XOL1_CAEEL
ID XOL1_CAEEL Reviewed; 417 AA.
AC Q23229; Q18064; Q23230; Q23231; Q7JP92;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=XO lethal protein 1;
GN Name=xol-1 {ECO:0000312|WormBase:C18A11.5b};
GN ORFNames=C18A11.5 {ECO:0000312|WormBase:C18A11.5b};
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 [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS B AND C),
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=7813020; DOI=10.1016/0092-8674(95)90452-2;
RA Rhind N.R., Miller L.M., Kopczynski J.B., Meyer B.J.;
RT "xol-1 acts as an early switch in the C. elegans male/hermaphrodite
RT decision.";
RL Cell 80:71-82(1995).
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.
RX PubMed=3167975; DOI=10.1016/0092-8674(88)90019-0;
RA Miller L.M., Plenefisch J.D., Casson L.P., Meyer B.J.;
RT "xol-1: a gene that controls the male modes of both sex determination and X
RT chromosome dosage compensation in C. elegans.";
RL Cell 55:167-183(1988).
RN [4]
RP INDUCTION.
RX PubMed=7821230; DOI=10.1242/dev.120.12.3681;
RA Hodgkin J., Zellan J.D., Albertson D.G.;
RT "Identification of a candidate primary sex determination locus, fox-1, on
RT the X chromosome of Caenorhabditis elegans.";
RL Development 120:3681-3689(1994).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=9217163; DOI=10.1038/40669;
RA Nicoll M., Akerib C.C., Meyer B.J.;
RT "X-chromosome-counting mechanisms that determine nematode sex.";
RL Nature 388:200-204(1997).
RN [6]
RP INDUCTION.
RX PubMed=9927456; DOI=10.1093/genetics/151.2.617;
RA Skipper M., Milne C.A., Hodgkin J.;
RT "Genetic and molecular analysis of fox-1, a numerator element involved in
RT Caenorhabditis elegans primary sex determination.";
RL Genetics 151:617-631(1999).
RN [7]
RP INDUCTION.
RX PubMed=9823896; DOI=10.1038/24164;
RA Carmi I., Kopczynski J.B., Meyer B.J.;
RT "The nuclear hormone receptor SEX-1 is an X-chromosome signal that
RT determines nematode sex.";
RL Nature 396:168-173(1998).
RN [8]
RP FUNCTION.
RX PubMed=33372658; DOI=10.7554/elife.62963;
RA Farboud B., Novak C.S., Nicoll M., Quiogue A., Meyer B.J.;
RT "Dose-dependent action of the RNA binding protein FOX-1 to relay X-
RT chromosome number and determine C. elegans sex.";
RL Elife 9:0-0(2020).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), AND LACK OF ATP-BINDING.
RX PubMed=12672694; DOI=10.1101/gad.1082303;
RA Luz J.G., Hassig C.A., Pickle C., Godzik A., Meyer B.J., Wilson I.A.;
RT "XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase
RT family member and a structural prototype for a class of developmental
RT regulators.";
RL Genes Dev. 17:977-990(2003).
CC -!- FUNCTION: Sex-determining factor that is required for sexual
CC differentiation and X chromosome dosage compensation to promote male
CC development (PubMed:7813020, PubMed:9217163, PubMed:33372658). High
CC expression during gastrulation triggers male development, while low
CC expression at that time triggers hermaphrodite development. Although
CC related to GHMP kinase, its mode of action remains unclear.
CC {ECO:0000269|PubMed:3167975, ECO:0000269|PubMed:33372658,
CC ECO:0000269|PubMed:7813020, ECO:0000269|PubMed:9217163}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7813020}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:C18A11.5b};
CC IsoId=Q23229-1; Sequence=Displayed;
CC Name=c {ECO:0000312|WormBase:C18A11.5c};
CC IsoId=Q23229-3; Sequence=VSP_016414;
CC -!- DEVELOPMENTAL STAGE: Specifically expressed at high levels in pre-comma
CC stage XO embryos. Also present at low levels throughout other larval
CC stages in XO animals, but are nearly undetectable in XX larvae and
CC adults of both sexes. {ECO:0000269|PubMed:7813020}.
