ID   SRTD3_HUMAN             Reviewed;         196 AA.
AC   Q9UJW9; B3KQB3; Q96CQ2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=SERTA domain-containing protein 3;
DE   AltName: Full=Replication protein-binding trans-activator;
DE            Short=RPA-binding trans-activator;
GN   Name=SERTAD3; Synonyms=RBT1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH RPA2.
RX   PubMed=10982866; DOI=10.1093/nar/28.18.3478;
RA   Cho J.M., Song D.J., Bergeron J., Benlimame N., Wold M.S.,
RA   Alaoui-Jamali M.A.;
RT   "RBT1, a novel transcriptional co-activator, binds the second subunit of
RT   replication protein A.";
RL   Nucleic Acids Res. 28:3478-3485(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary, and Uterus;
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   [5]
RP   FUNCTION, INDUCTION BY TYPE I INTERFERON, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH INFLUENZA VIRUS PROTEINS PA; PB1 AND PB2 (MICROBIAL
RP   INFECTION).
RX   PubMed=33147462; DOI=10.1016/j.celrep.2020.108342;
RA   Sun N., Li C., Li X.F., Deng Y.Q., Jiang T., Zhang N.N., Zu S., Zhang R.R.,
RA   Li L., Chen X., Liu P., Gold S., Lu N., Du P., Wang J., Qin C.F., Cheng G.;
RT   "Type-IInterferon-Inducible SERTAD3 Inhibits Influenza A Virus Replication
RT   by Blocking the Assembly of Viral RNA Polymerase Complex.";
RL   Cell Rep. 33:108342-108342(2020).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZIKA VIRUS CAPSID PROTEIN
RP   (MICROBIAL INFECTION), AND INDUCTION BY ZIKA VIRUS INFECTION.
RX   PubMed=36594413; DOI=10.1002/jmv.28451;
RA   Sun N., Zhang R.R., Song G.Y., Cai Q., Aliyari S.R., Nielsen-Saines K.,
RA   Jung J.U., Yang H., Cheng G., Qin C.F.;
RT   "SERTAD3 induces proteasomal degradation of ZIKV capsid protein and
RT   represents a therapeutic target.";
RL   J. Med. Virol. 0:0-0(2023).
CC   -!- FUNCTION: Antiviral interferon-stimulated protein that plays a role in
CC       innate immunity and in the suppression of viruses through different
CC       mechanisms (PubMed:33147462, PubMed:36594413). Plays a role in the late
CC       phase response of TLR-induced immune effector expression (By
CC       similarity). During influenza infection, interacts with PB2, PB1, and
CC       PA to disrupt the formation of the viral RdRp complex
CC       (PubMed:33147462). Inhibits zika virus by interacting with the capsid
CC       protein in the nucleolus and reducing its abundance through proteasomal
CC       degradation (PubMed:36594413). Strong transcriptional coactivator
CC       (PubMed:10982866). {ECO:0000250|UniProtKB:Q9ERC3,
CC       ECO:0000269|PubMed:10982866, ECO:0000269|PubMed:33147462,
CC       ECO:0000269|PubMed:36594413}.
CC   -!- SUBUNIT: Interacts with RPA2. {ECO:0000269|PubMed:10982866}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with influenza virus PA, PB1
CC       and PB2,leading to inhibition of RdRp complex assembly.
CC       {ECO:0000269|PubMed:33147462}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with zika virus capsid
CC       protein. {ECO:0000269|PubMed:36594413}.
