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NUCMR_DICDI
ID   NUCMR_DICDI             Reviewed;         756 AA.
AC   Q9U7C9; C7FZX6; Q55BM2; Q55BM3; Q6GW01;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Nucleomorphin;
DE   AltName: Full=Calmodulin-binding protein A;
DE   AltName: Full=Calmodulin-binding protein CaM-BP38;
GN   Name=numA;
GN   Synonyms=cmbA {ECO:0000312|dictyBase:DDB_G0269114},
GN   numB {ECO:0000312|EMBL:AAT48090.1}; ORFNames=DDB_G0269114;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAT48090.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CALMODULIN,
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DOMAIN DEED MOTIF, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11919178; DOI=10.1074/jbc.m109717200;
RA   Myre M.A., O'Day D.H.;
RT   "Nucleomorphin. A novel, acidic, nuclear calmodulin-binding protein from
RT   Dictyostelium that regulates nuclear number.";
RL   J. Biol. Chem. 277:19735-19744(2002).
RN   [2] {ECO:0000312|EMBL:AAT48090.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RX   PubMed=15535983; DOI=10.1016/j.bbagen.2004.08.002;
RA   Myre M.A., O'Day D.H.;
RT   "Dictyostelium nucleomorphin is a member of the BRCT-domain family of cell
RT   cycle checkpoint proteins.";
RL   Biochim. Biophys. Acta 1675:192-197(2004).
RN   [3] {ECO:0000312|EMBL:EAL71906.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4 {ECO:0000312|EMBL:EAL71906.1};
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [4] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11923193; DOI=10.1242/dev.129.7.1543;
RA   Van Driessche N., Shaw C., Katoh M., Morio T., Sucgang R., Ibarra M.,
RA   Kuwayama H., Saito T., Urushihara H., Maeda M., Takeuchi I., Ochiai H.,
RA   Eaton W., Tollett J., Halter J., Kuspa A., Tanaka Y., Shaulsky G.;
RT   "A transcriptional profile of multicellular development in Dictyostelium
RT   discoideum.";
RL   Development 129:1543-1552(2002).
RN   [5] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12912885; DOI=10.1128/ec.2.4.664-670.2003;
RA   Iranfar N., Fuller D., Loomis W.F.;
RT   "Genome-wide expression analyses of gene regulation during early
RT   development of Dictyostelium discoideum.";
RL   Eukaryot. Cell 2:664-670(2003).
RN   [6] {ECO:0000305}
RP   INTERACTION WITH CBPD1.
RX   PubMed=15325281; DOI=10.1016/j.bbrc.2004.07.168;
RA   Myre M.A., O'Day D.H.;
RT   "Dictyostelium calcium-binding protein 4a interacts with nucleomorphin, a
RT   BRCT-domain protein that regulates nuclear number.";
RL   Biochem. Biophys. Res. Commun. 322:665-671(2004).
RN   [7] {ECO:0000305}
RP   NUCLEAR LOCALIZATION SIGNAL, AND SUBCELLULAR LOCATION.
RX   PubMed=15896312; DOI=10.1016/j.bbrc.2005.04.101;
RA   Myre M.A., O'Day D.H.;
RT   "An N-terminal nuclear localization sequence but not the calmodulin-binding
RT   domain mediates nuclear localization of nucleomorphin, a protein that
RT   regulates nuclear number in Dictyostelium.";
RL   Biochem. Biophys. Res. Commun. 332:157-166(2005).
CC   -!- SUBUNIT: Interacts with calmodulin and CBPD1 in the presence of Ca(2+).
CC       {ECO:0000269|PubMed:11919178, ECO:0000269|PubMed:15325281}.
CC   -!- INTERACTION:
CC       Q9U7C9; Q54RF4: cbpD1; NbExp=2; IntAct=EBI-530708, EBI-531591;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11919178,
CC       ECO:0000269|PubMed:15896312}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2 {ECO:0000269|PubMed:15535983}; Synonyms=numA2
CC       {ECO:0000312|dictyBase:DDB_G0269114}, NumB
CC       {ECO:0000269|PubMed:15535983};
CC         IsoId=Q9U7C9-1; Sequence=Displayed;
CC       Name=1 {ECO:0000269|PubMed:11919178}; Synonyms=numA1
CC       {ECO:0000312|dictyBase:DDB_G0269114}, NumA
CC       {ECO:0000269|PubMed:11919178};
CC         IsoId=Q9U7C9-2; Sequence=VSP_052481;
CC   -!- DEVELOPMENTAL STAGE: Isoform 1 is expressed throughout development.
CC       Isoform 2 is expressed at low level during vegetative growth.
CC       Expression of isoform 2 increases rapidly during aggregation (1-4
CC       hours) and remains high throughout development.
CC       {ECO:0000269|PubMed:11919178, ECO:0000269|PubMed:11923193,
CC       ECO:0000269|PubMed:12912885, ECO:0000269|PubMed:15535983}.
