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SUN1_DICDI
ID   SUN1_DICDI              Reviewed;         905 AA.
AC   Q558Z2;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Sun domain-containing protein 1;
GN   Name=sun1; ORFNames=DDB_G0272869;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
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   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND SUBUNIT.
RX   PubMed=18266910; DOI=10.1111/j.1600-0854.2008.00721.x;
RA   Xiong H., Rivero F., Euteneuer U., Mondal S., Mana-Capelli S.,
RA   Larochelle D., Vogel A., Gassen B., Noegel A.A.;
RT   "Dictyostelium Sun-1 connects the centrosome to chromatin and ensures
RT   genome stability.";
RL   Traffic 9:708-724(2008).
RN   [4]
RP   SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19632001; DOI=10.1016/j.ejcb.2009.06.003;
RA   Schulz I., Baumann O., Samereier M., Zoglmeier C., Graef R.;
RT   "Dictyostelium Sun1 is a dynamic membrane protein of both nuclear membranes
RT   and required for centrosomal association with clustered centromeres.";
RL   Eur. J. Cell Biol. 88:621-638(2009).
CC   -!- FUNCTION: May have an important role in defining the spacing of the
CC       nuclear envelope lumen. Essential for centrosome attachment to the
CC       nucleus, maintenance of correct ploidy, proper mitosis, association of
CC       the centromere cluster with the centrosome and the maintenance of
CC       genome stability. Requires direct chromatin binding for inner nuclear
CC       membrane targeting. {ECO:0000269|PubMed:18266910,
CC       ECO:0000269|PubMed:19632001}.
CC   -!- SUBUNIT: Homodimer and homooligomer. {ECO:0000269|PubMed:18266910}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:18266910,
CC       ECO:0000269|PubMed:19632001}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:18266910, ECO:0000269|PubMed:19632001};
CC       Nucleoplasmic side {ECO:0000269|PubMed:18266910,
CC       ECO:0000269|PubMed:19632001}.
CC   -!- DISRUPTION PHENOTYPE: Shows significant reduced growth.
CC       {ECO:0000269|PubMed:19632001}.
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DR   EMBL; AAFI02000008; EAL71072.1; -; Genomic_DNA.
DR   RefSeq; XP_644924.1; XM_639832.1.
DR   AlphaFoldDB; Q558Z2; -.
DR   SMR; Q558Z2; -.
DR   STRING; 44689.DDB0219949; -.
DR   TCDB; 1.I.1.1.5; the nuclear pore complex (npc) family.
DR   PaxDb; Q558Z2; -.
DR   PRIDE; Q558Z2; -.
DR   EnsemblProtists; EAL71072; EAL71072; DDB_G0272869.
DR   GeneID; 8618603; -.
DR   KEGG; ddi:DDB_G0272869; -.
DR   dictyBase; DDB_G0272869; sun1.
DR   eggNOG; KOG2687; Eukaryota.
DR   HOGENOM; CLU_320658_0_0_1; -.
DR   InParanoid; Q558Z2; -.
DR   OMA; NISHHID; -.
DR   PRO; PR:Q558Z2; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:InterPro.
DR   GO; GO:0005635; C:nuclear envelope; IDA:dictyBase.
DR   GO; GO:0005637; C:nuclear inner membrane; IDA:dictyBase.
DR   GO; GO:0005640; C:nuclear outer membrane; IDA:dictyBase.
DR   GO; GO:0005654; C:nucleoplasm; IDA:dictyBase.
DR   GO; GO:0003682; F:chromatin binding; IDA:dictyBase.
DR   GO; GO:0003677; F:DNA binding; IDA:dictyBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0034508; P:centromere complex assembly; IMP:dictyBase.
DR   GO; GO:0007098; P:centrosome cycle; IMP:dictyBase.
DR   GO; GO:0051642; P:centrosome localization; IMP:dictyBase.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:dictyBase.
DR   GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR   GO; GO:0006997; P:nucleus organization; IMP:dictyBase.
DR   InterPro; IPR045119; SUN1-5.
DR   InterPro; IPR012919; SUN_dom.
DR   PANTHER; PTHR12911; PTHR12911; 2.
DR   Pfam; PF07738; Sad1_UNC; 1.
DR   PROSITE; PS51469; SUN; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Coiled coil; Membrane; Mitosis; Nucleus;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..905
FT                   /note="Sun domain-containing protein 1"
FT                   /id="PRO_0000390618"
FT   TOPO_DOM        1..290
FT                   /note="Nuclear"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        312..905
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          662..860
FT                   /note="SUN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          41..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          170..221
FT                   /evidence="ECO:0000255"
FT   COILED          359..456
FT                   /evidence="ECO:0000255"
FT   COILED          504..609
FT                   /evidence="ECO:0000255"
FT   COILED          864..901
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        41..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   905 AA;  104743 MW;  208FA7368F3280D2 CRC64;
     MSGDYKPNYQ SSPSRKRLPL QSKDQASIYK YQTPSTLNLY NNTVNNNSSN NSNNHLLHNS
     NPNSSYLYDS SKQYSNQINI RNNSNSNSNT NNITSKKASS SYSINNKVDH NSHNNNDDDD
     IEDDVDINYS TNNASSNILH NRFSNSNKDD SYIDYSTDEN PKILKQPQPL YNHLNNQIQQ
     QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQRNNNNNS NSSNNNNTST TIKRNNQQID
     NNSNKNIISK FIGDPWKNFY YGSNKSLWPF ERNNNSNNSS NNNNKVNFKQ AIWIFIFSVL
     FIGCLLGLFS TNFYGIHIYF PSFSTTKTNS PFNSTNNNIQ FSNLITKEQL YPIIDEYFKK
     NEILKSYNKL FEKIENDIKY LSEREQYKDI INEIKEELKL VKLSNMDEDR VNQLISKMIN
     HYNNNENNKQ ELKELLSKSI EELTKLKSDS KEQLIQISTE SMNQLGQLKS ESINQLGQVK
     SESIDKFQST LKSLSKEEQS KIEREFNHQF NQLNKDADQL LSQHSLKIEK LREEINENQQ
     SSLLKLTQEY KQLEERLKEF SSKLQQSISS SSMDQFESWK LVFIKDIEER INKESSKLTN
     QYIQLTQQFT KIQSFIKDNP SIDSLTNTIE SLEGIKLLIE DILEVYSADK IAKVDYALGL
     AGASIEYNAL HYRVSETYPP IKGSGSGSGS GGANGNSLGL YYYNLATNWI FPQPKPNPPE
     TILDPMVNTG SCWGFYTGNG TIVIRLAKKI AITEVTMEHI SSNISHHIDS APKEFQVFGL
     INSSDIGQSL GVFTYDTTIN RHLQTFKVNK IQSTTTTTTN QDQNDDDNIQ EFSHVALRIL
     SNHGYRYTCI YRFRVHGYQI PHPEQEQIQI IQEEQSFKQE EINQQQIEQI EQIEQIEKQQ
     QSDEL
 
 
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