EGAL1_CAEEL
ID EGAL1_CAEEL Reviewed; 574 AA.
AC Q17902; Q65ZH5;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Egalitarian protein homolog {ECO:0000312|WormBase:C10G6.1a};
GN Name=egal-1 {ECO:0000303|PubMed:20005871, ECO:0000312|WormBase:C10G6.1a};
GN ORFNames=C10G6.1 {ECO:0000312|WormBase:C10G6.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH BICD-1 AND DLC-1, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20005871; DOI=10.1016/j.ydbio.2009.12.004;
RA Fridolfsson H.N., Ly N., Meyerzon M., Starr D.A.;
RT "UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope
RT during nuclear migration.";
RL Dev. Biol. 338:237-250(2010).
CC -!- FUNCTION: Part of a complex with bicd-1 and dlc-1, which is recruited
CC to the nuclear envelope by unc-83, where in turn, it recruits dynein to
CC the nuclear surface and regulates nuclear migration in hypodermal
CC precursor cells. {ECO:0000269|PubMed:20005871}.
CC -!- SUBUNIT: Component of a dynein-regulating complex composed of at least
CC bicd-1, dlc-1 and egal-1. {ECO:0000269|PubMed:20005871}.
CC -!- INTERACTION:
CC Q17902; V6CJ04: bicd-1; NbExp=2; IntAct=EBI-328330, EBI-2006416;
CC Q17902; Q22799: dlc-1; NbExp=5; IntAct=EBI-328330, EBI-328324;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000305|PubMed:20005871}.
CC Note=Probably recruited to the nuclear envelope by unc-83.
CC {ECO:0000305|PubMed:20005871}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C10G6.1a};
CC IsoId=Q17902-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C10G6.1b};
CC IsoId=Q17902-2; Sequence=VSP_059366;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in animals that
CC are viable. However, animals display a small, but significant, defect
CC in nuclear migrations in hyp7 hypodermal precursor cells where an
CC average of 3%, and up to 21% in a single animal, of nuclei fail to
CC migrate. {ECO:0000269|PubMed:20005871}.
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DR EMBL; BX284604; CCD63389.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD63390.1; -; Genomic_DNA.
DR PIR; T29937; T29937.
DR RefSeq; NP_001021323.1; NM_001026152.3. [Q17902-1]
DR RefSeq; NP_001021324.1; NM_001026153.2. [Q17902-2]
DR AlphaFoldDB; Q17902; -.
DR SMR; Q17902; -.
DR ComplexPortal; CPX-1388; bicd-1-dlc-1-egal-1 microtubule-associated dynein motor complex.
DR DIP; DIP-26632N; -.
DR IntAct; Q17902; 2.
DR STRING; 6239.C10G6.1a.2; -.
DR EPD; Q17902; -.
DR PaxDb; Q17902; -.
DR PeptideAtlas; Q17902; -.
DR EnsemblMetazoa; C10G6.1a.1; C10G6.1a.1; WBGene00015680. [Q17902-1]
DR EnsemblMetazoa; C10G6.1b.1; C10G6.1b.1; WBGene00015680. [Q17902-2]
DR GeneID; 177352; -.
DR KEGG; cel:CELE_C10G6.1; -.
DR UCSC; C10G6.1b.1; c. elegans.
DR CTD; 177352; -.
DR WormBase; C10G6.1a; CE27677; WBGene00015680; egal-1. [Q17902-1]
DR WormBase; C10G6.1b; CE37193; WBGene00015680; egal-1. [Q17902-2]
DR eggNOG; KOG2405; Eukaryota.
DR GeneTree; ENSGT00390000003581; -.
DR HOGENOM; CLU_008186_0_0_1; -.
DR InParanoid; Q17902; -.
DR OMA; MEYEMAR; -.
DR OrthoDB; 640164at2759; -.
DR PRO; PR:Q17902; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00015680; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005875; C:microtubule associated complex; IC:ComplexPortal.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:1990923; C:PET complex; IBA:GO_Central.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0031047; P:gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0030473; P:nuclear migration along microtubule; IC:ComplexPortal.
DR GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome.
FT CHAIN 1..574
FT /note="Egalitarian protein homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000443515"
FT DOMAIN 312..414
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000255"
FT REGION 259..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 498..502
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059366"
SQ SEQUENCE 574 AA; 64842 MW; F9EB08582F3FA5FF CRC64;
MEEAKNMALL FFMDHLMQKN GRRTIHDLSC QFGARGFSEE MRNAVGTTQE GLTEFLQGHP
SLFTVEGDQV ILNGHNDLNA KNNPLLQSGI RSRNYEKEAV DFFVTKLTKF GPELQIKSLL
GHRSQAAPEV RLVSGRHLKE FCEFLQSQVD YFVVEGDRVR LKNMPEPDEN AIEMDDEGRP
LAGVKAKQAA VEYLKSVLEQ NEDQPIPLDQ FYQNFCQRFS HTIRQDVATN PKELLQFLKL
NRGLFFIRSN KVSLVKNRLN EDGSENGSDE GEETNNNGMF PLDQSALTRI HFVKALKPAQ
DLISRLWQDI NNMEKKVVGL DLKTVTVGVD GEIFLSLGVI ATTSQIGIFD LASSDVIILE
SGFKGILESE KVVKVIHDAR RVASLLAHKY AVHMRNVFDT QVAHSLLQHE KFNKSLNEMR
PISFINLQRV YYPQSIMLSD VTPRKMSMCP NWGVRPITEE FQLTIVEEAH CLLSALYQSL
SNLIPVHLRG VFEDKCIEVN HPEVLLASPN RPPPQPFISS PYRASTRRDV RNGGSIMQSF
SPAPYAAAPR PQMSDACTQT FSTGDIEVLN VFYE
