SDC3_CAEEL
ID SDC3_CAEEL Reviewed; 2150 AA.
AC P34706; O17596;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Zinc finger protein sdc-3;
GN Name=sdc-3; ORFNames=C25D7.3;
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 [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=8431944; DOI=10.1016/0092-8674(93)90113-5;
RA Klein R.D., Meyer B.J.;
RT "Independent domains of the Sdc-3 protein control sex determination and
RT dosage compensation in C. elegans.";
RL Cell 72:349-364(1993).
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, AND DISRUPTION PHENOTYPE.
RX PubMed=8939869; DOI=10.1126/science.274.5293.1732;
RA Lieb J.D., Capowski E.E., Meneely P., Meyer B.J.;
RT "DPY-26, a link between dosage compensation and meiotic chromosome
RT segregation in the nematode.";
RL Science 274:1732-1736(1996).
RN [4]
RP FUNCTION.
RX PubMed=8939870; DOI=10.1126/science.274.5293.1736;
RA Chuang P.-T., Lieb J.D., Meyer B.J.;
RT "Sex-specific assembly of a dosage compensation complex on the nematode X
RT chromosome.";
RL Science 274:1736-1739(1996).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF CYS-2080; CYS-2083; CYS-2119 AND CYS-2122.
RX PubMed=9056777; DOI=10.1242/dev.124.5.1019;
RA Davis T.L., Meyer B.J.;
RT "SDC-3 coordinates the assembly of a dosage compensation complex on the
RT nematode X chromosome.";
RL Development 124:1019-1031(1997).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9458050; DOI=10.1016/s0092-8674(00)80920-4;
RA Lieb J.D., Albrecht M.R., Chuang P.-T., Meyer B.J.;
RT "MIX-1: an essential component of the C. elegans mitotic machinery executes
RT X chromosome dosage compensation.";
RL Cell 92:265-277(1998).
RN [7]
RP FUNCTION, IDENTIFICATION IN A SDC COMPLEX, INTERACTION WITH SDC-1 AND
RP SDC-2, AND SUBCELLULAR LOCATION.
RX PubMed=11937488; DOI=10.1101/gad.972702;
RA Chu D.S., Dawes H.E., Lieb J.D., Chan R.C., Kuo A.F., Meyer B.J.;
RT "A molecular link between gene-specific and chromosome-wide transcriptional
RT repression.";
RL Genes Dev. 16:796-805(2002).
RN [8]
RP FUNCTION, INTERACTION WITH DPY-21, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=14660541; DOI=10.1242/dev.00886;
RA Yonker S.A., Meyer B.J.;
RT "Recruitment of C. elegans dosage compensation proteins for gene-specific
RT versus chromosome-wide repression.";
RL Development 130:6519-6532(2003).
RN [9]
RP SUMOYLATION.
RX PubMed=24043781; DOI=10.1073/pnas.1315793110;
RA Pferdehirt R.R., Meyer B.J.;
RT "SUMOylation is essential for sex-specific assembly and function of the
RT Caenorhabditis elegans dosage compensation complex on X chromosomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E3810-E3819(2013).
CC -!- FUNCTION: Component of the SDC complex that functions in sex
CC determination and in X chromosome dosage compensation specifically in
CC hermaphrodite (XX) animals (PubMed:8431944, PubMed:11937488). Plays a
CC central role in the recruitment of the condensin I-like dosage
CC compensation complex to the male sex-determining autosomal gene her-1,
CC thereby contributing to its repression and initiating hermaphrodite
CC sexual development (PubMed:11937488, PubMed:14660541). Involved in the
CC recruitment and assembly of the dosage compensation complex and the
CC dosage compensation protein dpy-21 onto the X chromosomes in
CC hermaphrodites, which leads to a reduction of X-linked gene
CC transcription and an equalization of X-linked gene expression between
CC the sexes (PubMed:14660541, PubMed:9458050, PubMed:8939870,
CC PubMed:9056777, PubMed:8939869). {ECO:0000269|PubMed:11937488,
CC ECO:0000269|PubMed:14660541, ECO:0000269|PubMed:8431944,
CC ECO:0000269|PubMed:8939869, ECO:0000269|PubMed:8939870,
CC ECO:0000269|PubMed:9056777, ECO:0000269|PubMed:9458050}.
CC -!- SUBUNIT: Component of the SDC complex, which consists of sdc-1, sdc-2
CC and sdc-3 (PubMed:11937488). Within the complex, interacts with sdc-1
CC and sdc-2 (PubMed:11937488). Interacts with dpy-21 (PubMed:14660541).
CC {ECO:0000269|PubMed:11937488, ECO:0000269|PubMed:14660541}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:11937488,
CC ECO:0000269|PubMed:14660541, ECO:0000269|PubMed:9056777}. Nucleus
CC {ECO:0000269|PubMed:9056777}. Note=Localizes specifically to X
CC chromosomes in hermaphrodite (XX) embryos after the 40-cell stage.
