ID   SDA1_RAT                Reviewed;         686 AA.
AC   Q5XIQ5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Protein SDA1 homolog;
DE   AltName: Full=SDA1 domain-containing protein 1;
GN   Name=Sdad1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584 AND SER-588, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Required for 60S pre-ribosomal subunits export to the
CC       cytoplasm. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SDA1 family. {ECO:0000305}.
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DR   EMBL; BC083620; AAH83620.1; -; mRNA.
DR   RefSeq; NP_001006959.1; NM_001006958.1.
DR   AlphaFoldDB; Q5XIQ5; -.
DR   SMR; Q5XIQ5; -.
DR   BioGRID; 252940; 1.
DR   STRING; 10116.ENSRNOP00000035588; -.
DR   iPTMnet; Q5XIQ5; -.
DR   PhosphoSitePlus; Q5XIQ5; -.
DR   PaxDb; Q5XIQ5; -.
DR   PRIDE; Q5XIQ5; -.
DR   GeneID; 289504; -.
DR   KEGG; rno:289504; -.
DR   UCSC; RGD:1359112; rat.
DR   CTD; 55153; -.
DR   RGD; 1359112; Sdad1.
DR   VEuPathDB; HostDB:ENSRNOG00000022229; -.
DR   eggNOG; KOG2229; Eukaryota.
DR   HOGENOM; CLU_009161_3_1_1; -.
DR   InParanoid; Q5XIQ5; -.
DR   OMA; AMYKTYK; -.
DR   OrthoDB; 426305at2759; -.
DR   PhylomeDB; Q5XIQ5; -.
DR   TreeFam; TF105727; -.
DR   PRO; PR:Q5XIQ5; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000022229; Expressed in testis and 19 other tissues.
DR   Genevisible; Q5XIQ5; RN.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR027312; Sda1.
DR   InterPro; IPR007949; SDA1_dom.
DR   InterPro; IPR012977; Uncharacterised_NUC130/133_N.
DR   PANTHER; PTHR12730; PTHR12730; 1.
DR   Pfam; PF08158; NUC130_3NT; 1.
DR   Pfam; PF05285; SDA1; 2.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Nucleus; Phosphoprotein; Protein transport;
KW   Reference proteome; Ribosome biogenesis; Transport.
FT   CHAIN           1..686
FT                   /note="Protein SDA1 homolog"
FT                   /id="PRO_0000287484"
FT   REGION          484..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          254..315
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        486..508
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..631
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU7"
FT   MOD_RES         234
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU7"
FT   MOD_RES         236
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU7"
FT   MOD_RES         551
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU7"
FT   MOD_RES         584
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         588
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         594
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVU7"
SQ   SEQUENCE   686 AA;  79633 MW;  652CA930793C5B26 CRC64;
     MSGRNNNKLP SNLPQLQNLI KRDPPAYVEE FLQQYNHYKS NMEIFKLQPN KPSKELAELV
     MFMAQIGHCY PEHLSEFPQE LKDLLSYNHT VLDPDLRMTF CKALILLRNK NLINPSDLLE
     LFFELLRCRD KLLRKTLYTH IVTDIKNINA KHKNNKVNVV LQNFMYTMLR DSNATAAKMS
     LDVMIELYRR NIWNDAKTVN VITTACFSKI TKILVAALTF FLGKDEEEKQ DSDSESEDDG
     PTARDLLVQY ATGKKGSKNK KKLEKAMKVL KKQKKKKKPE VFNFSAIHLI HDPQDFAEKL
     LKQLESCKER FEVKMMLMNL ISRLVGIHEL FLFNFYPFVQ RFLQPHQREV TKILLFAAQA
     SHHLVPPEII QSLLLTVANN FVTDKNSGEV MTVGINAIKE ITARCPLAMT EELLQDLAQY
     KTHKDKNVMM SARTLIHLFR TLNPQMLQKK FRGKPTEASI EARIQEYGEL DAKDYIPGAE
     VLELEKEENT ENDEDGWESA SLSEEEEDGE WVDVHHSSDE EQQAVAKKLD SMPMEERKAK
     AAAVSTSRVL TQDDFQKIRM AQMKKEMDAA PGKAQKRKYL DMDSDEESRG ELLSLRDIER
     LHKKPKSDKE TRLATAMAGR TDRKEFVRKK TKINPFSSST NKEKKKQKNF MMMRYSQNVR
     SKTSRSFREK QLALRDALLK KRKRMK