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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}.
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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
 
 
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