CC {ECO:0000269|PubMed:11937488, ECO:0000269|PubMed:14660541,
CC ECO:0000269|PubMed:9056777}.
CC -!- TISSUE SPECIFICITY: Expressed in somatic and in germline tissues in
CC hermaphrodites (XX). In males (XO), only present in embryos younger
CC than the 100-cell stage (at protein level).
CC {ECO:0000269|PubMed:9056777}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic and early larval stages and
CC in adult animals. {ECO:0000269|PubMed:8431944,
CC ECO:0000269|PubMed:9056777}.
CC -!- PTM: Sumoylated. Sumoylation is important for assembly of the dosage
CC compensation complex and its robust binding to the X chromosome.
CC {ECO:0000269|PubMed:24043781}.
CC -!- DISRUPTION PHENOTYPE: Disrupts the X-chromosome specific localization
CC of dpy-26, mix-1 and dpy-21. {ECO:0000269|PubMed:14660541,
CC ECO:0000269|PubMed:8939869, ECO:0000269|PubMed:9458050}.
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; M85149; AAA28144.1; -; Genomic_DNA.
DR EMBL; Z81039; CAB02774.1; -; Genomic_DNA.
DR PIR; A45172; S27802.
DR PIR; T19450; T19450.
DR RefSeq; NP_506703.1; NM_074302.1.
DR AlphaFoldDB; P34706; -.
DR BioGRID; 45005; 5.
DR ComplexPortal; CPX-3888; SDC complex.
DR STRING; 6239.C25D7.3; -.
DR iPTMnet; P34706; -.
DR EPD; P34706; -.
DR PaxDb; P34706; -.
DR PeptideAtlas; P34706; -.
DR EnsemblMetazoa; C25D7.3.1; C25D7.3.1; WBGene00004747.
DR GeneID; 180009; -.
DR KEGG; cel:CELE_C25D7.3; -.
DR UCSC; C25D7.3; c. elegans.
DR CTD; 180009; -.
DR WormBase; C25D7.3; CE08389; WBGene00004747; sdc-3.
DR eggNOG; ENOG502QTZX; Eukaryota.
DR GeneTree; ENSGT00970000196626; -.
DR HOGENOM; CLU_231764_0_0_1; -.
DR InParanoid; P34706; -.
DR OMA; ECEILME; -.
DR OrthoDB; 1316910at2759; -.
DR PRO; PR:P34706; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004747; Expressed in embryo and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0000805; C:X chromosome; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0042464; P:dosage compensation by hypoactivation of X chromosome; IC:ComplexPortal.
DR GO; GO:0042715; P:dosage compensation complex assembly involved in dosage compensation by hypoactivation of X chromosome; IDA:WormBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0007530; P:sex determination; IMP:WormBase.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Chromosome; Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..2150
FT /note="Zinc finger protein sdc-3"
FT /id="PRO_0000046891"
FT ZN_FING 2078..2105
FT /note="C2H2-type 1"
FT ZN_FING 2117..2141
FT /note="C2H2-type 2"
FT REGION 443..987
FT /note="Dosage compensation domain 1"
FT /evidence="ECO:0000269|PubMed:8431944"
FT REGION 874..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1508..1516
FT /note="Sex determination domain"
FT /evidence="ECO:0000269|PubMed:8431944"
FT REGION 2080..2105
FT /note="Dosage compensation domain 2"
FT /evidence="ECO:0000269|PubMed:8431944"
FT COMPBIAS 1263..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1340
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1520
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 2080
FT /note="C->S: Loss of X chromosome association and failure
FT in dosage compensation complex assembly; when associated
FT with S-2083; S-2119 and S-2122."
FT /evidence="ECO:0000269|PubMed:9056777"
FT MUTAGEN 2083
FT /note="C->S: Loss of X chromosome association and failure
FT in dosage compensation complex assembly; when associated
FT with S-2080; S-2119 and S-2122."
FT /evidence="ECO:0000269|PubMed:9056777"
FT MUTAGEN 2119
FT /note="C->S: Loss of X chromosome association and failure
FT in dosage compensation complex assembly; when associated
FT with S-2080; S-2083 and S-2122."
FT /evidence="ECO:0000269|PubMed:9056777"
FT MUTAGEN 2122
FT /note="C->S: Loss of X chromosome association and failure
FT in dosage compensation complex assembly; when associated
FT with S-2080; S-2083 and S-2119."
