LIN11_CAEEL
ID LIN11_CAEEL Reviewed; 405 AA.
AC P20154;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein lin-11;
DE AltName: Full=Abnormal cell lineage protein 11;
GN Name=lin-11; ORFNames=ZC247.3;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-405, AND FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=1970421; DOI=10.1038/344876a0;
RA Freyd G., Kim S.K., Horvitz H.R.;
RT "Novel cysteine-rich motif and homeodomain in the product of the
RT Caenorhabditis elegans cell lineage gene lin-11.";
RL Nature 344:876-879(1990).
RN [3]
RP CHARACTERIZATION OF LIM DOMAIN METAL-BINDING.
RX PubMed=1924383; DOI=10.1073/pnas.88.20.9210;
RA Li P.M., Reichert J., Freyd G., Horvitz H.R., Walsh C.T.;
RT "The LIM region of a presumptive Caenorhabditis elegans transcription
RT factor is an iron-sulfur- and zinc-containing metallodomain.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9210-9213(1991).
RN [4]
RP FUNCTION, AND SUMOYLATION AT LYS-17 AND LYS-18.
RX PubMed=15466489; DOI=10.1101/gad.1227104;
RA Broday L., Kolotuev I., Didier C., Bhoumik A., Gupta B.P., Sternberg P.W.,
RA Podbilewicz B., Ronai Z.;
RT "The small ubiquitin-like modifier (SUMO) is required for gonadal and
RT uterine-vulval morphogenesis in Caenorhabditis elegans.";
RL Genes Dev. 18:2380-2391(2004).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19561603; DOI=10.1038/nn.2347;
RA Hayashi Y., Hirotsu T., Iwata R., Kage-Nakadai E., Kunitomo H.,
RA Ishihara T., Iino Y., Kubo T.;
RT "A trophic role for Wnt-Ror kinase signaling during developmental pruning
RT in Caenorhabditis elegans.";
RL Nat. Neurosci. 12:981-987(2009).
RN [6]
RP FUNCTION.
RX PubMed=29672507; DOI=10.1371/journal.pbio.2004979;
RA Masoudi N., Tavazoie S., Glenwinkel L., Ryu L., Kim K., Hobert O.;
RT "Unconventional function of an Achaete-Scute homolog as a terminal selector
RT of nociceptive neuron identity.";
RL PLoS Biol. 16:E2004979-E2004979(2018).
CC -!- FUNCTION: Probable transcription factor which is required for
CC asymmetric division of vulval blast cells (PubMed:1970421,
CC PubMed:15466489). Involved in olfactory plasticity probably by
CC regulating the expression of transcription factor mbr-1 in RIF neurons
CC (PubMed:19561603). Plays a role in the chemorepulsive response toward
CC ascaroside pheromones mediated by the ADL sensory neurons, probably by
CC regulating E-box motif 5'-CANNTG-3' containing target genes in the ADL
CC neurons (PubMed:29672507). Plays a role in the differentiation of the
CC ADL sensory neurons (PubMed:29672507). {ECO:0000269|PubMed:15466489,
CC ECO:0000269|PubMed:19561603, ECO:0000269|PubMed:1970421,
CC ECO:0000269|PubMed:29672507}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in ADL, AVJL, AIZL, RICL, RIF and AVG
CC neurons. {ECO:0000269|PubMed:19561603}.
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DR EMBL; Z80221; CAB02310.1; -; Genomic_DNA.
DR EMBL; X54355; CAA38240.1; -; mRNA.
DR PIR; T27509; T27509.
DR RefSeq; NP_492696.1; NM_060295.4.
DR AlphaFoldDB; P20154; -.
DR SMR; P20154; -.
DR BioGRID; 38311; 29.
DR IntAct; P20154; 26.
DR STRING; 6239.ZC247.3; -.
DR PaxDb; P20154; -.
DR PeptideAtlas; P20154; -.
DR PRIDE; P20154; -.
DR EnsemblMetazoa; ZC247.3.1; ZC247.3.1; WBGene00003000.
DR GeneID; 172893; -.
DR KEGG; cel:CELE_ZC247.3; -.
DR UCSC; ZC247.3; c. elegans.
DR CTD; 172893; -.
DR WormBase; ZC247.3; CE15150; WBGene00003000; lin-11.
DR eggNOG; KOG0490; Eukaryota.
DR GeneTree; ENSGT00940000164085; -.
DR HOGENOM; CLU_662657_0_0_1; -.
DR InParanoid; P20154; -.
DR OMA; NDQQFYP; -.
DR OrthoDB; 813697at2759; -.
DR PhylomeDB; P20154; -.
DR SignaLink; P20154; -.
DR PRO; PR:P20154; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003000; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007413; P:axonal fasciculation; IMP:WormBase.
DR GO; GO:0001708; P:cell fate specification; IMP:WormBase.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0040026; P:positive regulation of vulval development; IMP:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Homeobox; Isopeptide bond; LIM domain;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..405
FT /note="Protein lin-11"
FT /id="PRO_0000075814"
FT DOMAIN 68..124
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 127..187
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DNA_BIND 241..300
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 189..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000305"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 45777 MW; F9B507780079B442 CRC64;
MHSSSSFIIT SLEEEEKKPP AHHLHQQSIE DVGSVTSSAT LLLLDSATWM MPSSTTQPHI
SEISGNECAA CAQPILDRYV FTVLGKCWHQ SCLRCCDCRA PMSMTCFSRD GLILCKTDFS
RRYSQRCAGC DGKLEKEDLV RRARDKVFHI RCFQCSVCQR LLDTGDQLYI MEGNRFVCQS
DFQTATKTST PTSIHRPVSN GSECNSDVEE DNVDACDEVG LDDGEGDCGK DNSDDSNSAK
RRGPRTTIKA KQLETLKNAF AATPKPTRHI REQLAAETGL NMRVIQVWFQ NRRSKERRMK
QLRFGGYRQS RRPRRDDIVD MFPNDQQFYP PPPPSNVQFF CDPYTTSPNN PETIQMAPQF
AVPTENMNMV PEPYTEQSAT PPEFNEDTFA CIYSTDLGKP TPVSW
