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SDC2_CAEEL
ID   SDC2_CAEEL              Reviewed;        2962 AA.
AC   G5EBL3;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Sex determination and dosage compensation protein sdc-2 {ECO:0000305};
GN   Name=sdc-2 {ECO:0000312|WormBase:C35C5.1};
GN   ORFNames=C35C5.1 {ECO:0000312|WormBase:C35C5.1};
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:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=10364546; DOI=10.1126/science.284.5421.1800;
RA   Dawes H.E., Berlin D.S., Lapidus D.M., Nusbaum C., Davis T.L., Meyer B.J.;
RT   "Dosage compensation proteins targeted to X chromosomes by a determinant of
RT   hermaphrodite fate.";
RL   Science 284:1800-1804(1999).
RN   [2] {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   [3] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=2759421; DOI=10.1093/genetics/122.3.579;
RA   Nusbaum C., Meyer B.J.;
RT   "The Caenorhabditis elegans gene sdc-2 controls sex determination and
RT   dosage compensation in XX animals.";
RL   Genetics 122:579-593(1989).
RN   [4] {ECO:0000305}
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   [5] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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   [6] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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   [7] {ECO:0000305}
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   [8] {ECO:0000305}
RP   FUNCTION, IDENTIFICATION IN A SDC COMPLEX, INTERACTION WITH SDC-1 AND
RP   SDC-3, AND TISSUE SPECIFICITY.
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   [9] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION 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   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23666922; DOI=10.1101/gad.217026.113;
RA   Farboud B., Nix P., Jow M.M., Gladden J.M., Meyer B.J.;
RT   "Molecular antagonism between X-chromosome and autosome signals determines
RT   nematode sex.";
RL   Genes Dev. 27:1159-1178(2013).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25204677; DOI=10.1186/s12915-014-0064-6;
RA   Crook-McMahon H.M., Olahova M., Button E.L., Winter J.J., Veal E.A.;
RT   "Genome-wide screening identifies new genes required for stress-induced
RT   phase 2 detoxification gene expression in animals.";
RL   BMC Biol. 12:64-64(2014).
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:2759421, PubMed:10364546). Required
CC       for the recruitment of the condensin I-like dosage compensation complex
CC       to the male sex-determining autosomal gene her-1, thereby contributing
CC       to its repression and initiating hermaphrodite sexual development
CC       (PubMed:2759421, PubMed:10364546, PubMed:14660541, PubMed:11937488).
CC       Plays a central role in X-chromosome recognition and in the recruitment
CC       and assembly of the dosage compensation complex and the dosage
CC       compensation protein dpy-21 onto the X chromosomes in hermaphrodites,
CC       which leads to a reduction of X-linked gene transcription and an
CC       equalization of X-linked gene expression between the sexes
CC       (PubMed:8939869, PubMed:8939870, PubMed:9458050, PubMed:9056777,
CC       PubMed:10364546, PubMed:14660541). May confer protection against
CC       toxicity induced by heavy metals such as arsenite (PubMed:25204677).
CC       {ECO:0000269|PubMed:10364546, ECO:0000269|PubMed:11937488,
CC       ECO:0000269|PubMed:14660541, ECO:0000269|PubMed:25204677,
CC       ECO:0000269|PubMed:2759421, ECO:0000269|PubMed:8939869,
CC       ECO:0000269|PubMed:8939870, ECO:0000269|PubMed:9056777,
CC       ECO:0000269|PubMed:9458050}.
CC   -!- SUBUNIT: Component of the SDC complex, which consists of sdc-1, sdc-2
CC       and sdc-3. Within the complex, interacts with sdc-1 and sdc-3.
CC       {ECO:0000269|PubMed:11937488}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:10364546}.
CC       Note=Localizes specifically to X chromosomes in hermaphrodite (XX)
CC       embryos. {ECO:0000269|PubMed:10364546}.
