SSL1_CAEEL
ID SSL1_CAEEL Reviewed; 2395 AA.
AC Q9NEL2; E0R7L4; E0R7L5; E0R7L6; Q6Q9H2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 4.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Helicase ssl-1;
DE EC=3.6.4.-;
DE AltName: Full=Swi/snf2-like protein 1;
GN Name=ssl-1; ORFNames=Y111B2A.22;
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] (ISOFORM A), AND FUNCTION.
RX PubMed=15068795; DOI=10.1016/s1534-5807(04)00065-6;
RA Ceol C.J., Horvitz H.R.;
RT "A new class of C. elegans synMuv genes implicates a Tip60/NuA4-like HAT
RT complex as a negative regulator of Ras signaling.";
RL Dev. Cell 6:563-576(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 DISRUPTION PHENOTYPE.
RX PubMed=17011494; DOI=10.1016/j.devcel.2006.07.015;
RA Grote P., Conradt B.;
RT "The PLZF-like protein TRA-4 cooperates with the Gli-like transcription
RT factor TRA-1 to promote female development in C. elegans.";
RL Dev. Cell 11:561-573(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17009877; DOI=10.1371/journal.pgen.0020161;
RA Updike D.L., Mango S.E.;
RT "Temporal regulation of foregut development by HTZ-1/H2A.Z and PHA-
RT 4/FoxA.";
RL PLoS Genet. 2:1500-1510(2006).
CC -!- FUNCTION: Probable catalytic component of a chromatin-remodeling
CC complex which mediates the ATP-dependent exchange of histone H2A
CC variant H2AV/htz-1 for H2A, leading to transcriptional regulation of
CC selected genes by chromatin remodeling. Involved in foregut
CC development, and may be involved in vulval development.
CC {ECO:0000269|PubMed:15068795, ECO:0000269|PubMed:17009877}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a;
CC IsoId=Q9NEL2-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9NEL2-2; Sequence=VSP_043687, VSP_043688;
CC Name=c;
CC IsoId=Q9NEL2-3; Sequence=VSP_043685;
CC Name=d;
CC IsoId=Q9NEL2-4; Sequence=VSP_043686;
CC -!- DISRUPTION PHENOTYPE: Defects in feminization. Embryonic arrest.
CC {ECO:0000269|PubMed:17009877, ECO:0000269|PubMed:17011494}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY551965; AAS65429.1; -; mRNA.
DR EMBL; AL132904; CAC35851.3; -; Genomic_DNA.
DR EMBL; AL132904; CBW48563.1; -; Genomic_DNA.
DR EMBL; AL132904; CBW48564.1; -; Genomic_DNA.
DR EMBL; AL132904; CBW48565.1; -; Genomic_DNA.
DR RefSeq; NP_001255179.1; NM_001268250.1. [Q9NEL2-1]
DR RefSeq; NP_001255180.1; NM_001268251.1. [Q9NEL2-2]
DR RefSeq; NP_001255181.1; NM_001268252.1.
DR RefSeq; NP_001255182.1; NM_001268253.1.
DR AlphaFoldDB; Q9NEL2; -.
DR SMR; Q9NEL2; -.
DR BioGRID; 55513; 11.
DR IntAct; Q9NEL2; 2.
DR MINT; Q9NEL2; -.
DR STRING; 6239.Y111B2A.22a; -.
DR EPD; Q9NEL2; -.
DR PaxDb; Q9NEL2; -.
DR PeptideAtlas; Q9NEL2; -.
DR PRIDE; Q9NEL2; -.
DR EnsemblMetazoa; Y111B2A.22a.1; Y111B2A.22a.1; WBGene00007027. [Q9NEL2-1]
DR EnsemblMetazoa; Y111B2A.22b.1; Y111B2A.22b.1; WBGene00007027. [Q9NEL2-2]
DR EnsemblMetazoa; Y111B2A.22c.1; Y111B2A.22c.1; WBGene00007027. [Q9NEL2-3]
DR EnsemblMetazoa; Y111B2A.22d.1; Y111B2A.22d.1; WBGene00007027. [Q9NEL2-4]
DR GeneID; 190954; -.
DR KEGG; cel:CELE_Y111B2A.22; -.
DR UCSC; Y111B2A.22; c. elegans. [Q9NEL2-1]
DR CTD; 190954; -.
DR WormBase; Y111B2A.22a; CE40241; WBGene00007027; ssl-1. [Q9NEL2-1]
DR WormBase; Y111B2A.22b; CE45331; WBGene00007027; ssl-1. [Q9NEL2-2]
DR WormBase; Y111B2A.22c; CE45313; WBGene00007027; ssl-1. [Q9NEL2-3]
DR WormBase; Y111B2A.22d; CE45363; WBGene00007027; ssl-1. [Q9NEL2-4]
DR eggNOG; KOG0391; Eukaryota.
