcoma;
RX   PubMed=7690966; DOI=10.1073/pnas.90.18.8633;
RA   Zhao G.-Q., Zhou X., Eberspaecher H., Solursh M., de Crombrugghe B.;
RT   "Cartilage homeoprotein 1, a homeoprotein selectively expressed in
RT   chondrocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:8633-8637(1993).
RN   [2]
RP   ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), SUBUNIT, SUBCELLULAR LOCATION, AND
RP   REGION.
RX   PubMed=12390248; DOI=10.1046/j.1365-2443.2002.00587.x;
RA   Furukawa K., Iioka T., Morishita M., Yamaguchi A., Shindo H., Namba H.,
RA   Yamashita S., Tsukazaki T.;
RT   "Functional domains of paired-like homeoprotein Cart1 and the relationship
RT   between dimerization and transcription activity.";
RL   Genes Cells 7:1135-1147(2002).
RN   [3]
RP   FUNCTION, INTERACTION WITH EP300, SUBCELLULAR LOCATION, ACETYLATION AT
RP   LYS-131, AND MUTAGENESIS OF LYS-131.
RX   PubMed=12929931; DOI=10.1359/jbmr.2003.18.8.1419;
RA   Iioka T., Furukawa K., Yamaguchi A., Shindo H., Yamashita S., Tsukazaki T.;
RT   "P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1),
RT   paired-like homeoprotein, through acetylation of the conserved lysine
RT   residue adjacent to the homeodomain.";
RL   J. Bone Miner. Res. 18:1419-1429(2003).
RN   [4]
RP   DOMAIN.
RX   PubMed=12559496; DOI=10.1016/s0925-4773(02)00416-1;
RA   Brouwer A., ten Berge D., Wiegerinck R., Meijlink F.;
RT   "The OAR/aristaless domain of the homeodomain protein Cart1 has an
RT   attenuating role in vivo.";
RL   Mech. Dev. 120:241-252(2003).
CC   -!- FUNCTION: Sequence-specific DNA-binding transcription factor that binds
CC       palindromic sequences within promoters and may activate or repress the
CC       transcription of a subset of genes (PubMed:12929931). Most probably
CC       regulates the expression of genes involved in the development of
CC       mesenchyme-derived craniofacial structures (By similarity). Early on in
CC       development, it plays a role in forebrain mesenchyme survival (By
CC       similarity). May also induce epithelial to mesenchymal transition (EMT)
CC       through the expression of SNAI1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q15699, ECO:0000269|PubMed:12929931}.
CC   -!- SUBUNIT: Binds DNA as a homodimer; required for transcriptional
CC       activation (PubMed:12390248). Interacts (via homeobox domain) with
CC       EP300; acetylates ALX1 and stimulates its transcriptional activity
CC       (PubMed:12929931). {ECO:0000269|PubMed:12390248,
CC       ECO:0000269|PubMed:12929931}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12390248,
CC       ECO:0000269|PubMed:12929931}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=alpha {ECO:0000303|PubMed:12390248};
CC         IsoId=Q63087-1; Sequence=Displayed;
CC       Name=2; Synonyms=beta {ECO:0000303|PubMed:12390248};
CC         IsoId=Q63087-2; Sequence=VSP_057658, VSP_057659;
CC       Name=3; Synonyms=gamma {ECO:0000303|PubMed:12390248};
CC         IsoId=Q63087-3; Sequence=VSP_057657;
CC   -!- TISSUE SPECIFICITY: Expressed in chondrocytes.
CC       {ECO:0000269|PubMed:7690966}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in condensed prechondrocytic mesenchymal
CC       cells and in early chondrocytes of cartilage primordia. Expression is
CC       lower in mature chondrocytes. {ECO:0000269|PubMed:7690966}.
CC   -!- DOMAIN: The OAR motif may negatively regulate DNA-binding and therefore
CC       transcriptional activity. It is found in the C-terminal transactivation
CC       domain that stimulates transcription. {ECO:0000269|PubMed:12390248,
CC       ECO:0000269|PubMed:12559496}.
CC   -!- PTM: Acetylated at Lys-131 by EP300; increases interaction with EP300
CC       and stimulates ALX1 transcriptional activity.
CC       {ECO:0000269|PubMed:12929931}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Unable to bind DNA and activate
CC       transcription. Acts as a dominant negative through dimerization with
CC       isoform 1. {ECO:0000269|PubMed:12390248}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Unable to bind DNA and activate
CC       transcription. Acts as a dominant negative through dimerization with
CC       isoform 1. {ECO:0000269|PubMed:12390248}.
CC   -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000305}.
