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LHX1_CHICK
ID   LHX1_CHICK              Reviewed;         406 AA.
AC   P53411;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=LIM/homeobox protein Lhx1;
DE            Short=LIM homeobox protein 1;
DE   AltName: Full=Homeobox protein Lim-1;
GN   Name=LHX1; Synonyms=LIM-1, LIM1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   PubMed=7528105; DOI=10.1016/0092-8674(94)90027-2;
RA   Tsuchida T., Ensini M., Morton S.B., Baldassare M., Edlund T.,
RA   Jessell T.M., Pfaff S.L.;
RT   "Topographic organization of embryonic motor neurons defined by expression
RT   of LIM homeobox genes.";
RL   Cell 79:957-970(1994).
CC   -!- FUNCTION: Transcriptional factor that defines subclasses of motoneurons
CC       that segregate into columns in the spinal cord and select distinct axon
CC       pathways. Acts in conjunction with ISL-2. {ECO:0000269|PubMed:7528105}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed prior to the formation of distinct motor
CC       axon pathways and before the segregation of motor neurons into columns.
CC       Expression is confined to the motor neurons in the lateral subdivision
CC       of the lateral motor column (LMC). {ECO:0000269|PubMed:7528105}.
CC   -!- DOMAIN: The LIM domains exert a negative regulatory function and
CC       disruption of the LIM domains produces an activated form. In addition,
CC       two activation domains and a negative regulatory domain exist C-
CC       terminally to the homeobox (By similarity). {ECO:0000250}.
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DR   EMBL; L35569; AAA62173.1; -; mRNA.
DR   PIR; I50375; I50375.
DR   RefSeq; NP_990744.1; NM_205413.1.
DR   AlphaFoldDB; P53411; -.
DR   SMR; P53411; -.
DR   STRING; 9031.ENSGALP00000008672; -.
DR   PaxDb; P53411; -.
DR   GeneID; 396381; -.
DR   KEGG; gga:396381; -.
DR   CTD; 3975; -.
DR   VEuPathDB; HostDB:geneid_396381; -.
DR   eggNOG; KOG0490; Eukaryota.
DR   InParanoid; P53411; -.
DR   OrthoDB; 1070389at2759; -.
DR   PhylomeDB; P53411; -.
DR   PRO; PR:P53411; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005634; C:nucleus; IDA:AgBase.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; ISS:UniProtKB.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; ISS:UniProtKB.
DR   GO; GO:0009948; P:anterior/posterior axis specification; ISS:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; ISS:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; ISS:UniProtKB.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; ISS:UniProtKB.
DR   GO; GO:0021937; P:cerebellar Purkinje cell-granule cell precursor cell signaling involved in regulation of granule cell precursor cell proliferation; ISS:UniProtKB.
DR   GO; GO:0021549; P:cerebellum development; ISS:UniProtKB.
DR   GO; GO:0072049; P:comma-shaped body morphogenesis; ISS:UniProtKB.
DR   GO; GO:0097379; P:dorsal spinal cord interneuron posterior axon guidance; IDA:UniProtKB.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; ISS:UniProtKB.
DR   GO; GO:0001705; P:ectoderm formation; ISS:UniProtKB.
DR   GO; GO:0009880; P:embryonic pattern specification; ISS:UniProtKB.
DR   GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; ISS:UniProtKB.
DR   GO; GO:0048703; P:embryonic viscerocranium morphogenesis; ISS:UniProtKB.
DR   GO; GO:0001706; P:endoderm formation; ISS:UniProtKB.
DR   GO; GO:0060429; P:epithelium development; ISS:UniProtKB.
DR   GO; GO:0021871; P:forebrain regionalization; ISS:UniProtKB.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; ISS:UniProtKB.
DR   GO; GO:0060322; P:head development; ISS:UniProtKB.
DR   GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR   GO; GO:0060993; P:kidney morphogenesis; NAS:AgBase.
DR   GO; GO:0097477; P:lateral motor column neuron migration; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0072179; P:nephric duct formation; NAS:AgBase.
DR   GO; GO:0072178; P:nephric duct morphogenesis; ISS:UniProtKB.
DR   GO; GO:0061205; P:paramesonephric duct development; ISS:UniProtKB.
DR   GO; GO:0007389; P:pattern specification process; ISS:UniProtKB.
DR   GO; GO:2000744; P:positive regulation of anterior head development; ISS:UniProtKB.
DR   GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR   GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR   GO; GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB.
DR   GO; GO:2000768; P:positive regulation of nephron tubule epithelial cell differentiation; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0009791; P:post-embryonic development; ISS:UniProtKB.
DR   GO; GO:0090009; P:primitive streak formation; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:2001141; P:regulation of RNA biosynthetic process; NAS:AgBase.
DR   GO; GO:0072077; P:renal vesicle morphogenesis; ISS:UniProtKB.
DR   GO; GO:0032526; P:response to retinoic acid; IDA:AgBase.
DR   GO; GO:0010842; P:retina layer formation; ISS:UniProtKB.
DR   GO; GO:0072050; P:S-shaped body morphogenesis; ISS:UniProtKB.
DR   GO; GO:0021527; P:spinal cord association neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0021522; P:spinal cord motor neuron differentiation; IEP:UniProtKB.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
DR   GO; GO:0001655; P:urogenital system development; ISS:UniProtKB.
DR   GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR001781; Znf_LIM.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF00412; LIM; 2.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00132; LIM; 2.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE   2: Evidence at transcript level;
KW   DNA-binding; Homeobox; LIM domain; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Zinc.
FT   CHAIN           1..406
FT                   /note="LIM/homeobox protein Lhx1"
FT                   /id="PRO_0000075775"
FT   DOMAIN          4..54
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          63..117
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DNA_BIND        180..239
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          125..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   406 AA;  44845 MW;  DF1B7BF1F32B9056 CRC64;
     MVHCAGCKRP ILDRFLLNVL DRAWHVKCVQ CCECKCNLTE KCFSREGKLY CKNDFFRCFG
     TKCAGCAQGI SPSDLVRRAR SKVFHLNCFT CMMCNKQLST GEELYIIDEN KFVCKEDYLN
     NSNTAKENSL HSATTGSDPS LSPDSQDPSQ DDAKDSESAN VSDKETGSNE NDDQNLGAKR
     RGPRTTIKAK QLETLKAAFA ATPKPTRHIR EQLAQETGLN MRVIQVWFQN RRSKERRMKQ
     LSALGARRHA FFRSPRRMRP LVDRLEPGEL LPNGPFSFYG DYQSEYYGPG ANYEFFPQGP
     PSSQAQTPVE LPFGAAGGPP GTPLGALEHP LPGHHPPGEA QRFPDMLAHP AGDSPSPEPT
     LPGSLHSMSA EVFGPSPPFS SISVNGGANY GNHLSHPPEM NEAAVW
 
 
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