CC   -!- TISSUE SPECIFICITY: Expressed in hermaphrodites (XX), but absent in
CC       males (XO) (at protein level). {ECO:0000269|PubMed:11937488}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos after the 40-cell stage and
CC       in adults. {ECO:0000269|PubMed:10364546}.
CC   -!- DISRUPTION PHENOTYPE: Results in high lethality of hermaphrodites (XX)
CC       and in masculinization of surviving XX animals (PubMed:2759421).
CC       Disrupts the X-chromosome specific localization of sdc-3, dpy-21, dpy-
CC       26, dpy-27 and mix-1 (PubMed:9056777, PubMed:8939869, PubMed:8939870,
CC       PubMed:9458050, PubMed:14660541). RNAi-mediated knockdown results in
CC       86% viability of hermaphrodites (PubMed:23666922). RNAi-mediated
CC       knockdown results in increased sensitivity to the heavy metal arsenite
CC       (PubMed:25204677). RNAi-mediated knockdown reduces the viability of
CC       hermaphrodites to 19% in a double xol-1(y9) and sex-1(y263) mutant
CC       background (PubMed:23666922). RNAi-mediated knockdown reduces the
CC       viability of hermaphrodites to 11% in a triple sea-1(y356), xol-1(y9)
CC       and sex-1(y263) mutant background (PubMed:23666922). RNAi-mediated
CC       knockdown reduces the viability of hermaphrodites to 42% in a triple
CC       sea-2(y407), xol-1(y9) sex-1(y263) mutant background (PubMed:23666922).
CC       RNAi-mediated knockdown reduces the viability of hermaphrodites to 51%
CC       in a quadruple sea-1(y356), sea-2(y407), xol-1(y9) sex-1(y263) mutant
CC       background (PubMed:23666922). {ECO:0000269|PubMed:14660541,
CC       ECO:0000269|PubMed:23666922, ECO:0000269|PubMed:25204677,
CC       ECO:0000269|PubMed:2759421, ECO:0000269|PubMed:8939869,
CC       ECO:0000269|PubMed:8939870, ECO:0000269|PubMed:9056777,
CC       ECO:0000269|PubMed:9458050}.
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DR   EMBL; AF111934; AAD18003.1; -; mRNA.
DR   EMBL; BX284606; CAB01693.1; -; Genomic_DNA.
DR   PIR; T19756; T19756.
DR   RefSeq; NP_509924.1; NM_077523.5.
DR   SMR; G5EBL3; -.
DR   ComplexPortal; CPX-3888; SDC complex.
DR   STRING; 6239.C35C5.1; -.
DR   EPD; G5EBL3; -.
DR   PaxDb; G5EBL3; -.
DR   PeptideAtlas; G5EBL3; -.
DR   EnsemblMetazoa; C35C5.1.1; C35C5.1.1; WBGene00004746.
DR   GeneID; 181341; -.
DR   KEGG; cel:CELE_C35C5.1; -.
DR   CTD; 181341; -.
DR   WormBase; C35C5.1; CE18542; WBGene00004746; sdc-2.
DR   eggNOG; ENOG502QPJP; Eukaryota.
DR   GeneTree; ENSGT00970000196472; -.
DR   HOGENOM; CLU_225808_0_0_1; -.
DR   InParanoid; G5EBL3; -.
DR   OMA; YMSDEQD; -.
DR   OrthoDB; 622145at2759; -.
DR   PRO; PR:G5EBL3; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00004746; Expressed in embryo and 3 other tissues.
DR   GO; GO:0000228; C:nuclear chromosome; IDA:WormBase.
DR   GO; GO:0000805; C:X chromosome; IDA:ComplexPortal.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0042464; P:dosage compensation by hypoactivation of X chromosome; 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; IC:ComplexPortal.
DR   GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Chromosome; Coiled coil; Differentiation; Reference proteome;
KW   Sexual differentiation; Transcription; Transcription regulation.