CC   -!- DISRUPTION PHENOTYPE: Mutants lacking the DEED domain form
CC       multinucleated cells. {ECO:0000269|PubMed:11919178}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEU04155.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF140042; AAD56608.2; -; mRNA.
DR   EMBL; AY631855; AAT48090.1; -; mRNA.
DR   EMBL; AAFI02000005; EAL71906.1; -; Genomic_DNA.
DR   EMBL; AAFI02000005; EAL71907.2; -; Genomic_DNA.
DR   EMBL; AAFI02000005; EEU04155.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001134480.1; XM_001134480.1.
DR   RefSeq; XP_002649205.1; XM_002649159.1.
DR   RefSeq; XP_646808.2; XM_641716.2.
DR   AlphaFoldDB; Q9U7C9; -.
DR   IntAct; Q9U7C9; 1.
DR   STRING; 44689.DDB0231257; -.
DR   PaxDb; Q9U7C9; -.
DR   EnsemblProtists; EAL71906; EAL71906; DDB_G0269114.
DR   EnsemblProtists; EAL71907; EAL71907; DDB_G0269114.
DR   EnsemblProtists; EEU04155; EEU04155; DDB_G0269114.
DR   GeneID; 8617781; -.
DR   KEGG; ddi:DDB_G0269114; -.
DR   dictyBase; DDB_G0269114; numA.
DR   eggNOG; ENOG502RFA6; Eukaryota.
DR   HOGENOM; CLU_368610_0_0_1; -.
DR   InParanoid; Q9U7C9; -.
DR   OMA; EYVHYCA; -.
DR   PRO; PR:Q9U7C9; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005813; C:centrosome; IDA:dictyBase.
DR   GO; GO:0005635; C:nuclear envelope; IDA:dictyBase.
DR   GO; GO:0005730; C:nucleolus; IDA:dictyBase.
DR   GO; GO:0005654; C:nucleoplasm; IDA:dictyBase.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IPI:dictyBase.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:dictyBase.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   Pfam; PF00533; BRCT; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   PROSITE; PS50172; BRCT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calmodulin-binding; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..756
FT                   /note="Nucleomorphin"
FT                   /id="PRO_0000293632"
FT   DOMAIN          124..216
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..512
FT                   /note="Calmodulin binding"
FT                   /evidence="ECO:0000269|PubMed:11919178"
FT   REGION          514..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..588
FT                   /note="DEED region"
FT                   /evidence="ECO:0000269|PubMed:11919178"
FT   REGION          589..606
FT                   /note="Calmodulin binding"
FT                   /evidence="ECO:0000269|PubMed:11919178"
FT   REGION          596..613
FT                   /note="Calmodulin binding"
FT                   /evidence="ECO:0000269|PubMed:11919178"
FT   REGION          613..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           464..480
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:15896312"
FT   COMPBIAS        284..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..586
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..254
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:11919178"
FT                   /id="VSP_052481"
SQ   SEQUENCE   756 AA;  85404 MW;  C5DF0DB1A281C836 CRC64;
     MDLDYSSDNS RLVADNQNNK TNTKNQSQLS TSSQIPQTSQ SYQQQQQHNQ QQQQQQQQKQ
     NSRPSSPKTI QAKVNNNNNN NNNNNNNNNN NNNNGATISH PPTSQSNEDL SSSAEIHHDD
     SAQLNSNIFE NLGFVIDITI NLKRKMELVK IIKKNGGKSC YSCTKATHLI TTKQGYLEKT
     QKVTQAISLG IPILVKEYVH YCAFKKELLG VENYLVSSLI LNPTSTTLNS SQDLIEKPNE
     EEPQNGTINE QPIAMTIDNT LESNKPIETI QPSSLEKQEP KETELQTQQQ PQTELKSELE
     PQQLQLIQEK DKNINNLSID SNHMDTSKIE AGNNISNQTQ SNIISSVVQT IEPLKECNKI
     DLDNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNSSSNNKN KNNVDEAQEG LNINSVMDVH
     LTSSTSSTLS SSDNQDNELL RDEGTTPKSK KKFSQKKNHL LNLKKSYQDP EIIAHSRPRK
     SSGGVSLVEA LSDHANYISN LDGFKYYARA NKSSLNSNAT TSGGNNRSIK LNEYKYDDEE
     EDEEDEDEED EEEDEEEEEE EEEEEEDYDD EDLNDEESDE DDFDSDEDVS RFIKGKLLQK
     QQKIYKDLER FEHSRQQQHH HHQSSQVNSS KPRSRSHSRD YIESEIAKYL LNNSEKQIPL
     SPTKKRSLSN QFHQDGGNNT TDGNLFNNFS TNGGGNRTNI DDSIKQSILE SPSSSSLKSS
     KSKKSKKPFL PPLSTLVHIL VTFIILSAFF MSLPSN
 
 
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