CC -!- DEVELOPMENTAL STAGE: [Isoform b]: Most abundant in male embryos
CC (PubMed:33372658). Expressed at low levels in hermaphrodite embryos
CC (PubMed:33372658). {ECO:0000269|PubMed:33372658}.
CC -!- INDUCTION: Down-regulated by at least 4 X-linked genes, termed X-signal
CC elements including fox-1 and sex-1 (PubMed:9217163). High levels of
CC xol-1 in males correlate with low sdc-2 expression, preventing dosage
CC compensation. Conversely, low levels of xol-1 in hermaphrodites
CC correlate with high sdc-2 expression and the assembly of the dosage
CC compensation complex on the X chromosome. {ECO:0000269|PubMed:7821230,
CC ECO:0000269|PubMed:9217163, ECO:0000269|PubMed:9823896,
CC ECO:0000269|PubMed:9927456}.
CC -!- DISRUPTION PHENOTYPE: Worms are XO-lethal, due to inappropriate
CC activating dosage compensation where only 1 X chromosome is present. In
CC contrast xol-1 overexpression is XX-lethal, deactivating the dosage
CC compensation pathway and elevating the expression of X chromosome genes
CC to lethal levels in hermaphrodites. {ECO:0000269|PubMed:7813020}.
CC -!- MISCELLANEOUS: [Isoform b]: Only functional isoform (PubMed:33372658).
CC Produced by alternative splicing of intron 6 which results in the
CC deletion of intron 6 and retention of exon 7 coding sequences
CC (PubMed:33372658). {ECO:0000269|PubMed:33372658}.
CC -!- MISCELLANEOUS: [Isoform c]: Inactive isoform (PubMed:7813020,
CC PubMed:33372658). Produced by alternative splicing of intron 6 which
CC results in the retention of intron 6 and deletion of exon 7 coding
CC sequences (PubMed:33372658). An in-frame UAA stop codon within intron 6
CC prematurely terminates translation (PubMed:7813020). Intron 6 retention
CC and exon 7 deletion can also be due to use of an alternative 3' splice
CC acceptor site in the 3'UTR resulting in trans-splicing to the
CC transcripts of unrelated genes (PubMed:33372658).
CC {ECO:0000269|PubMed:33372658, ECO:0000269|PubMed:7813020}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Xol-1 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although clearly related the GHMP kinase family as
CC demonstrated by the 3D-structure, it lacks many conserved feature of
CC GHMP kinases and probably does not bind ATP, suggesting that it
CC probably does not have kinase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67048.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L35129; AAA67048.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L35129; AAA67049.1; -; Genomic_DNA.
DR EMBL; L35129; AAA67047.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD65063.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD65064.1; -; Genomic_DNA.
DR PIR; A55473; A55473.
DR PIR; B55473; B55473.
DR PIR; C55473; C55473.
DR PIR; F89581; F89581.
DR RefSeq; NP_001024418.1; NM_001029247.1. [Q23229-1]
DR RefSeq; NP_001024419.1; NM_001029248.1. [Q23229-3]
DR PDB; 1MG7; X-ray; 1.55 A; A/B=1-417.
DR PDBsum; 1MG7; -.
DR AlphaFoldDB; Q23229; -.
DR SMR; Q23229; -.
DR STRING; 6239.C18A11.5c; -.
DR PaxDb; Q23229; -.
DR EnsemblMetazoa; C18A11.5b.1; C18A11.5b.1; WBGene00006962. [Q23229-1]
DR EnsemblMetazoa; C18A11.5c.1; C18A11.5c.1; WBGene00006962. [Q23229-3]
DR GeneID; 181061; -.
DR KEGG; cel:CELE_C18A11.5; -.
DR UCSC; C18A11.5c; c. elegans. [Q23229-1]
DR CTD; 181061; -.