FT   CHAIN           1..2962
FT                   /note="Sex determination and dosage compensation protein
FT                   sdc-2"
FT                   /id="PRO_0000440872"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1061..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1535..1554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2198..2227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          995..1085
FT                   /evidence="ECO:0000255"
FT   COILED          1140..1268
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1065..1110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2962 AA;  344436 MW;  07C0A5EB8375DD0D CRC64;
     MSDESELGNQ SEMESFNESD SPDEADPDVV IIHDIVHLRA STTGDYSQSE IGKLPEQNTF
     FLPGRVKRNI SSNDSDVIID EDEIPDGAIR ITSDTHFIGS SRGTSELGDF EMDEQEFLNI
     TIEENGNEQE LEEHLRNAYR HEEEECFEEE DDIIELPPLP VKPAVKKPRR KLPKHLSIES
     GSTAKTSKLV AEVVHDHPRP VNYRMKPAVT DDGKVVEQKR TRVTRNIMSH TIPQYHLEGE
     ETEFGRVKES TLSKTIEQYL QAGKLVSPKC DQFREQIVAT AVEYDGSVKM LQFENALKKH
     SGKQKRLKYQ TGWWKASKSH YERAVNGYVA MPKTPVLSIS DDPVLYKHHS LFPKNQSSEL
     EKINVQLRIR LNSKRQNNDV IPDSSYFVRE FLMQKHSISL RMNRSSDLPE LFVPPTLECG
     YFPQDAVTVQ QQEHYLMMRF EEAQDEYHNI TYRSIAPPVE FQVGTISAKE LHKFHRIGRH
     IHGFFVVWEN KFPEYDESGI CCPRKRYLVD MFNLICFPLY TEYEQWESRL RVAFDKTIVY
     NLHLSEILRC NRPVFDFLSK NKSMLQPITL KEIVYLIEQS NMDAKSFAVK FGLRTFYDHG
     RATSNKDYLS AFLIITGGAK VVTEEIDSER LRVFNSDYME SGVLTSSGDV YTFEFDKIPN
     NYQISIGCNA DGVAEMEQED VRHELSECSS RITRIIGDSK KPEKIIARPL VKTNQNDGMK
     FFTRKDLLNY RIKLYDPSYV VPRAKKQIVN EPAKKKPGRK SKTRYDAAMQ QNNFEIEGVP
     SDVDSEFEGY LSDSENVFQK PSKLMRSTSS DSVFIDYQYR EKMFLDVSWF HQQKMIDRSL
     PPLKKRKRKM NRIYHKHSVR YTMLQANGCA FTEMYRCYDK ILPCGTKEIA RTKNAIRFPH
     RFRTYNIPQV YGPGDKQLIT EVFGVVKDVI TRATGFESAS IRTANDIAQA VYDANIARRE
     LLENLEPSDN GILPSPAYLA IEMLSHQKMS GRLCLESARK DVQNNVDKMY NDYMDLDPLD
     KELHFEISQS IRQSKLNESL EEYERNRERQ LAKTLKTVPM DKRSQAALAR REEKRRESRR
     KLADKYAEQR RMMASTRRLE KRTTQKQVDP ETIQRLRRED EVRKRKRFEE EDRRGMIRRR
     EERVALQEKV DRMLEEGLRL EKVREAERIR QQQEEERIEM ETILISRRVR EEEEEKMRLE