CC   -!- INTERACTION:
CC       Q9UJW9; X5D778: ANKRD11; NbExp=3; IntAct=EBI-748621, EBI-17183751;
CC       Q9UJW9; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-748621, EBI-745073;
CC       Q9UJW9; Q13515: BFSP2; NbExp=3; IntAct=EBI-748621, EBI-10229433;
CC       Q9UJW9; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-748621, EBI-747505;
CC       Q9UJW9; P24863: CCNC; NbExp=3; IntAct=EBI-748621, EBI-395261;
CC       Q9UJW9; Q6IPU0: CENPP; NbExp=3; IntAct=EBI-748621, EBI-10250303;
CC       Q9UJW9; Q96LK0: CEP19; NbExp=3; IntAct=EBI-748621, EBI-741885;
CC       Q9UJW9; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-748621, EBI-11962928;
CC       Q9UJW9; Q9UBT7: CTNNAL1; NbExp=3; IntAct=EBI-748621, EBI-514206;
CC       Q9UJW9; Q9UER7: DAXX; NbExp=3; IntAct=EBI-748621, EBI-77321;
CC       Q9UJW9; Q6W0C5: DPPA3; NbExp=3; IntAct=EBI-748621, EBI-12082590;
CC       Q9UJW9; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-748621, EBI-744099;
CC       Q9UJW9; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-748621, EBI-12013806;
CC       Q9UJW9; Q9H4M3: FBXO44; NbExp=3; IntAct=EBI-748621, EBI-2322644;
CC       Q9UJW9; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-748621, EBI-11958845;
CC       Q9UJW9; Q969Y2: GTPBP3; NbExp=3; IntAct=EBI-748621, EBI-740290;
CC       Q9UJW9; Q9Y5R4: HEMK1; NbExp=3; IntAct=EBI-748621, EBI-10329202;
CC       Q9UJW9; O14964: HGS; NbExp=3; IntAct=EBI-748621, EBI-740220;
CC       Q9UJW9; Q14005-2: IL16; NbExp=3; IntAct=EBI-748621, EBI-17178971;
CC       Q9UJW9; Q9NV31: IMP3; NbExp=3; IntAct=EBI-748621, EBI-747481;
CC       Q9UJW9; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-748621, EBI-2556193;
CC       Q9UJW9; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-748621, EBI-739890;
CC       Q9UJW9; P52292: KPNA2; NbExp=4; IntAct=EBI-748621, EBI-349938;
CC       Q9UJW9; O95983-2: MBD3; NbExp=3; IntAct=EBI-748621, EBI-11978579;
CC       Q9UJW9; Q71SY5: MED25; NbExp=3; IntAct=EBI-748621, EBI-394558;
CC       Q9UJW9; A6NI15: MSGN1; NbExp=3; IntAct=EBI-748621, EBI-11991020;
CC       Q9UJW9; P16860: NPPB; NbExp=3; IntAct=EBI-748621, EBI-747044;
CC       Q9UJW9; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-748621, EBI-741048;
CC       Q9UJW9; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-748621, EBI-10181968;
CC       Q9UJW9; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-748621, EBI-79165;
CC       Q9UJW9; Q16512: PKN1; NbExp=3; IntAct=EBI-748621, EBI-602382;
CC       Q9UJW9; P54646: PRKAA2; NbExp=3; IntAct=EBI-748621, EBI-1383852;
CC       Q9UJW9; P15927: RPA2; NbExp=5; IntAct=EBI-748621, EBI-621404;
CC       Q9UJW9; Q14D33: RTP5; NbExp=3; IntAct=EBI-748621, EBI-10217913;
CC       Q9UJW9; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-748621, EBI-358489;
CC       Q9UJW9; P14678-2: SNRPB; NbExp=4; IntAct=EBI-748621, EBI-372475;
CC       Q9UJW9; Q96JI7: SPG11; NbExp=3; IntAct=EBI-748621, EBI-2822128;
CC       Q9UJW9; Q6ZRS2-3: SRCAP; NbExp=3; IntAct=EBI-748621, EBI-12029182;
CC       Q9UJW9; P51687: SUOX; NbExp=5; IntAct=EBI-748621, EBI-3921347;
CC       Q9UJW9; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-748621, EBI-745958;
CC       Q9UJW9; Q08117-2: TLE5; NbExp=3; IntAct=EBI-748621, EBI-11741437;
CC       Q9UJW9; O14787-2: TNPO2; NbExp=3; IntAct=EBI-748621, EBI-12076664;
CC       Q9UJW9; Q8N7U7-2: TPRX1; NbExp=3; IntAct=EBI-748621, EBI-14115717;
CC       Q9UJW9; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-748621, EBI-8451480;
CC       Q9UJW9; Q9BSJ2: TUBGCP2; NbExp=3; IntAct=EBI-748621, EBI-357881;
CC       Q9UJW9; P10599: TXN; NbExp=3; IntAct=EBI-748621, EBI-594644;
CC       Q9UJW9; Q9BZL1: UBL5; NbExp=4; IntAct=EBI-748621, EBI-607755;
CC       Q9UJW9; Q8N6Y0: USHBP1; NbExp=7; IntAct=EBI-748621, EBI-739895;
CC       Q9UJW9; Q96DA0: ZG16B; NbExp=5; IntAct=EBI-748621, EBI-953824;
CC       Q9UJW9; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-748621, EBI-10183064;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10982866}.
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DR   EMBL; AF192529; AAF05761.1; -; mRNA.
DR   EMBL; AK074604; BAG51975.1; -; mRNA.
