HBL1_CAEEL
ID HBL1_CAEEL Reviewed; 982 AA.
AC Q9XYD3; Q19389;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Hunchback-like protein;
GN Name=hbl-1 {ECO:0000312|WormBase:F13D11.2a};
GN Synonyms=lin-57 {ECO:0000312|WormBase:F13D11.2a};
GN ORFNames=F13D11.2 {ECO:0000312|WormBase:F13D11.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=9917360; DOI=10.1006/dbio.1998.9096;
RA Fay D.S., Stanley H.M., Han M., Wood W.B.;
RT "A Caenorhabditis elegans homologue of hunchback is required for late
RT stages of development but not early embryonic patterning.";
RL Dev. Biol. 205:240-253(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21471153; DOI=10.1242/dev.057109;
RA Huang X., Zhang H., Zhang H.;
RT "The zinc-finger protein SEA-2 regulates larval developmental timing and
RT adult lifespan in C. elegans.";
RL Development 138:2059-2068(2011).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF LEU-83.
RX PubMed=28933985; DOI=10.1080/15384101.2017.1344798;
RA Metheetrairut C., Ahuja Y., Slack F.J.;
RT "acn-1, a C. elegans homologue of ACE, genetically interacts with the let-7
RT microRNA and other heterochronic genes.";
RL Cell Cycle 16:1800-1809(2017).
CC -!- FUNCTION: Required for the late stages of development (PubMed:9917360).
CC Plays a role in the developmental timing of postembryonic hypodermal
CC seam cell fusion events and adult alae production (PubMed:28933985,
CC PubMed:21471153). {ECO:0000269|PubMed:21471153,
CC ECO:0000269|PubMed:28933985, ECO:0000269|PubMed:9917360}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed primarily in ectodermal cells during
CC embryonic and larval development.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in premature alae
CC formation at the L3 larval stage (PubMed:21471153). This phenotype is
CC partially suppressed in a sea-2 bp283 mutant background
CC (PubMed:21471153). {ECO:0000269|PubMed:21471153}.
CC -!- SIMILARITY: Belongs to the hunchback C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF097737; AAD16170.1; -; mRNA.
DR EMBL; BX284606; CCD69456.1; -; Genomic_DNA.
DR PIR; T16057; T16057.
DR PIR; T43676; T43676.
DR RefSeq; NP_001041243.1; NM_001047778.3.
DR AlphaFoldDB; Q9XYD3; -.
DR BioGRID; 45781; 2.
DR STRING; 6239.F13D11.2a; -.
DR EPD; Q9XYD3; -.
DR PaxDb; Q9XYD3; -.
DR EnsemblMetazoa; F13D11.2a.1; F13D11.2a.1; WBGene00001824.
DR GeneID; 180848; -.
DR KEGG; cel:CELE_F13D11.2; -.
DR UCSC; F13D11.2a; c. elegans.
DR CTD; 180848; -.
DR WormBase; F13D11.2a; CE27956; WBGene00001824; hbl-1.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000171732; -.
DR InParanoid; Q9XYD3; -.
DR OMA; HLEYHYR; -.
DR OrthoDB; 476235at2759; -.
DR PhylomeDB; Q9XYD3; -.
DR PRO; PR:Q9XYD3; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001824; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q9XYD3; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0019538; P:protein metabolic process; IMP:WormBase.
DR GO; GO:0040034; P:regulation of development, heterochronic; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR027742; Hunchback.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24392:SF33; PTHR24392:SF33; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..982
FT /note="Hunchback-like protein"
FT /id="PRO_0000046984"
FT ZN_FING 336..358
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 361..384
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 538..560
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 567..589
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 595..617
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 623..647
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 734..756
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 929..951
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 957..981
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 87..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 83
FT /note="L->M: In mg285; causes precocious hypodermal seam
FT cell fusion and adult alae production in larval stages L3
FT and L4."
FT /evidence="ECO:0000269|PubMed:28933985"
SQ SEQUENCE 982 AA; 106952 MW; 49812554CF3CE30F CRC64;
MVQSDSPEEL AQRAKPAWRL QQMPVQLSNF VSKTPLIGSE WPPTGDWRSA NNNSLGDWNK
CCVPGSEIPQ HLGPFGNSSL TMLTAQQPGE KIHPDGGYVS PKEDGRKSSE HTNSYDVSAS
QSPSNDGAQS DSTSDEHIDV ECMTETEMDT DEKDSTIKPE DQATPKLEEG SDSKPESTSV
EGTSSNYQVT SEPVQMPQMP IPVIPSFLKN SLPAPIPITP TQSANVERSN SPSIEEALLL
TLSQQQFAEV FAEAAKIRKS SSESIGFQRS GTSAFLNIEP KEMSMSSANN NNEEAPASTV
SACSTPTTTT SASFCRPPGL GPVALPPTQN GQTPMLVCPI CGFMCPSKFH FNSHMNTHGD
HQCSMCDYTS RTEGRLKKHM RESHTVEEQL RAGFESEPAK ESASSPKNLS LSKDGSATSP
INEIFNLSTT MASILDSTNN AVSSTSTTEQ PSALSALTLD MSSTPSLLST LAHSSFGVSA
LDQIKAISEN PSFMPEGGIN LASALGVVSN AIKGDTPSPE KQSNGECRRS SSGKIKIFKC
KQCGHQSLSK DDQWAHARTH IPAEKQLNCQ HCNFVTEYKH HLEYHYRNHI GSKPFQCKKC
AYNCVNKSML NSHMKSHTNH YQFRCMDCTY ATKYCHSLKL HLKKYNHRRV PEGIEMSGGD
SSPPFTSDAT ITFSPLMKQE IKTETVEPVT SIAQPFPFNP MMGNHGLNFA NHMLLNKHLD
VGLMGLRNSV MSPLKCSACD FVASSADEKM RHSMSHILNS SNVPTSIASL YNSLNLPSFS
HVAPDNDNAL ESMDCDVKID DDNITESHCY EEMDQGSDSA VSPTGSSQIS SGDEETKKCK
SLSLEQISAR ANGNNSPMSN DSAMEKDGES ADDAPHSPSD TTSVPSPPLH SSSIVAPIPI
TPQPNEFLQS ILAQASLLGP LLANRPSAFY CDHCKIPFDT QQVLDSHMRF HTPGNPFMCS
DCQYQAFNEL SFALHMYQAR HQ
