SAD1_SCHPO
ID SAD1_SCHPO Reviewed; 514 AA.
AC Q09825; Q9UU40;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Spindle pole body-associated protein sad1;
GN Name=sad1; ORFNames=SPBC12D12.01, SPBC16H5.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7744953; DOI=10.1083/jcb.129.4.1033;
RA Hagan I., Yanagida M.;
RT "The product of the spindle formation gene sad1+ associates with the
RT fission yeast spindle pole body and is essential for viability.";
RL J. Cell Biol. 129:1033-1047(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-157.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11676915; DOI=10.1016/s0960-9822(01)00478-x;
RA Krapp A., Schmidt S., Cano E., Simanis V.;
RT "S. pombe cdc11p, together with sid4p, provides an anchor for septation
RT initiation network proteins on the spindle pole body.";
RL Curr. Biol. 11:1559-1568(2001).
RN [5]
RP INTERACTION WITH CDC31.
RX PubMed=12857865; DOI=10.1091/mbc.e02-10-0661;
RA Paoletti A., Bordes N., Haddad R., Schwartz C.L., Chang F., Bornens M.;
RT "Fission yeast cdc31p is a component of the half-bridge and controls SPB
RT duplication.";
RL Mol. Biol. Cell 14:2793-2808(2003).
RN [6]
RP FUNCTION, INTERACTION WITH BQT1, AND SUBCELLULAR LOCATION.
RX PubMed=16615890; DOI=10.1016/j.cell.2006.01.048;
RA Chikashige Y., Tsutsumi C., Yamane M., Okamasa K., Haraguchi T.,
RA Hiraoka Y.;
RT "Meiotic proteins bqt1 and bqt2 tether telomeres to form the bouquet
RT arrangement of chromosomes.";
RL Cell 125:59-69(2006).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Associates with the spindle pole body and maintains a
CC functional interface between the nuclear membrane and the microtubule
CC motor proteins. Involved in chromosome segregation during meiosis where
CC it associates with the telomeres. {ECO:0000269|PubMed:16615890}.
CC -!- SUBUNIT: Interacts with bqt1. The bqt1-bqt2-sad1 complex binds rap1.
CC Interacts also with cdc31. {ECO:0000269|PubMed:12857865,
CC ECO:0000269|PubMed:16615890}.
CC -!- INTERACTION:
CC Q09825; Q92358: bqt1; NbExp=4; IntAct=EBI-929731, EBI-929655;
CC Q09825; P87245: kms1; NbExp=5; IntAct=EBI-929731, EBI-1542265;
CC Q09825; O74843: sif1; NbExp=3; IntAct=EBI-929731, EBI-1542307;
CC Q09825; O94531: ufe1; NbExp=3; IntAct=EBI-929731, EBI-1542297;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body. Nucleus membrane; Single-pass membrane
CC protein.
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DR EMBL; X85105; CAA59426.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17899.1; -; Genomic_DNA.
DR EMBL; AB027829; BAA87133.1; -; Genomic_DNA.
DR PIR; A57280; A57280.
DR RefSeq; NP_595947.2; NM_001021855.3.
DR PDB; 6A6W; X-ray; 2.60 A; B=88-101.
DR PDBsum; 6A6W; -.
DR AlphaFoldDB; Q09825; -.
DR SMR; Q09825; -.
DR BioGRID; 276458; 57.
DR IntAct; Q09825; 33.
DR MINT; Q09825; -.
DR STRING; 4896.SPBC12D12.01.1; -.
DR iPTMnet; Q09825; -.
DR MaxQB; Q09825; -.
DR PaxDb; Q09825; -.
DR PRIDE; Q09825; -.
DR EnsemblFungi; SPBC12D12.01.1; SPBC12D12.01.1:pep; SPBC12D12.01.
DR GeneID; 2539914; -.
DR KEGG; spo:SPBC12D12.01; -.
DR PomBase; SPBC12D12.01; sad1.
DR VEuPathDB; FungiDB:SPBC12D12.01; -.
DR eggNOG; KOG2687; Eukaryota.
DR HOGENOM; CLU_537650_0_0_1; -.
DR InParanoid; Q09825; -.
DR OMA; NGAHPAW; -.
DR PhylomeDB; Q09825; -.
DR PRO; PR:Q09825; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0061497; C:inner plaque of mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; TAS:PomBase.
DR GO; GO:0031021; C:interphase microtubule organizing center; IDA:PomBase.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IPI:PomBase.
DR GO; GO:0090619; C:meiotic spindle pole; EXP:PomBase.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0071958; C:new mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0071957; C:old mitotic spindle pole body; IDA:PomBase.
DR GO; GO:1990612; C:Sad1-Kms1 LINC complex; EXP:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0106166; F:spindle pole body-nuclear membrane anchor activity; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0072766; P:centromere clustering at the mitotic interphase nuclear envelope; IMP:PomBase.
DR GO; GO:0032121; P:meiotic attachment of telomeric heterochromatin to spindle pole body; IPI:PomBase.
DR GO; GO:0140480; P:mitotic spindle pole body insertion into the nuclear envelope; IMP:PomBase.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR InterPro; IPR045119; SUN1-5.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911; PTHR12911; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Membrane;
KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..514
FT /note="Spindle pole body-associated protein sad1"
FT /id="PRO_0000218915"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 322..488
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphoserine; by CDC2"
FT /evidence="ECO:0000255"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:6A6W"
SQ SEQUENCE 514 AA; 58077 MW; DCA4CAC1E1F98F0D CRC64;
MFTNTPVGGK RERQNGAHPA WSTLGANSAQ IHQNTADLAS KMHKLRYTKI RSPPTRVSIE
SITPKQRFPA PNFEQAYHSN IRYEQEESDN EEFENVVKNG HEASTNVFYE SDGDDEEFVN
EEYENSIDEE SDDEGYSLNE DTTATNASFR YPMNQRSTRK SQFYSSKFKP LLWFGITLFS
TLLIITLLHK GQEFYSRSFS SDNSQPSNSP VPNIPPASND TKTSLKPDII KDFTDSPSKV
GGNEEFDYST GDLITKKEFD KILQQKVEQL KQSLKEEMSN YKSSVPFEVE LNDDWKFFIE
STVRKYLTDP VSMPNFALLS TGAEVLPALT SKRYVRRPSA FIPRFTSYFF DSLVVRGHEP
SIALTPNNAV AMCWSFQGSE GQLGISLSRP VYVTNVTIEH VQHKIAHDLS SAPKDFELWV
QGMSSKMFVL LGKARYSLTE DSIQTFSFES SNYIVAEPIQ NVILKIKSNW GNPNYTCLYQ
VRVHGTVPNA DEQPIPSLGE KAESTAENTG QDSS