DR GeneTree; ENSGT00940000167340; -.
DR HOGENOM; CLU_000982_0_0_1; -.
DR InParanoid; Q9NEL2; -.
DR OMA; KSANEGM; -.
DR OrthoDB; 188211at2759; -.
DR PhylomeDB; Q9NEL2; -.
DR PRO; PR:Q9NEL2; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00007027; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0009996; P:negative regulation of cell fate specification; IMP:UniProtKB.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Chromatin regulator; Coiled coil;
KW Developmental protein; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..2395
FT /note="Helicase ssl-1"
FT /id="PRO_0000311237"
FT DOMAIN 227..300
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 570..735
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1196..1342
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1615..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1977..2073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2092..2143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2276..2306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2350..2395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 388..464
FT /evidence="ECO:0000255"
FT COILED 1452..1476
FT /evidence="ECO:0000255"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1977..2041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2050..2073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2350..2385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 583..590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..1521
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_043685"
FT VAR_SEQ 1..146
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_043686"
FT VAR_SEQ 1512..1920
FT /note="IKFYDELDDIMPIWLPPSPPDSDADFDLRMEDDCLDLMYEIEQMNEARLPQV
FT CHEMRRPLAEKQQKQNTLNAFNDILSAKEKESVYDAVNKCLQMPQSEAITAESAASPAY
FT TEHSSFSMDDTSQDAKIEPSLTENQQPTTTATTTTTVPQQQQQQQQQKSSKKKRNDNRT
FT AQNRTAENGVKRATTPPPSWREEPDYDGAEWNIVEDYALLQAVQVEFANAHLVEKSANE
FT GMVLNWEFVSNAVNKQTRFFRSARQCSIRYQMFVRPKELGQLVASDPISKKTMKVDLSH
FT TELSHLRKGRMTTESQYAHDYGILTDKKHVNRFKSVRVAATRRPVQFWRGPKALESRNL
FT QSLNGGMPPRHESRLAEFDVKTNIRLDAEDIVTMSDESIVAYEASKKKLLASRQTKPSP
FT RQD -> VRDRRRRSSSLLQKAAQKPAKKPQNFQIRARSPSKRKSQAPSFDPYVSYAPH
FT ALASPPDSPRKRRSRGARSLGSGGGGGGGSRSVGRPARRSVKKEESDDDDEDYCQEEEV
FT KRNPAEKVPPKRKRVVFVEPPEVKPPEPKKRVVVPAPSSSSSALTTLPQQGPLISLPKA
FT VPVVPRPQQQAPPQLIKKHQQTLMPVKVLKISGGGGGTPGPSSVSPGPSILRRTVVPGI
FT GAGGVGRLPLVRMPVRPPFPGSQAPAPPLRSGVAPTAPAAAPRQFVVPSSRVRVITTRT
FT PVATTMVQQQQSPSPLMFPVRVVQRPGPSGPPPPGPPDRPGFGIYEKPRFSLGSRRSRG
FT DSGPEDPAPPQPPPPTTSRPPPQA (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_043687"
FT VAR_SEQ 1921..2395
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_043688"