DR   EMBL; CH471126; EAW56966.1; -; Genomic_DNA.
DR   EMBL; BC014061; AAH14061.1; -; mRNA.
DR   EMBL; BC050643; AAH50643.1; -; mRNA.
DR   CCDS; CCDS12558.1; -.
DR   RefSeq; NP_037500.2; NM_013368.3.
DR   RefSeq; NP_976219.1; NM_203344.2.
DR   RefSeq; XP_005258889.1; XM_005258832.3.
DR   RefSeq; XP_006723242.1; XM_006723179.3.
DR   AlphaFoldDB; Q9UJW9; -.
DR   BioGRID; 118983; 47.
DR   IntAct; Q9UJW9; 68.
DR   STRING; 9606.ENSP00000375882; -.
DR   iPTMnet; Q9UJW9; -.
DR   PhosphoSitePlus; Q9UJW9; -.
DR   BioMuta; SERTAD3; -.
DR   DMDM; 60415943; -.
DR   EPD; Q9UJW9; -.
DR   PaxDb; 9606-ENSP00000325414; -.
DR   PeptideAtlas; Q9UJW9; -.
DR   Antibodypedia; 55379; 60 antibodies from 16 providers.
DR   DNASU; 29946; -.
DR   Ensembl; ENST00000322354.4; ENSP00000325414.2; ENSG00000167565.13.
DR   Ensembl; ENST00000392028.8; ENSP00000375882.3; ENSG00000167565.13.
DR   GeneID; 29946; -.
DR   KEGG; hsa:29946; -.
DR   MANE-Select; ENST00000322354.4; ENSP00000325414.2; NM_203344.3; NP_976219.1.
DR   UCSC; uc002onu.5; human.
DR   AGR; HGNC:17931; -.
DR   CTD; 29946; -.
DR   DisGeNET; 29946; -.
DR   GeneCards; SERTAD3; -.
DR   HGNC; HGNC:17931; SERTAD3.
DR   HPA; ENSG00000167565; Low tissue specificity.
DR   MIM; 612125; gene.
DR   neXtProt; NX_Q9UJW9; -.
DR   OpenTargets; ENSG00000167565; -.
DR   PharmGKB; PA134941720; -.
DR   VEuPathDB; HostDB:ENSG00000167565; -.
DR   eggNOG; ENOG502RY30; Eukaryota.
DR   GeneTree; ENSGT00940000154733; -.
DR   HOGENOM; CLU_097197_0_0_1; -.
DR   InParanoid; Q9UJW9; -.
DR   OMA; PGPQNEV; -.
DR   OrthoDB; 4603198at2759; -.
DR   PhylomeDB; Q9UJW9; -.
DR   TreeFam; TF101069; -.
DR   PathwayCommons; Q9UJW9; -.
DR   SignaLink; Q9UJW9; -.
DR   BioGRID-ORCS; 29946; 16 hits in 1164 CRISPR screens.
DR   GenomeRNAi; 29946; -.
DR   Pharos; Q9UJW9; Tbio.
DR   PRO; PR:Q9UJW9; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9UJW9; Protein.
DR   Bgee; ENSG00000167565; Expressed in oocyte and 154 other cell types or tissues.
DR   ExpressionAtlas; Q9UJW9; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; IDA:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB.
DR   InterPro; IPR009263; SERTA_dom.
DR   InterPro; IPR039585; SERTAD3.
DR   PANTHER; PTHR15530; SERTA DOMAIN-CONTAINING PROTEIN 3; 1.
DR   PANTHER; PTHR15530:SF0; SERTA DOMAIN-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF06031; SERTA; 1.
DR   PROSITE; PS51053; SERTA; 1.
DR   Genevisible; Q9UJW9; HS.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..196
FT                   /note="SERTA domain-containing protein 3"
FT                   /id="PRO_0000191615"
FT   DOMAIN          26..73
FT                   /note="SERTA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00396"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        2
FT                   /note="V -> E (in Ref. 1; AAF05761)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   196 AA;  21769 MW;  9C54AFA126F17AF1 CRC64;
     MVGGLKRKHS DLEEEEERWE WSPAGLQSYQ QALLRISLDK VQRSLGPRAP SLRRHVLIHN
     TLQQLQAALR LAPAPALPPE PLFLGEEDFS LSATIGSILR ELDTSMDGTE PPQNPVTPLG
     LQNEVPPQPD PVFLEALSSR YLGDSGLDDF FLDIDTSAVE KEPARAPPEP PHNLFCAPGS
     WEWNELDHIM EIILGS
//