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DR   EMBL; L14018; AAA40877.1; -; mRNA.
DR   PIR; A47523; A47523.
DR   RefSeq; NP_037053.1; NM_012921.1. [Q63087-1]
DR   RefSeq; XP_006241355.1; XM_006241293.2. [Q63087-1]
DR   AlphaFoldDB; Q63087; -.
DR   SMR; Q63087; -.
DR   STRING; 10116.ENSRNOP00000006007; -.
DR   iPTMnet; Q63087; -.
DR   PhosphoSitePlus; Q63087; -.
DR   PaxDb; Q63087; -.
DR   Ensembl; ENSRNOT00000006007; ENSRNOP00000006007; ENSRNOG00000004390. [Q63087-1]
DR   Ensembl; ENSRNOT00000107157; ENSRNOP00000080707; ENSRNOG00000004390. [Q63087-3]
DR   GeneID; 25401; -.
DR   KEGG; rno:25401; -.
DR   UCSC; RGD:2273; rat. [Q63087-1]
DR   CTD; 8092; -.
DR   RGD; 2273; Alx1.
DR   eggNOG; KOG0490; Eukaryota.
DR   GeneTree; ENSGT00940000158251; -.
DR   HOGENOM; CLU_047013_0_1_1; -.
DR   InParanoid; Q63087; -.
DR   OMA; SSPCGDQ; -.
DR   PhylomeDB; Q63087; -.
DR   TreeFam; TF350743; -.
DR   PRO; PR:Q63087; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000004390; Expressed in kidney and 2 other tissues.
DR   ExpressionAtlas; Q63087; baseline and differential.
DR   Genevisible; Q63087; RN.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISO:RGD.
DR   GO; GO:0014031; P:mesenchymal cell development; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0001755; P:neural crest cell migration; IEA:InterPro.
DR   GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR   GO; GO:0001501; P:skeletal system development; TAS:RGD.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR033209; ALX1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR003654; OAR_dom.
DR   PANTHER; PTHR24329:SF359; PTHR24329:SF359; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF03826; OAR; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS50803; OAR; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; Developmental protein;
KW   DNA-binding; Homeobox; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..326
FT                   /note="ALX homeobox protein 1"
FT                   /id="PRO_0000048857"
FT   DNA_BIND        132..191
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          192..326
FT                   /note="Transactivation domain"
FT                   /evidence="ECO:0000269|PubMed:12390248"
FT   MOTIF           306..319
FT                   /note="OAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00138"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15699"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15699"
FT   MOD_RES         131
FT                   /note="N6-acetyllysine; by EP300"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C8B0"
FT   MOD_RES         306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15699"
FT   VAR_SEQ         177..219
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12390248"
FT                   /id="VSP_057657"
FT   VAR_SEQ         178..192
FT                   /note="VWFQNRRAKWRKRER -> GQVEKKRTLRPNTAS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12390248"
FT                   /id="VSP_057658"
FT   VAR_SEQ         193..326
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12390248"
FT                   /id="VSP_057659"
FT   MUTAGEN         131
FT                   /note="K->R: Loss of EP300-mediated transcriptional
FT                   coactivation."
FT                   /evidence="ECO:0000269|PubMed:12929931"
FT   MUTAGEN         133..136
FT                   /note="RRHR->GGHG: Loss of transcriptional activity. Loss
FT                   of DNA-binding. Altered localization to the nucleus."
FT                   /evidence="ECO:0000269|PubMed:12390248"
FT   MUTAGEN         188..190
FT                   /note="RKR->GKG: Loss of transcriptional activity. No
FT                   effect on DNA-binding. Loss of homodimerization. Altered
FT                   localization to the nucleus."
FT                   /evidence="ECO:0000269|PubMed:12390248"
SQ   SEQUENCE   326 AA;  36904 MW;  0DD201EC595C74AE CRC64;
     MEFLSEKFAL KSPPSKNSDF YMGTGGALEH VMETLDNESF YGKATAGKCV QAFGPLPRAE
     HHVRLDRTSP CQDSSVNYGI TKVEGQPLHT ELNRAMDGCN NLRMSPVKGM PEKSELDELG
     DKCDSNVSSS KKRRHRTTFT SLQLEELEKV FQKTHYPDVY VREQLALRTE LTEARVQVWF
     QNRRAKWRKR ERYGQIQQAK SHFAATYDIS VLPRTDSYPQ IQNNLWAGNT SGGSVVTSCM
     LPRDASSCMT PYSHSPRTDS SYTGFSNHQN QFGHVPLNNF FTDSLLTGTT NGHAFETKPE
     FERRSSSIAV LRMKAKEHTA NISWAM
 
 
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