SQ SEQUENCE 2395 AA; 268727 MW; 410ED3B87AEFD8C1 CRC64;
MPATPVRASS TRISRRTSSR SVADDQPSTS SAVAPPPSPI AIETDEDAVV EEEKKKKKTS
DDLEIITPRT PVDRRIPYIC SILLTENRSI RDKLVLSSGP VRQEDHEEQI ARAQRIQPVV
DQIQRVEQII LNGSVEDILK DPRFAVMADL TKEPPPTPAP PPPIQKTMQP IEVKIEDSEG
SNTAQPSVLP SCGGGETNVE RAAKREAHVL ARIAELRKNG LWSNSRLPKC VEPERNKTHW
DYLLEEVKWM AVDFRTETNT KRKIAKVIAH AIAKQHRDKQ IEIERAAERE IKEKRKMCAG
IAKMVRDFWS STDKVVDIRA KEVLESRLRK ARNKHLMFVI GQVDEMSNIV QEGLVSSSKS
PSIASDRDDK DEEFKAPGSD SESDDEQTIA NAEKSQKKED VRQEVDALQN EATVDMDDFL
YTLPPEYLKA YGLTQEDLEE MKREKLEEQK ARKEACGDNE EKMEIDESPS SDAQKPSTSS
SDLTAEQLQD PTAEDGNGDG HGVLENVDYV KLNSQDSDER QQELANIAEE ALKFQPKGYT
LETTQVKTPV PFLIRGQLRE YQMVGLDWMV TLYEKNLNGI LADEMGLGKT IQTISLLAHM
ACSESIWGPH LIVVPTSVIL NWEMEFKKWC PALKILTYFG TAKERAEKRK GWMKPNCFHV
CITSYKTVTQ DIRAFKQRAW QYLILDEAQN IKNWKSQRWQ ALLNVRARRR LLLTGTPLQN
SLMELWSLMH FLMPTIFSSH DDFKDWFSNP LTGMMEGNME FNAPLIGRLH KVLRPFILRR
LKKEVEKQLP EKTEHIVNCS LSKRQRYLYD DFMSRRSTKE NLKSGNMMSV LNIVMQLRKC
CNHPNLFEPR PVVAPFVVEK LQLDVPARLF EISQQDPSSS SASQIPEIFN LSKIGYQSSV
RSAKPLIEEL EAMSTYPEPR APEVGGFRFN RTAFVAKNPH TEESEDEGVM RSRVLPKPIN
GTAQPLQNGN SIPQNAPNRP QTSCIRSKTV VNTVPLTIST DRSGFHFNMA NVGRGVVRLD
DSARMSPPLK RQKLTGTATN WSDYVPRHVV EKMEESRKNQ LEIVRRRFEM IRAPIIPLEM
VALVREEIIA EFPRLAVEED EVVQERLLEY CELLVQRFGM YVEPVLTDAW QCRPSSSGLP
SYIRNNLSNI ELNSRSLLLN TSTNFDTRMS ISRALQFPEL RLIEYDCGKL QTLAVLLRQL
YLYKHRCLIF TQMSKMLDVL QTFLSHHGYQ YFRLDGTTGV EQRQAMMERF NADPKVFCFI
LSTRSGGVGV NLTGADTVIF YDSDWNPTMD AQAQDRCHRI GQTRNVSIYR LISERTIEEN
ILRKATQKRR LGELAIDEAG FTPEFFKQSD SIRDLFDGEN VEVTAVADVA TTMSEKEMEV
AMAKCEDEAD VNAAKIAVAE ANVDNAEFDE KSLPPMSNLQ GDEEADEKYM ELIQQLKPIE
RYAINFLETQ YKPEFEEECK EAEALIDQKR EEWDKNLNDT AVIDLDDSDS LLLNDPSTSA
DFYQSSSLLD EIKFYDELDD IMPIWLPPSP PDSDADFDLR MEDDCLDLMY EIEQMNEARL
PQVCHEMRRP LAEKQQKQNT LNAFNDILSA KEKESVYDAV NKCLQMPQSE AITAESAASP
AYTEHSSFSM DDTSQDAKIE PSLTENQQPT TTATTTTTVP QQQQQQQQQK SSKKKRNDNR
TAQNRTAENG VKRATTPPPS WREEPDYDGA EWNIVEDYAL LQAVQVEFAN AHLVEKSANE
GMVLNWEFVS NAVNKQTRFF RSARQCSIRY QMFVRPKELG QLVASDPISK KTMKVDLSHT
ELSHLRKGRM TTESQYAHDY GILTDKKHVN RFKSVRVAAT RRPVQFWRGP KALESRNLQS
LNGGMPPRHE SRLAEFDVKT NIRLDAEDIV TMSDESIVAY EASKKKLLAS RQTKPSPRQD
VRFHTLVLRP YTVPVTTEYS AAPSRREMRI AVPPLQPSAL STISSVAAAA TSGPLPSIQH
LQSSSTGLGS QQNLQNSHNS EQRNNVQNMH QNQYNSSQNP PIPIRQIGAA SSHQHDQGSQ
GPGGKPQAYH LVQQGSQQQQ QQQQQATLQR RNAAAAAGSN VQFIQQQQQQ QQSGKNCGQG
QSFVVMGSQS SSNDGQGGAS TVGGGGGGSQ QPHQQQQQQP QQRIQYIPQV TGSGNNGGGG
GRGGYGSTLV MPRGGRVVRP AGTLPGGGRL YVDHNRHPYP MSSNVVPVRV LPATQQGQQR
MMTGQRRPAP APGTVAAMVL PNRGAGGIPQ MRSLQRGSYT GGGGQQRINV MVQPQQMRSN
NGGGVGGQGG LQGGPGGPQG IRRPLVGRPL QRGVDNQAPT VAQVVVAPPQ GMQQASQGPP
VLHMQRAVSM QMPTSHHHQG QQQAPPQSSQ QASQQAPTSD SGTSAPPRQA PPPQN