DR WormBase; C18A11.5b; CE35709; WBGene00006962; xol-1. [Q23229-1]
DR WormBase; C18A11.5c; CE24807; WBGene00006962; xol-1. [Q23229-3]
DR eggNOG; ENOG502TITU; Eukaryota.
DR HOGENOM; CLU_659271_0_0_1; -.
DR InParanoid; Q23229; -.
DR OMA; MEEDSIW; -.
DR OrthoDB; 1822677at2759; -.
DR EvolutionaryTrace; Q23229; -.
DR PRO; PR:Q23229; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006962; Expressed in embryo and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0042464; P:dosage compensation by hypoactivation of X chromosome; IMP:UniProtKB.
DR GO; GO:0000366; P:intergenic mRNA trans splicing; IDA:UniProtKB.
DR GO; GO:0030238; P:male sex determination; IMP:UniProtKB.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR015193; Xol-1_GHMP-like.
DR InterPro; IPR015192; Xol-1_N.
DR Pfam; PF09109; Xol-1_GHMP-like; 1.
DR Pfam; PF09108; Xol-1_N; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; Differentiation;
KW Nucleus; Reference proteome.
FT CHAIN 1..417
FT /note="XO lethal protein 1"
FT /id="PRO_0000156673"
FT REGION 373..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..417
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 323..417
FT /note="IAIATESRQSVSSVSFDLLKLGPGASLVTLANSRRFEPECRVVLQIEVKPVS
FT PGETSSEGISDEHHYEEYDEDDIMEEEEAPSARQDDTYDEDEE -> YSAQYYLSMTHF
FT SNRISIPLFSSLVFLTVSIVINAMCHKSIFCKRVISRLPFPHCQILKLSHFSTGRTFLS
FT YLSIIAKCTPISHINQSNILPAQNKIFAIKQFS (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_016414"
FT CONFLICT 323..417
FT /note="IAIATESRQSVSSVSFDLLKLGPGASLVTLANSRRFEPECRVVLQIEVKPVS
FT PGETSSEGISDEHHYEEYDEDDIMEEEEAPSARQDDTYDEDEE -> VSYHIICYFHIN
FT CMFDKTLFTKIFCSHIVFTSR (in Ref. 1; AAA67048)"
FT /evidence="ECO:0000305"
FT STRAND 9..21
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:1MG7"
FT STRAND 40..50
FT /evidence="ECO:0007829|PDB:1MG7"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1MG7"
FT STRAND 54..72
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1MG7"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:1MG7"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:1MG7"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:1MG7"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 229..241
FT /evidence="ECO:0007829|PDB:1MG7"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 274..289
FT /evidence="ECO:0007829|PDB:1MG7"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:1MG7"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:1MG7"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:1MG7"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:1MG7"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:1MG7"
FT STRAND 361..372
FT /evidence="ECO:0007829|PDB:1MG7"
SQ SEQUENCE 417 AA; 47159 MW; 364FE008D91C8662 CRC64;
MQVEANSERR VKILGIDRSE NSPVLTYMET EDDPNFRNSK LAAAPHTVHM MDSGFLAINR
QCLVKGKAIL AREPKSSNEH MIDDLPKHAH DQHTLSILRD FIDQLKLHNV YEINFYDPLD
SSGKLAVIPM LIALWKCMLA SETDICDQEV LKSIMNSVIA KFELQIPCKN AVIDATLSGS
REEVHIIAED GSLENSNGTT EHFNKKHDLV FVKTDLHPED FTPQMFPSQA KAKLLRDAFN
NEEDEDTFPD ILVPAYMTAH SKNRVRQEDY TCLEVEFDSQ VALEKLMNEH EQVEGFEVQQ
GGILVALKKD SFFDDELIEK IAIAIATESR QSVSSVSFDL LKLGPGASLV TLANSRRFEP
ECRVVLQIEV KPVSPGETSS EGISDEHHYE EYDEDDIMEE EEAPSARQDD TYDEDEE