FT /evidence="ECO:0000269|PubMed:9056777"
FT CONFLICT 451
FT /note="A -> R (in Ref. 1; AAA28144)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="S -> C (in Ref. 1; AAA28144)"
FT /evidence="ECO:0000305"
FT CONFLICT 937
FT /note="A -> R (in Ref. 1; AAA28144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2150 AA; 249770 MW; E6A29F205124B589 CRC64;
MSDEPPIVLP TEEDGPFSNC VSIAFVNDKS IPVELRIRKA IRGKVTFTQE LVVAARRLYL
DGELERPDLN YHVAADFYDP FMIPVPDHRN WEYNPLYPRE WPRLIDRDLV QKIKMSNTYK
KNQARRKRRR LLRIFHRKRG GEFLNYLWHS KENDVHYKRY MAAYQFPLPF EKCIRDVVRE
ELKDPETSFS KPPSVVHHSK IRPATPDLLK LAKYLGKDRF CFIVTPFKFR SQFRLRYYKK
SPFKRSNILE KWLKFKKVRD QGVFNIRDAA REVKKLLQRK NVYHMTDPQC EQEFWDVYRL
QMQWLEEDNI EENITMLREN LSKVTDEEFN RSVYIMRPEN RASIHDDVTF TTDAEINLKP
IVLELFRNNM PLEDIRQVKE CIDDMINLTV CQELIPQVAT IETVRDYSGV EQHRLKYIRP
ENELEIMFQL ATVLVKNENT HDQEITSPMF ALLRTEQYLW SIPLRPFLRM YTDWRKTKLN
FKKFRKFSPE LVSKAPIDLF KVFLTTNMDK KGVATKDTDC FDYRTASEIK KLYHEEFIRV
RPIIEHQRFH RCYTSVITEE PLPNPFYWVH RGQWEKVYEC NWKQRVKPLA GRFSWKTKHP
NICDLPRLEK DDKQEMEMLA KMREKIREYN KEKEKHPFYV SSSLPEFAST SDFVKFPISN
TGIKYTAPRR NQPKVQRSLV TYTRFRLAEL EDKDFSFPEE KMLEKNRLLE KLNFEERLQL
DALMSKDVKY KPRMIPEKGF LQLQDEKLIL KRLCEKEDEW SGKQKRRFPD LYEQATQEAE
RLGDPDASTS GTSNKELGLL PVWKHDDFRD LKKINVLGSK EYPISSPYLI KRLHYDIHLE
IVRDKLKSWI YRTELWEKMK PVYERLKRDK EKREKEWHEM RAAQRAQKEK EEEDQRRMDM
GIEHGQESLL KSITPEVEQQ ILLPISRENS FEEMLPAPQE AYDEDLDQDI DIHFDGAESV
CTGIRLDSED RELVDSPDQV ENEEPERVEA VTENIRQEMS DAEMRDLMRK KREQYSMLFP
NVPQPFQPLN RFDVTAPGAG IVPPYDEAPD FDLSAYLEED HVRIPTLSTV EINSLLKDQD
LVEEQEIVEE EETPLVVEEP DIPAAPVLSA EEKASRISRE MSALRKLPDA AFNYASDRDG
VVVEEVETIE EIQEIYNDKL EKMIAARLGS IAQGANIERL SEDQLLGDQG SEDISFEEIQ
VDLLLESGVE VQVNQSVTIS RSSTSFESLL VEDPEEHPEQ LPVSASEKAN NQIVPEVEVE
GSVVPVTNQQ EENVTSEGPT LQEGSSIPSS SHIYTVDELL GTESPGPEAT ETPVAEESPK
KKSGKTTRGR PKKVKENLKK RIQPRRGQKE EAAHEPEVVE EQEQVEPEVG PEVVHEPVPA
PAAQLETEPI EQQIEEPDKV FEPIIEALPL FETSPVPAPE GNIPSRAHSS DDDVQVISSE
TDPNGPINLV EQVQNDKLTA YQYSTEELLG EYGELDEAGA PSPSEIVVHD EVLQDEVLQP
NPKSSKKRGR RRKKTPPHIA KARKVFTSIS KTEEIELAPT PTQQSRKRMA NVSSEEATAT
RRQKRAKVEE PNDSDVSRVL TPEPEDLHET ERPGHVGEEG FETPSLRTGR ESTASSVKTS
RSKRLFLSKN NPVPRMRIQS QAGTNASPTP ARRTGVARDS VSPDGASEKL KQLPKSVQDI
FEVFDVERSA ERGESATVTN LEGPVKIEIE DENWMAPPAI TETSRKSKKR LRAEKQQQIL
DDIKLELNGE PPQKRECEIL MERVQVKIEE GVENADCRIV QANFNCKSVE EHETLPLKII
RVFEENEKPV HKFFMTQIIW KEINEAFMTD PEKFMLLVRI LFSDRNISGQ IYKISMTVTD
RIKGFDDDFI KLLTQFPKKL SQEHKPLVDY NKLAHALREK ASLHLNNHKI TPFTFHGVIS
NITEMKEKII GRCEIGMLTD GDRDVLNSTE NMLLGAYMKS VLRMTAQSQV SWAHPEYIKR
RLEMIYYGWR MFLGSGGFFR VALAINRKDV KPMSQQFRDF FIEYLKDVNE NYAKAVELVQ
MDEDKLMEAM IEKAGLSSID LLALDEDVQG QVSESHKHKC VQCSIRNQSV YFSSYSLLEL
HGKLHQNLHE LAPEDADDCQ DCYETLTSSF EVIVHRINHH HSRRCFFADD