     RLRKAERERE QERLKREEEE ERKRLEQLRE AEKLKAEIEK ENERKLQEER TRKALELERK
     IEEIKRVSTL KDMFGPLPIA KENEQTEKDF QILLDDHELT LLTISRDPLN EKYQEARTEF
     ERLDIKSMLL RKAEKLIDVL TIHYDVPIEQ TCRYFTSSIE SNENRMAVNE QLNKLFENMA
     NCFTFNIQDG ENGLQSKRKW DFQFKKCAVF DGVSQSTVNF IEEKMRENTK KKHLATPKTV
     ISIDTSLLKQ SLLRSHARFD PDISLYAQNH TANSIGDVTL KMSNYSLDFA TQSIHDKELA
     EKATPKKGPT VRRHIKNLFG SEKVIVRRSL AAGKPASLNS EDSDSEDSRE GSPVAEFLPT
     NPVCSFWKLV VKIENSTTDK EKTELCEDLD KLILRKDDLF SKSLKWMFPL LATFYVLLSN
     AVLNENEEII SDKNQTGVTK DEILKSTIND LMIIAAYFEE GSRERSNLRK MISMNGFSVV
     FNRVILFAKK TCTLAKELES NSRSLSGYVI EDLFESLLAE IERTMRQELG SSVRKTGKLE
     RDFEEIVKLI QNEKKLALSH KSHKNDENRR FRLNTVVKWY DAIICHCKEE LTQAIVDAFP
     LNAITKNKET SHVAMENGDD EAMLSDTSDN QMSTTDYQMP KNICRNSEIF PEDAFAKAYA
     VVRIPSKKER AQMLSVYRKK NAQSGCVENK GLSRMPKFEE PFVDSVWRTI EKRINNMTHS
     EEKQIKRFIP VSRSHKLNEK VKFYAMVMIQ ERDSRDTRLF NSKFQDDNLW HCYSKSSLNH
     EKMESRILQH IEHTVLSKSN FNQMKWSVQC VNGNKKDAIH YFTDLYKYRS ESEFRSALSC
     GKLKFNFKVY THLWFMGNLL PTSYNPDSHD DKLFVPCSGC TSGDVIIIHK CTCAYHNDTF
     SDKFIYANTS LPVGIDKVTR LVGRFVCEHG PSSFLILEHC SANVDANIPF ESENVEFSAE
     LRIVKRKTMH SQLVKTFAEE HTHLRDASRH RAISTVTLDS SGSGRSTRCE IFEDSPSEDE
     NDENQLDTTR IGRKIDPIIV DSDKAYLIAE GERMALRIKR LLDPELQKFR SKNFVSRSKS
     VDAPKTSKQK TVIRRSQSVC DLNDVNEYAQ KKVRNTKDSF ATLFRDHEYS TRRTYEEQLN
     NELLDVVTTF GGASNVSADK KYNILASILA FEKEVQLVND KNGELFKTVS NLVQRNSLQH
     VKGVILAEDN QTLRSTDNTS EVFPESKAVN EYLKFEIYKR KMMVNAKLMA DTVKDLKLKH
     AEYRPFAKLI ATYDSIFKFN VYLFEHFLNC ISKHVFNPYA IYCEETRPTG TELSKFQLTL
     KLIETSMPTV LSMLFNTEPL RRQLSELSEI HKKVRSEDLA CTIASLCRYA IERIRIPQTA
     DKRLCDFSWL NSAEDHRETV SFIRLTLEHT LPDMKTENEQ TRFVEFLKEA EGFHFSYKFV
     EAQCKTFVRN HGDSKQAFFT AFYNQNEAFY GSLQKFMSNG TIDPKMKLYY QHQAFLRLHN
     IVKKRSHIIT SDDYHRSSDV CKAMLLSEIV SNPKIAQEAY ISGSVLDRMY TSLCKIKAKM
     PLISPSYIGT SLTCFEDELL FSAVREAKVH TDTRVVFRSK SCMRPNEKAG DANFKTCKVT
     LLVNLETALL SMVFKSRDQS EIDKDDRLDI DILDEEVIKP IIDWNRIFET FIQPTYNTLF
     SRMEKRERVS ILPENPLGRL ENYAFTNPNQ DKDCQAVLEY IDVASDTDAE ESIEDPLDIV
     EMTLKRALPR SMSPSSKRRR MR
 
 
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