MIG39_CAEEL
ID MIG39_CAEEL Reviewed; 943 AA.
AC P34418;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Zinc finger BED domain-containing protein 39 {ECO:0000303|PubMed:25446539};
DE AltName: Full=Abnormal cell migration protein 39 {ECO:0000312|WormBase:F42H10.5a};
GN Name=mig-39 {ECO:0000312|WormBase:F42H10.5a};
GN ORFNames=F42H10.5 {ECO:0000312|WormBase:F42H10.5a};
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=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-231.
RX PubMed=25446539; DOI=10.1016/j.ydbio.2014.10.008;
RA Kikuchi T., Shibata Y., Kim H.S., Kubota Y., Yoshina S., Mitani S.,
RA Nishiwaki K.;
RT "The BED finger domain protein MIG-39 halts migration of distal tip cells
RT in Caenorhabditis elegans.";
RL Dev. Biol. 397:151-161(2015).
CC -!- FUNCTION: Regulates the timing and orientation of distal tip cell
CC migration during gonadal development. May act in parallel to cacn-1 and
CC Rac GTPases to control the anterior and posterior migration of distal
CC tip cells. {ECO:0000269|PubMed:25446539}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25446539}. Cytoplasm
CC {ECO:0000269|PubMed:25446539}. Note=Expressed in the nucleus of distal
CC tip cells and in the cytoplasm of germ cells. Localized to the
CC peripheral chromatin region of the nucleus.
CC {ECO:0000269|PubMed:25446539}.
CC -!- TISSUE SPECIFICITY: Expressed in distal tip cells and in germline
CC cells. {ECO:0000269|PubMed:25446539}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the nucleus of distal tip cells until
CC larval stage L4 when expression decreases onwards to late adulthood.
CC {ECO:0000269|PubMed:25446539}.
CC -!- DISRUPTION PHENOTYPE: Defective cessation of distal tip cell migration
CC from the dorsal muscle towards the mid-body during gonadal development.
CC RNAi-mediated knockdown of cacn-1 in mig-39 null animals results in a
CC strong overshoot phenotype in which anterior and posterior distal tip
CC cells. RNAi-mediated knockdown of Rac GTPase, Rac-2, in double mig-39
CC and either ced-10 or mig-2 (which are also Rac GTPases) null animals,
CC suppresses the overshoot phenotype in mig-39 null animals.
CC {ECO:0000269|PubMed:25446539}.
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; FO080327; CCD62889.1; -; Genomic_DNA.
DR PIR; S44653; S44653.
DR RefSeq; NP_498871.3; NM_066470.4.
DR AlphaFoldDB; P34418; -.
DR BioGRID; 50446; 5.
DR IntAct; P34418; 4.
DR STRING; 6239.F42H10.5.2; -.
DR EPD; P34418; -.
DR PaxDb; P34418; -.
DR PeptideAtlas; P34418; -.
DR EnsemblMetazoa; F42H10.5a.1; F42H10.5a.1; WBGene00018369.
DR EnsemblMetazoa; F42H10.5a.2; F42H10.5a.2; WBGene00018369.
DR EnsemblMetazoa; F42H10.5a.3; F42H10.5a.3; WBGene00018369.
DR GeneID; 185686; -.
DR KEGG; cel:CELE_F42H10.5; -.
DR UCSC; F42H10.5; c. elegans.
DR CTD; 185686; -.
DR WormBase; F42H10.5a; CE44927; WBGene00018369; mig-39.
DR eggNOG; KOG1121; Eukaryota.
DR HOGENOM; CLU_298478_0_0_1; -.
DR InParanoid; P34418; -.
DR OMA; PRMLEPY; -.
DR OrthoDB; 320294at2759; -.
DR PRO; PR:P34418; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00018369; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; P34418; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IMP:WormBase.
DR GO; GO:0005634; C:nucleus; IMP:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:1903355; P:negative regulation of distal tip cell migration; IMP:WormBase.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..943
FT /note="Zinc finger BED domain-containing protein 39"
FT /evidence="ECO:0000305"
FT /id="PRO_0000065336"
FT ZN_FING 184..235
FT /note="BED-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 231
FT /note="E->K: In tk102; defective cessation of distal tip
FT cell migration during gonadal development."
FT /evidence="ECO:0000269|PubMed:25446539"
SQ SEQUENCE 943 AA; 102999 MW; 3ED8D36211EE8CB8 CRC64;
MSSVSSDIDG PPETKRFRID VDTQVGIDTP SVSTNCAPPV AGEASQDGQS PAAPSSASYR
SSNSSVISSS ESPIKDEDVD VHDGQDDTED IAMDVSGSTG SIVNNSEIFE MLNKTFGGVF
NCDLEGIMRP SALMHPSSPP TPIQSAGIPG ALAVAQSPAA QLFSGDDWSW HRNPAASIRS
GGTNKQTPVW KYFVYNKTEN LSRCIVGDCT YMLKGPHTST LACHLKKHTR EYSEFQKLKT
EYSRTKLDQQ PKIPDGAPHP LTLQTQNTPR QTGSPASTCN TNSNTSSSVS SGSGIGSGSG
STMDLSMKKP KKEPSSAKLN EMLFNGLRQA TNNSNGSPPT TPHAPQLPNI PSFVTNMMLQ
MNPLHMMLAQ SLPGATPPTP TSSNAGLNAL QQAGLTLAAN GQIIQSKKWR NDDKKQKELC
TKFALALATS HVDFEVVQNP LWKEVFEMAQ PKFSIPTESQ YEHIVNSTSH KLIQSLKSQL
SASKKLNLLL DITKITADIS RVTVSVALTG GAGNSYETQV ILLAFRNING NQSEDLTAVF
EKVLQDYNIS PSSINRVICS GLNELAEPAE LPKQMDSFSS RLANCFKSWL ETSPTVEVLK
KNVYAMLVSY LTVPAAIQLA SQMLKAKFEV PLTEPFHVIV EHLVAHRDIY QMNMEGITLI
SEREWNKVTG IHHLMNIFKP FMTYSTDMTT VDTVIPTIVQ IQNVLEKDIY HLGDIGSDLL
TSLKQTVAPI MNPEHENFDS TYIQATALNP QLAVTLTSDQ MTTAKSLIET EISRRTKKMR
KAQSDKKLAM GVDSLLANVM RKNDGGSDGG CETALAIYGD LFQSITGNSS ESKENIVNQY
FDEISSTTSV ESMFMLRTFG NPMQAPLSYW KSCSSRCSEL SDLATELLSI PIFTLTAERV
LSFSPDSSSL NTNLILTNLD STDQFEKQVL LRFNRQIVSK LFN